Vinci-Biochem S.r.l.
Via Ponte di Bagnolo, 10
50059 Vinci (Firenze)
Tel. +39 0571 568 147
vb@vincibiochem.it
www.vincibiochem.it
| Sample Preparation | |||||
| Mitochondrial Fractionation Kit | 100 rxns | V13-40015 | data sheet | ||
| Mitochondria/Cytosol Fractionation Kit | 25 assays | BVN-K256-25 | page | data sheet | The Mitochondria/Cytosol Fractionation Kit provides unique formulations of reagents for effective isolation of a highly enriched mitochondrial fraction from cytosolic fraction of mammalian cells including both apoptotic and nonapoptotic cells. The enriched mitochondrial and cytosolic fractions can be used for studying apoptotic and signal transduction pathways to detect translocation of factors interested between the two fractions by Western blotting, ELISA, or other assays. Procedures are simple and easy to perform, no ultracentrifugations and toxic chemicals are involved. |
| Mitochondria/Cytosol Fractionation Kit | 100 assays | BVN-K256-100 | page | data sheet | The Mitochondria/Cytosol Fractionation Kit provides unique formulations of reagents for effective isolation of a highly enriched mitochondrial fraction from cytosolic fraction of mammalian cells including both apoptotic and nonapoptotic cells. The enriched mitochondrial and cytosolic fractions can be used for studying apoptotic and signal transduction pathways to detect translocation of factors interested between the two fractions by Western blotting, ELISA, or other assays. Procedures are simple and easy to perform, no ultracentrifugations and toxic chemicals are involved. |
| Mitochondrial DNA Isolation Kit | 50 assays | BVN-K280-50 | page | data sheet | Mitochondria are semiautonomous organelles which functions in aging process, apoptosis, anti-HIV drugs, and cancers. Mitochondrial DNA (mtDNA) has a very high mutation rate and the mutations on mtDNA appear to be related to certain diseases such as diabetes, Alzheimer’s disease, and muscle disorders. Isolation and quantification of mtDNA are often required to study the relationships between the diseases and mtDNA. The Mitochondrial DNA Extraction Kit provides convenient tools for isolating mtDNA from a variety of cells and tissues in high yield and purity, without contaminations from genomic DNA. The purified mtDNA can be used for a variety of studies such as enzyme manipulations, Southern blotting, cloning, PCR analysis, and amplifications. |
| Mitochondrial Protein IP Kit | 50 assays | BVN-K285-50 | page | data sheet |
Mitochondria are the power house of the cells
and play an essential role in energy production.
Damage to the mitochondria activates signaling
pathways that induce apoptosis. Mitochondria
also regulate and mediate transport of the
metabolites and ions needed for oxidative
phosphorylation and maintenance of membrane
potential for ATP synthesis. Mitochondrial
dysfunction leads to several disorders like
cardiac dysfunction, diabetes, aging and
neurological disorder, mainly caused by
mutations in mitochondrial DNA or in nuclear
genes that code for mitochondrial components.
Thus, mitochondria have several different
functions in the cell. BioVision ready to use mitochondria Protein IP Buffer is optimized for immunoprecipitation (IP and co-IP) using mitochondria and mitochondrial extracts. The buffer is a gentle formulation, which maintains the stability of mitochondrial complexes. The Mitochondrial Protein IP kit is provided with different choices of detergents like n-Dodecyl-beta-D-maltoside, Triton X-100 and digitonin to achieve different stringency conditions for protein-protein interaction studies. Triton X-100 is the most commonly used detergent especially for membrane protein solubilization. However, in case of fragile complexes digitonin or n-Dodecyl-beta-D-maltoside is the choice of detergents. |
| MitoCheck Mitochondrial (Tissue) Isolation Kit | 1 ea | CAY-701010-1 | page | data sheet | When measuring mitochondrial function or the effects of an unknown on mitochondrial function, it can be difficult to determine a mechanism using whole organisms or tissue. When this is the case, isolated mitochondria provide a simple and biochemically relevant experimental model. Cayman's MitoCheck Mitochondrial (Tissue) Isolation Kit includes a complete package of reagents and step-by-step instructions for isolating coupled mitochondria* from freshly harvested mammalian heart, liver, or kidney tissue through a process of differential centrifugation in isotonic buffers. *Coupled mitochondria are defined as mitochondria capable of phosphorylating ADP at the F1FO-ATP synthase (Complex V) through the utilization of a proton (H+) gradient, which is generated by the electron transport chain (ETC) in the presence of appropriate substrates (e.g., succinate) and in the absence of uncouplers and mitochondrial inhibitors. |
| Yeast Mitochondria Isolation Kit | 50 assays | BVN-K259-50 | page | data sheet |
Mitochondria are the power house of the cells
because they generate most of the supply of
energy in the form of adenosine tri-phosphate
(ATP). Mitochondria are double membrane
organelles: an outer membrane and a folded inner
membrane called cristae. Isolated mitochondria
is a useful tool to study mitochondrial
respiration, assembly of the respiratory
complexes, apoptosis, mtDNA and mtRNA, and for
protein profiling. BioVision’s Yeast
Mitochondria Isolation kit will enable fast and
easy purification of mitochondria from yeast
cells, utilizing yeast cell wall lysis and
homogenization. This Mitochondria Isolation Kit is tested for Pichia pastoris & Saccharomyces cerevisiae & can be used to isolate mitochondria from other yeast. Under fermentable media, the yield is ~150-200 µg of mitochondria & under non-fermentable media (e.g. Glycerol) ~200-250 µg of mitochondria from a culture of OD ~20. |
| ELISAs, Assays Kits & Sets | |||||
| Acetoacetate Colorimetric Assay Kit | 100 assays | BVN-K650-100 | page | data sheet | Acetoacetate (AcAc), a β-ketoacid, is one of the three ketone bodies and is formed via condensation of two molecules of acetyl-CoA in liver mitochondria. AcAc can be enzymatically reduced to 3-β-hydroxybutyrate (β-HB), or decarboxylated producing acetone (CH3)2CO). Ketone bodies (βHB: 78%; AcAc: 20% & CH3)2CO: 2%) are mainly used as an alternative energy source when glucose cannot be delivered to the system. Excessive concentration of ketone bodies (ketoacidosis) is observed in patients with Type I diabetes, severe starvation or alcoholism. Traditionally, AcAc levels have been qualitatively detected using dipsticks that use sodium nitroferricyanide as a chromophore. BioVision’s Acetoacetate Assay Kit has adapted that principle with a modification that provides a sensitive method to quantitate endogenous levels of AcAc in human blood, and urine. In this non-enzymatic assay, AcAc reacts with a substrate to generate a colored product that can be measured at 550 nm. The reaction is specific for AcAc and does not detect 3-β-hydroxybutyrate. The assay kit can detect samples containing acetoacetate as low as 25 µM. |
| Aconitase Activity Colorimetric Assay Kit | 100 assays | BVN-K716-100 | data sheet | Aconitase (aconitate hydratase; EC 4.2.1.3) is an iron-sulfur protein containing an [Fe₄S₄]²ᶧ cluster that catalyzes the stereospecific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle, a non-redox-active process. Tissue contains two aconitases, a mitochondrial (m-) and a cytosolic (c-) aconitase. They are related, but distinctly different enzymes and are coded for on different chromosomes. Loss of aconitase activity in cells or other biological samples treated with pro-oxidants has been interpreted as a measure of oxidative damage. BioVision’s Aconitase Assay Kit is a highly sensitive, simple, direct and HTS-ready colorimetric assay for measuring Aconitase activity in biological samples. In the assay, citrate is converted by aconitase into isocitrate, which is further processed resulting in a product that converts a nearly colorless probe into an intensely colored form with a λmax at 450nm. | |
| ADP Colorimetric Assay Kit II | 100 assays | BVN-K356-100 | data sheet | ADP is a product of ATP dephosphorylation and it can be rephosphorylated to ATP. Dephosphorylation and rephosphorylation occur via various phosphorylases and kinases. ADP is stored in platelets and can be released to interact with variety of purinergic receptors. ADP levels regulate several enzymes involved in intermediary metabolism. ADP conversion to ATP primarily occurs within the mitochondrion and chloroplast although several such processes occur in the cytoplasm. Conventionally, ADP levels are measured by luciferase/luciferin mediated assays after ADP is converted to ATP. However, the luciferase system is unstable and luminescence equipment is not generally available in most laboratories. BioVision ADP Assay kit II is suitable for measuring ADP levels in samples that contain reducing substances, which may interfere with oxidase-based assays. In this assay, ADP in the presence of ADP Enzyme Mix is converted to an intermediate, which reduces a colorless Probe to a colored product with strong absorbance at 450 nm. ADP Assay Kit II is simple, fast and high-throughput ready. It can detect less than 20 μM of ADP in samples. | |
| ADP Colorimetric/Fluorometric Assay Kit | 100 assays | BVN-K355-100 | data sheet | ADP is a product of ATP dephosphorylation and it can be rephosphorylated to ATP. De-phosphorylation and rephosphorylation occur via various phosphatases, phosphorylases and kinases. ADP is stored in platelets and can be released to interact with a variety of purinergic receptors. ADP levels regulate several enzymes involved in intermediary metabolism. ADP conversion to ATP primarily occurs within the mitochondrion and chloroplast although several such processes occur in the cytoplasm. Conventionally, ADP levels are measured by luciferase/luciferin mediated assays after ADP is converted to ATP. However, the luciferase system is unstable and luminescence equipment is not generally available in most laboratories. BioVision’s newly designed ADP Assay Kit provides a convenient colorimetric and fluorometric means to measure ADP level. In the assay, ADP is converted to ATP and pyruvate. The generated pyruvate can be quantified by colorimetric (λmax = 570 nm) or fluorometric method (Ex/Em 535/587 nm). The assay is simple, sensitive, stable and high-throughput adaptable. The assay can detect as low as 1 µM ADP in biological samples. | |
| Mitochondrial Apoptosis Detection Fluorometric Kit, MitoCapture | 25 assays | BVN-K250-25 | data sheet | Disruption of the mitochondrial transmembrane potential is one of the earliest intracellular events that occur following induction of apoptosis. The MitoCapture™ Apoptosis Detection Kit provides a simple, fluorescent-based method for distinguishing between healthy and apoptotic cells by detecting the changes in the mitochondrial transmembrane potential. The kit utilizes MitoCapture™, a cationic dye that fluoresces differently in healthy vs apoptotic cells. In healthy cells, MitoCapture accumulates and aggregates in the mitocondria, giving off a bright red fluorescence. In apoptotic cells, MitoCapture cannot aggregate in the mitochondria due to the altered mitochondrial transmembrane potential, and thus it remains in the cytoplasm in its monomer form, fluorescing green. The fluorescent signals can be easily detected by fluorescence microscopy using a band-pass filter (detects FITC and rhodamine) or analyzed by flow cytometry using FITC channel for green monomers (Ex/Em = 488/530+ 30 nm) and (optional) PI channel for red aggregates (Em = 488/590+ 42 nm). | |
| Mitochondrial Apoptosis Detection Fluorometric Kit, MitoCapture | 100 assays | BVN-K250-100 | data sheet | Disruption of the mitochondrial transmembrane potential is one of the earliest intracellular events that occur following induction of apoptosis. The MitoCapture™ Apoptosis Detection Kit provides a simple, fluorescent-based method for distinguishing between healthy and apoptotic cells by detecting the changes in the mitochondrial transmembrane potential. The kit utilizes MitoCapture™, a cationic dye that fluoresces differently in healthy vs apoptotic cells. In healthy cells, MitoCapture accumulates and aggregates in the mitocondria, giving off a bright red fluorescence. In apoptotic cells, MitoCapture cannot aggregate in the mitochondria due to the altered mitochondrial transmembrane potential, and thus it remains in the cytoplasm in its monomer form, fluorescing green. The fluorescent signals can be easily detected by fluorescence microscopy using a band-pass filter (detects FITC and rhodamine) or analyzed by flow cytometry using FITC channel for green monomers (Ex/Em = 488/530+ 30 nm) and (optional) PI channel for red aggregates (Em = 488/590+ 42 nm). | |
| ATP Colorimetric/Fluorometric Assay Kit | 100 assays | BVN-K354-100 | page | data sheet | ATP is the primary energy currency of living systems. Virtually all energy requiring processes utilize the chemical energy stored in the phosphate bond of ATP. ATP is formed exclusively in the mitochondria and a variety of genetic diseases can affect ATP formation in the mitochondria. There are a number of commercially available ATP assays which detects femtomoles or less of ATP by measuring luminescence (BioVision Kit 254-200, for example) but these kits require specialized luminescence instrumentation and utilize luciferase which can be difficult to maintain in active form. BioVision newly developed ATP Colorimetric and Fluorometric Assay kit is designed to be a robust, simple method which utilizes the phosphorylation of glycerol to generate a product that is easily quantified by colorimetric (λmax = 570 nm) or fluorometric (Ex/Em = 535/587 nm) methods. The assay can detect as low as 50 picomol (1 µM) of ATP in various samples. The kit provides sufficient reagents for 100 assays. |
| L-Carnitine Colorimetric/Fluorometric Assay Kit | 100 assays | BVN-K642-100 | data sheet | Carnitine is a quaternary ammonium compound biosynthesized from the amino acids lysine and methionine. It is required for transport of fatty acids into the mitochondrial matrix via the carnitine/acylcarnitine shuttle where β-oxidation occurs, acetate is generated and the acetate utilized in the TCA cycle for the generation of energy. L-Carnitine is often sold as a nutritional supplement. Carnitine exists in two stereoisomers. Only L-carnitine is biologically active. BioVision's L-Carnitine Assay Kit is a simple convenient means of measuring free L-Carnitine in biological samples such as serum. The assay transfers an acetyl group from CoA to carnitine and the free CoA formed is further processed with subsequent oxidation of the Oxi-Red probe to give fluorescence (Ex/Em 535 nm 587 nm) and absorbance (570 nm). The normal range for serum L-Carnitine is ~20-100 µM. The detection sensitivity is ~1 µM for the fluorometric assay and ~10 µM for the colorimetric assay. | |
| Chromeo™ Live Cell Mitochondrial Staining Kit | 1 kit | V13-15005 | data sheet | ||
| Citrate Colorimetric/Fluorometric Assay Kit | 100 assays | BVN-K655-100 | page | data sheet | Citric acid (HOOC-CH₂-C(-OH)(-COOH)-CH₂-COOH) is a key intermediate in the TCA cycle which occurs in mitochondria. It is formed by the addition of oxaloacetate to the acetyl group of acetyl-CoA derived from the glycolytic pathway. Citrate can be transported out of mitochondria and converted back to acetyl CoA for fatty acid synthesis. Citrate is an allosteric modulator of both fatty acid synthesis (acetyl-CoA carboxylase) and glycolysis (phospho- fructokinase). Citrate is widely used industrially in foods, beverages and pharmaceuticals. Citrate metabolism and disposition can vary widely due to sex, age and a variety of other factors. BioVision's Citrate Assay Kit provides a simple, sensitive and rapid means of quantifying citrate in a variety of samples. In the assay, citrate is converted to pyruvate via oxaloacetate. The pyruvate is quantified by converting a nearly colorless probe to an intensely colored (570 nm) and fluorescent (Ex/Em, 535/587 nm) product. The Citrate Assay Kit can detect 0.1 to 10 nmoles (~2 µM-10 mM) of citrate in a variety of samples. |
| Citrate Synthase Activity Colorimetric Assay Kit | 100 assays | BVN-K318-100 | page | data sheet | Citrate Synthase (EC 2.3.3.1) is a key enzyme that is present in all living organisms. It catalyzes the conversion of acetyl-CoA and oxaloacetate into citrate and serves as a marker for intact mitochondria. A recent study showed that increased activity of mitochondrial Citrate Synthase is directly associated with metabolic and endocrine abnormalities such as obesity. In BioVision’s Citrate Synthase Activity Assay Kit, Citrate Synthase reacts with substrate mix to form an intermediate, which subsequently reacts with developer to generate the colored product. The rate of color development is proportional to the enzyme activity. The assay is simple, rapid and can detect Citrate Synthase activity less than 1 mU in a variety of samples. |
| CTRP5 (human) Competitive ELISA Kit | 96 wells | AG-45A-0031EK-KI01 | page | data sheet | Assay Type: Competitive. Detection Type: Colorimetric. Sample Type: Cell Culture Supernatant , Plasma , Serum. Range: 0.001 to 5µg/ml. Sensitivity: 1ng/ml. AN1103 CTRP5 (C1qTNF-related protein 5; C1QTNF5) belongs to a highly conserved family of adiponectin paralogs. CTRP5 mediates activation of AMP-activated protein kinase (AMPK) in muscle and liver cells, thereby regulating glucose and lipid metabolism. Serum levels of CTRP5 are significantly higher in obese/diabetic animal models compared to normal controls. Furthermore, CTRP5 may be a putative biomarker for mitochondrial dysfunction. |
| CTRP5 (human) Competitive ELISA Kit | 100 assays | BVN-K4925-100 | page | data sheet | CTRP5, a 25 kD secretory protein, is a member of the C1q and tumor necrosis factor superfamily whose structure resembles adiponectin. A RT-PCR study demonstrated CTRP5 expression in RPE, liver, lung, placenta, and brain and it has been proposed that a CTRP mutation (S163R) plays a critical role in affecting its higher order protein structure, potentially leading to a cause of abnormal adhesion between the RPE and Bruch membrane. Recent data indicates that CTRP is one of the genes highly induced by elimination of mitochondria and able to activate AMPK in a rat myotube cell line, L6. Stimulation of L6 with recombinant CTRP5, full length as well as globular domain, enhanced glucose uptake and fatty acid oxidation. These biochemical events did not seem to be mediated via AdipoR1 or AdipoR2, suggesting that a novel receptor(s) may exist for CTRP5 in this muscle cell line. Some CTRP members can physically interact with adiponectin, forming various multimeric structures. Therefore, measuring serum or plasma CTRP5 may provide important information on its involvement in novel metabolism. This assay is a competitive Enzyme Linked-Immunosorbent Assay (ELISA) for quantitative determination of human CTRP5 in biological fluids. A polyclonal antibody recognizing native human CTRP5 reacts with a series of predetermined recombinant human CTRP5 standard proteins or samples under competition in the human CTRP5-coated plate. Their relative reactivity is plotted with that of the standard proteins. This ELISA is specific for the measurement of natural and recombinant human CTRP5. It does not cross-react with mouse CTRP5, human CTRP2 (globular), human CTRP6, human CTRP7 (globular), human CTRP9 (globular), human CTRP10 (globular), mouse CTRP2 (globular), mouse CTRP9 (globular), human adiponectin, human adiponectin (globular), mouse adiponectin, mouse adiponectin (globular), rat adiponectin, rat adiponectin (globular), human RBP4, human Nampt, human vaspin, human GPX3, human ANGPTL3, human progranulin, human leptin. The assay range is 0.001 – 5 µg CTRP5/ml and a detection limit of 1 ng/ml (based on adding two standard deviations to the mean value of the (50) zero standards). |
| CTRP5 (human) Competitive ELISA Kit (Twin Plex) | 2 x 96 wells | AG-45A-0031TP-KI01 | page | data sheet | Assay Type: Competitive. Detection Type: Colorimetric. Sample Type: Cell Culture Supernatant , Plasma , Serum. Range: 0.001 to 5µg/ml. Sensitivity: 1ng/ml. AN1103 CTRP5 (C1qTNF-related protein 5; C1QTNF5) belongs to a highly conserved family of adiponectin paralogs. CTRP5 mediates activation of AMP-activated protein kinase (AMPK) in muscle and liver cells, thereby regulating glucose and lipid metabolism. Serum levels of CTRP5 are significantly higher in obese/diabetic animal models compared to normal controls. Furthermore, CTRP5 may be a putative biomarker for mitochondrial dysfunction. |
| Cytochrome c Releasing Apoptosis Assay Kit | 100 assays | BVN-K257-100 | page | data sheet | Cytochrome c plays an important role in apoptosis. The protein is located in the space between the inner and outer mitochondrial membranes. An apoptotic stimulus triggers the release of cytochrome c from the mitochondria into cytosol where it binds to Apaf-1. The cytochrome c/Apaf-1 complex activates caspase-9, which then activates caspase-3 and other downstream caspases. BioVision’s Cytochrome c Releasing Apoptosis Assay Kit provides an effective means for detecting cytochrome c translocation from mitochondria into cytosol during apoptosis. The kit provides unique formulations of reagents to isolate a highly enriched mitochondria fraction from cytosol. The procedure is so simple and easy to perform, no ultracentrifugation is required and no toxic chemicals are involved. Cytochrome c releasing from mitochondria into cytosol is then determined by Western blotting using the cytochrome c antibody provided in the kit. |
| Cytochrome Oxidase Activity Colorimetric Assay Kit | 100 assays | BVN-K287-100 | page | data sheet |
Cytochrome c Oxidase (EC 1.9.3.1) or Complex IV
is the fourth complex of the Electron Transport
Chain located in the mitochondrial (or
bacterial) membrane. It provides energy to the
cell by coupling electron transport through the
Cytochrome c chain with the process of oxidative
phosphorylation. Complex IV contains 13
different subunits encoded by both mitochondrial
DNA and nuclear DNA. It receives an electron
from each of the four Cytochrome c molecules,
and transfers it to one oxygen molecule,
converting it into two molecules of water. In
this process, it also binds to four proton
molecules and translocates them across the
membrane to establish electrochemical gradient,
which is utilized for the synthesis of ATP.
Cytochrome Oxidase Activity Assay Kit is simple,
fast and high-throughput adaptable. This assay
kit can be used for purified mitochondria or
tissue extracts containing mitochondria. The
activity of the enzyme is determined
colorimetrically by following the oxidation of
reduced Cytochrome c as an absorbance decrease
at 550 nm. |
| Fumarase Activity Colorimetric Assay Kit | 100 assays | BVN-K596-100 | page | data sheet | Fumarase (Fumarate Hydratase: EC 4.2.1.2) is an enzyme that catalyzes the reversible reaction of hydration and dehydration of fumarate to Malate. It has two forms: mitochondrial and cytosolic forms. The mitochondrial form of fumarase is one of the key enzymes in citric acid cycle, while cytosolic form is important for metabolism of amino acids and fumarate. In humans, fumarase deficiency leads to serious health problems such as fetal brain abnormality, hypotonia, and renal cell carcinoma. Therefore, accurate measurement of fumarase activity is important for preventing, diagnosis and mechanistic study of fumarase deficiency. Biovision’s Fumarase Activity Assay kit provides a quick and easy method for monitoring fumarase activity in various samples. In this kit, fumarase converts fumarate into malate, which then reacts with Enzyme Mix to form an intermediate. The intermediate subsequently reduces the Developer to a colored product with strong absorbance at 450 nm. The assay is simple and high-throughput ready and can detect less than 50 U/ml of fumarase activity in variety of sample types. |
| GPX1 (human) ELISA Kit | 1x96T | YIF-LF-EK0110 | page | data sheet | Glutathione peroxidases (Gpxs) are ubiquitously expressed proteins which catalyze the reduction of hydrogen peroxides and organic hydroperoxides by glutathione. There are several isoforms which differ in their primary structure and localization. The classical cytosolic /mitochondrial GPx1 (cGPx) is a selenium-dependent enzyme, first of the GPx family to be discovered. GPx2, also known as gastrointestinal GPx (GI-GPx), is an intracellular enzyme expressed only at the epithelium of the gastrointestinal tract (1). Extracellular plasma GPx (pGPx or GPx3) is mainly expressed by the kidney from where it is released into the blood circulation (2). Phospholipid hydroperoxide GPx4 (PH-GPx) expressed in most tissues, can reduce many hydroperoxides including hydroperoxides integrated in membranes, hydroperoxy lipids in low density lipoprotein or thymine (3). All mammalian GPx family members, except for the recently described Cys containing GPx3 and epididymis-specific secretory GPx (eGPx or GPx5) isoforms, possess selenocysteine at the active site (4-5). |
| JC-1 Mitochondrial Membrane Potential Assay Kit | 100 tests | CAY-10009172-100 | page | data sheet | |
| Malate Dehydrogenase Activity Colorimetric Assay Kit | 100 assays | BVN-K654-100 | Malate Dehydrogenase (MDH) (EC 1.1.1.37) is an important enzyme which reversibly converts L-malate into oxaloacetate in the presence of NAD. In eukaryotic cells, malate dehydrogenase has 2 isoforms: MDH1 and MDH2. MDH1 is cytosolic & participates in the malate-aspartate shuttle, which transports malate into mitochondria for utilization in ATP generation whereas MDH2 is a mitochondrial enzyme and part of the citric acid cycle. MDH activity is increased in some neurodegenerative diseases such as Alzheimer’s disease, and abnormal MDH activity in serum can serve as a diagnostic tool for severe liver damage (e.g. Hepatocellular carcinoma). In BioVision’s Malate Dehydrogenase Activity Assay kit, MDH reacts with malate to form an intermediate. The generated intermediate reacts with MDH Developer to form a colored product with strong absorbance at 450 nm. The assay is simple, sensitive and can detect less than 0.5 mU of MDH activity in various sample types. | ||
| MitoCheck Citrate Synthase Activity Assay Kit | 96 wells | CAY-701040-96 | page | data sheet | The condensation of the dicarboxylate oxaloacetate and acetyl CoA to the tricarboxylate citrate is catalyzed by citrate synthase. It is within this reaction that carbon molecules (as acetyl CoA) obtained from pyruvate oxidation are fed into the tricarboxylic acid (TCA or citric acid) cycle. As a mitochondrial enzyme, citrate synthase is commonly used as a normalization factor for mitochondrial protein, but can also be used as a biomarker for mitochondrial content in a tissue homogenate. Cayman's MitoCheck Citrate Synthase Assay Kit allows for the simple and convenient determination of citrate synthase activity from isolated mitochondria or cell homogenates. This assay measures the production of SH-CoA by monitoring the absorbance of Citrate Synthase Developing Reagent at 412 nm in a convenient 96-well format. |
| MitoCheck Complex I Activity Assay Kit | 96 wells | CAY-700930-96 | page | data sheet | |
| MitoCheck Complex II Activity Assay Kit | 96 wells | CAY-700940-96 | page | data sheet | |
| MitoCheck Complex II/III Activity Assay Kit | 96 wells | CAY-700950-96 | page | data sheet | |
| Mitochondrial Permeability Transition Pore Assay Kit | 100 assays | BVN-K239-100 | page | data sheet | Mitochondria are the power centrals of the cell and play an essential role in energy production. Damage to mitochondria activates signaling pathways that induce apoptosis. The mitochondrial permeability transition pore (MPT pore or MPTP) is a nonspecific channel formed by components of the inner and outer mitochondrial membranes, and appears to be involved in the release of mitochondrial components during cell death. In healthy cells, MPTP’s flicker between open and closed states but during cell death MPTP’s dramatically alter the permeability of the mitochondria. Cytochrome c release and loss of mitochondrial membrane potential are subsequent to continuous pore activation. BioVision’s Mitochondrial Permeability Transition Pore Assay Kit provides a direct method of measuring cell death by measuring MPTP opening rather than relying on mitochondrial membrane potential alone. |
| Monoamine Oxidase A (MAO-A) Inhibitor Screening Kit (Fluorometric) | 100 assays | BVN-K796-100 | page | data sheet | Monoamine oxidases (MAO, EC 1.4.3.4) are a family of enzymes that can oxidize a wide variety of endogenous primary amines. Two isoforms, MAO-A and MAO-B, have been identified based on their substrate, inhibitor specificity, and tissue localization. MAO-A can oxidize primary amines such as serotonin and norepinephrine. MAO-A is a mitochondrial-bound enzyme that is ubiquitously expressed throughout the brain and other tissues. It has been implicated in panic, anxiety, and depression. Several MAO-A specific inhibitors such as clorgyline, brofaromine, toloxatone, tetrindole, etc. have been used as antidepressants, but their usage has been limited due to side effects. BioVision’s MAO-A Inhibitor Screening Kit offers a rapid, simple, sensitive, and reliable test suitable for high-throughput screening of MAO-A inhibitors. The assay is based on the fluorometric detection of H2O2, one of the byproducts generated during the oxidative deamination of MAO substrate. |
| Monoamine Oxidase Activity (Total MAO/MAO-A/MAO-B) Fluorometric Assay Kit | 100 assays | BVN-K795-100 | page | data sheet | Monoamine oxidases (MAO, EC 1.4.3.4) are a family of enzymes that can oxidize a wide variety of endogenous primary amines. Two isoforms, MAO-A and MAO-B, have been identified based on their substrate, inhibitor specificity and tissue localization. Clonogenic studies have shown that these two isozymes have similar catalytic characteristics, yet their amino acid sequences are different. MAO-A favors Serotonin, Norerpinephrine and Dopamine as substrates, while phenylethylamine and benzylamine are MAO-B preferred substrates. MAO-A and MAO-B are mitochondrial-bound enzymes that are ubiquitously expressed throughout the brain and other tissues. Imbalance of MAOs levels has been associated with schizophrenia, depression, attention deficit and other disorders. MAO-A has been implicated in panic, anxiety and depression, whereas MAO-B defects result in Alzheimer’s and Parkinson’s diseases. BioVision’s Monoamine Oxidase Activity (Total MAO/MAO-A/MAO-B) assay is a sensitive assay to detect total monoamine oxidase activity as well as MAO-A and MAO-B isoenzyme activities separately in the presence of Clorgyline and Selegiline - specific inhibitors for MAO-A and MAO-B, respectively. The assay is based on the fluorometric detection of H2O2, one of the byproducts generated during the oxidative deamination of the MAO substrate. The assay can detect as little as 5 µU of MAO enzymatic activity. |
| Monoamine Oxidase B (MAO-B) Inhibitor Screening Kit (Fluorometric) | 100 assays | BVN-K797-100 | page | data sheet | Monoamine oxidases (MAO, EC 1.4.3.4) are a family of enzymes that can oxidize a wide variety of endogenous primary amines. Two isoforms, MAO-A and MAO-B, have been identified based on their substrate, inhibitor specificity, and tissue localization. MAO-B can oxidize primary amines, but its list of specific substrates (i.e. benzylamine, phenylethylamine) is more limited compared to MAO-A. MAO-B is a mitochondrial-bound enzyme that is ubiquitously expressed throughout the brain and other tissues. It has been investigated in numerous studies including Parkinson’s disease, Alzheimer’s, and tobacco addiction. Specific MAO-B inhibitors such as selegiline, & rasagiline have been used to treat Parkinson’s patients, but their benefits are considered rather modest. BioVision’s MAO-B Inhibitor Screening Kit offers a rapid, simple, sensitive, and reliable test suitable for high-throughput screening of MAO-B inhibitors. The assay is based on the fluorometric detection of H2O2, one of the byproducts generated during the oxidative deamination of MAO substrate. |
| Oxygen Consumption Rate Assay Kit (MitoXpress®-Xtra HS Method) | 96 wells | CAY-600800-96 | page | data sheet | |
| Oxygen Consumption/MitoMembrane Potential Dual Assay Kit | 96 wells | CAY-600880-96 | page | data sheet | |
| Peroxiredoxin 1 (Prx1) (human) ELISA Kit | 1x96T | YIF-LF-EK0131 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. |
| Peroxiredoxin 1 (Prx1) (human) ELISA Kit (10x96T) | 10x96T | YIF-LF-EK0133 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. |
| Peroxiredoxin 1 (Prx1) (human) ELISA Kit (4x96T) | 4x96T | YIF-LF-EK0132 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. |
| Peroxiredoxin 2 (Prx2) (human) ELISA Kit | 1x96T | YIF-LF-EK0248 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. |
| Peroxiredoxin 2 (Prx2) (human) ELISA Kit (10x96T) | 10x96T | YIF-LF-EK0250 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. |
| Peroxiredoxin 2 (Prx2) (human) ELISA Kit (4x96T) | 4x96T | YIF-LF-EK0249 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. |
| Peroxiredoxin 3 (Prx3) (human) ELISA Kit | 1x96T | YIF-LF-EK0113 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling. |
| Peroxiredoxin 3 (Prx3) (human) ELISA Kit (10x96T) | 10x96T | YIF-LF-EK0115 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling. |
| Peroxiredoxin 3 (Prx3) (human) ELISA Kit (4x96T) | 4x96T | YIF-LF-EK0114 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling. |
| Peroxiredoxin 5 (Prx5) (human) ELISA Kit | 1x96T | YIF-LF-EK0212 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling. |
| Peroxiredoxin 5 (Prx5) (human) ELISA Kit (10x96T) | 10x96T | YIF-LF-EK0214 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling. |
| Peroxiredoxin 5 (Prx5) (human) ELISA Kit (4x96T) | 4x96T | YIF-LF-EK0213 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling. |
| Peroxiredoxin 6 (Prx6) (human) ELISA Kit | 1x96T | YIF-LF-EK0206 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Involved in redox regulation of the cell. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. |
| Peroxiredoxin 6 (Prx6) (human) ELISA Kit (10x96T) | 10x96T | YIF-LF-EK0208 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Involved in redox regulation of the cell. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. |
| Peroxiredoxin 6 (Prx6) (human) ELISA Kit (4x96T) | 4x96T | YIF-LF-EK0207 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Involved in redox regulation of the cell. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. |
| Peroxiredoxin IV (Prx4) (human) ELISA Kit (10x96T) | 10x96T | YIF-LF-EK0167 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). |
| Peroxiredoxin IV (Prx4) (human) ELISA Kit (20x96T) | 20x96T | YIF-LF-EK0168 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). |
| Peroxiredoxin IV (Prx4) (human) ELISA Kit (4x96T) | 4x96T | YIF-LF-EK0166 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). |
| Peroxiredoxin IV (Prx4) (human) Kit ELISA Kit | 1x96T | YIF-LF-EK0165 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). |
| Pyruvate Dehydrogenase (PDH) Activity Colorimetric Assay Kit | 100 assays | BVN-K679-100 | page | data sheet | Pyruvate Dehydrogenase (PDH) (EC 1.2.4.1) has a vital role in carbohydrate metabolism. It forms a well-characterized enzyme complex with dihydrolipoyl transacetylase (E2) and dihydrolipoyl dehydrogenase (E3). PDH converts pyruvate into acetyl-CoA in the presence of NAD and CoA, and links glycolysis to the citric acid cycle. PDH activity is inhibited by high intracellular ratios of ATP/ADP, NADH/NAD or Acetyl-CoA/CoA. In humans, PDH deficiency reduces mitochondrial function and is linked to neurodegenerative diseases. PDH deficiency is X-linked; it results in 2 forms of abnormality: a metabolic form (lactic acidosis) and a neurological form (seizure and/or neuropathological spasm). Recent studies show that PDH is a target of oncogene-induced senescence; activation of PDH enhances pyruvate utilization and increases respiration and redox stress. BioVision’s PDH assay kit provides a quick and easy way for monitoring PDH activity in various samples. In the assay, PDH converts pyruvate into an intermediate, which reduces the developer to a colored product with strong absorbance at 450 nm. The assay is simple, sensitive and can detect pyruvate dehydrogenase activity lower than 0.1 mU in a variety of samples. |
| Quick Cell Proliferation colorimetric Assay Kit | 500 assays | BVN-K301-500 | page | data sheet | The Quick Cell Proliferation Assay Kit provides all reagents and detailed instructions for a fast and sensitive quantification of cell proliferation and viability. The assay is based on the cleavage of the tetrazolium salt WST-1 to formazan by cellular mitochondrial dehydrogenases. Expansion in the number of viable cells resulted in an increase in the activity of the mitochondrial dehydrogenases, which leads to the increase in the amount of formazan dye formed. The formazan dye produced by viable cells can be quantified by multi-well spectrophotometer (microtiter plate reader) by measuring the absorbance of the dye solution at 440 nm. The assay can be used for the measurement of cell proliferation in response to growth factors, cytokines, mitogens, and nutrients, etc. It can also be used for the analysis of cytotoxic compounds like anticancer drugs and many other toxic agents and pharmaceutical compounds. The new method is so simple, requiring no washing, no harvesting, and no solubilization steps, and is faster and more sensitive than MTT, XTT, or MTS-based assays. The entire assay can be performed in a microtiter plate. |
| Quick Cell Proliferation Colorimetric Assay Kit | 2500 assays | BVN-K301-2500 | page | data sheet | The Quick Cell Proliferation Assay Kit provides all reagents and detailed instructions for a fast and sensitive quantification of cell proliferation and viability. The assay is based on the cleavage of the tetrazolium salt WST-1 to formazan by cellular mitochondrial dehydrogenases. Expansion in the number of viable cells resulted in an increase in the activity of the mitochondrial dehydrogenases, which leads to the increase in the amount of formazan dye formed. The formazan dye produced by viable cells can be quantified by multi-well spectrophotometer (microtiter plate reader) by measuring the absorbance of the dye solution at 440 nm. The assay can be used for the measurement of cell proliferation in response to growth factors, cytokines, mitogens, and nutrients, etc. It can also be used for the analysis of cytotoxic compounds like anticancer drugs and many other toxic agents and pharmaceutical compounds. The new method is so simple, requiring no washing, no harvesting, and no solubilization steps, and is faster and more sensitive than MTT, XTT, or MTS-based assays. The entire assay can be performed in a microtiter plate. |
| Quick Cell Proliferation colorimetric Assay Kit Plus | 2500 assays | BVN-K302-2500 | page | data sheet | The Quick Cell Proliferation Assay Kit II provides by far the easiest and most sensitive means for quantifying cell proliferation and viability. The assay is based on the cleavage of the tetrazolium salt to formazan by cellular mitochondrial dehydrogenase. The amount of the dye generated by activity of dehydrogenase is directly proportional to the number of living cells. The formazan dye produced by viable cells can be quantified by multi-well spectrophotometer (microtiter plate reader) by measuring the absorbance of the dye solution at 440 nm. The assay can be used for measurement of cell proliferation in response to growth factors, cytokines, mitogens, and nutrients, etc. It can also be used for the analysis of cytotoxic compounds like anticancer drugs and many other toxic agents and pharmaceutical compounds. The new method is so simple, just add-and-read, requiring no washing, no harvesting, and no solubilization steps. It is faster, stable, and more sensitive than MTT, XTT, MTS based assays. The assay correlates well with the [3H]-thymidine incorporation assay. |
| Quick Cell Proliferation colorimetric Assay Kit Plus | 500 assays | BVN-K302-500 | page | data sheet | The Quick Cell Proliferation Assay Kit II provides by far the easiest and most sensitive means for quantifying cell proliferation and viability. The assay is based on the cleavage of the tetrazolium salt to formazan by cellular mitochondrial dehydrogenase. The amount of the dye generated by activity of dehydrogenase is directly proportional to the number of living cells. The formazan dye produced by viable cells can be quantified by multi-well spectrophotometer (microtiter plate reader) by measuring the absorbance of the dye solution at 440 nm. The assay can be used for measurement of cell proliferation in response to growth factors, cytokines, mitogens, and nutrients, etc. It can also be used for the analysis of cytotoxic compounds like anticancer drugs and many other toxic agents and pharmaceutical compounds. The new method is so simple, just add-and-read, requiring no washing, no harvesting, and no solubilization steps. It is faster, stable, and more sensitive than MTT, XTT, MTS based assays. The assay correlates well with the [3H]-thymidine incorporation assay. |
| Ready-to-use Cell Proliferation Colorimetric Reagent, WST-1 | 2500 assays | BVN-K304-2500 | page | data sheet | The ready-to-use cell proliferation reagent, WST-1 provides a simple and accurate method to measure cell proliferation, which is based on the cleavage of the tetrazolium salt WST-1 to formazan by cellular mitochondrial dehydrogenases. Expansion in the number of viable cells results in an increase in the activity of the mitochondrial dehydrogenases, which in turn leads to increase in the amount of formazan dye formed. The formazan dye produced by viable cells can be quantified by measuring the absorbance at 440 nm. This new method is non-radioactive, rapid and more sensitive than MTT, XTT, or MTS-based assays. The entire assay can be performed in the same microtiter plate and does not require extra steps like washing, harvesting and cell solubilization. |
| Succinate Dehydrogenase Activity Colorimetric Assay Kit | 100 assays | BVN-K660-100 | page | data sheet | Succinate Dehydrogenase (SDH) (EC 1.3.5.1) or succinate-coenzyme Q reductase (SQR) or respiratory complex II is an enzyme complex, which is bound to the inner mitochondrial membrane. SDH participates in both the citric acid cycle and electron transport chain. In mammals and many bacteria, SDH consists of 2 hydrophilic subunits, SDHA (flavoprotein) and SDHB (iron-sulfur protein) and 2 hydrophobic membrane anchor subunits: SDHC and SDHD. SDH oxidizes succinate to fumarate and transfers the electrons to ubiquinone. SDH deficiency in humans leads to a variety of phenotypes including Leigh syndrome, a neurometabolic disorder, tumor formation, and myopathy. Recent studies show that SDH can prevent the generation of ROS (reactive oxygen species); therefore, measurement of succinate dehydrogenase activity has wide applications. BioVision’s Succinate Dehydrogenase Activity Assay kit is rapid, simple and high-throughput adaptable. In this assay, Succinate dehydrogenase converts succinate to fumarate, and transfers the electron to an artificial electron acceptor (Probe), which changes the color from blue to a colorless product (depending upon the sample enzymatic activity). This assay kit can detect less than 0.1mU Succinate Dehydrogenase Activity in a variety of samples. |
| Succinyl-CoA Synthetase Activity Colorimetric Assay Kit | 100 assays | BVN-K597-100 | page | data sheet | Succinyl-CoA Synthetase (SCS, also called Succinyl-CoA ligase, Succinate Thiokinase) (EC 6.2.1.5) is a critical enzyme in the citric acid cycle and an important metabolic intermediate for porphyrin, heme and ketone body biosynthesis. It is located in the mitochondrial matrix and is a heterodimer composed of one α and one β subunit. In humans, Succinyl-CoA Synthetase deficiency causes the build-up of lactic acid leading to lactic acidosis, which can be fatal in infants. Measurement and analysis of SCS activity is useful for both mechanistic studies as well as for diagnostic purposes. In BioVision’s Succinyl-CoA Synthetase Activity Assay, SCS converts succinate into succinyl-CoA in the presence of ATP and CoA. Succinyl-CoA reacts with the Developer to form a colored product with strong absorbance at 450 nm. This assay kit is simple, sensitive, and high-throughput adaptable. It can detect less than 0.1 mU of Succinyl-CoA Synthetase activity in a variety of samples. |
| Superoxide Dismutase 1 (SOD1) (human) ELISA Kit | 1x96T | YIF-LF-EK0101 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. |
| Superoxide Dismutase 1 (SOD1) (human) ELISA Kit (10x96T) | 10x96T | YIF-LF-EK0103 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. |
| Superoxide Dismutase 1 (SOD1) (human) ELISA Kit (4x96T) | 4x96T | YIF-LF-EK0102 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. |
| Superoxide Dismutase 2 (SOD2) (human) ELISA Kit | 1x96T | YIF-LF-EK0104 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. |
| Superoxide Dismutase 2 (SOD2) (human) ELISA Kit (10x96T) | 10x96T | YIF-LF-EK0106 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. |
| Superoxide Dismutase 2 (SOD2) (human) ELISA Kit (4x96T) | 4x96T | YIF-LF-EK0105 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. |
| Superoxide Dismutase 3 (SOD3) (human) ELISA Kit | 1x96T | YIF-LF-EK0107 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Destroys radicals which are normally produced within the cells and which are toxic to biological systems. |
| Superoxide Dismutase 3 (SOD3) (human) ELISA Kit (10x96T) | 10x96T | YIF-LF-EK0109 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Destroys radicals which are normally produced within the cells and which are toxic to biological systems. |
| Superoxide Dismutase 3 (SOD3) (human) ELISA Kit (4x96T) | 4x96T | YIF-LF-EK0108 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Destroys radicals which are normally produced within the cells and which are toxic to biological systems. |
| Superoxide Dismutase 4 (SOD4) (human) ELISA Kit | 1x96T | YIF-LF-EK0209 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu,Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. |
| Superoxide Dismutase 4 (SOD4) (human) ELISA Kit (10x96T) | 10x96T | YIF-LF-EK0211 | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu,Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. | ||
| Superoxide Dismutase 4 (SOD4) (human) ELISA Kit (4x96T) | 4x96T | YIF-LF-EK0210 | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu,Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. | ||
| Thioredoxin Reductase 2 (human) ELISA Kit | 1x96T | YIF-LF-EK0218 | The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxido-reductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 ° 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1). | ||
| Thioredoxin Reductase 2 (human) ELISA Kit (10x96T) | 10x96T | YIF-LF-EK0220 | The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxido-reductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 ° 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1). | ||
| Thioredoxin Reductase 2 (human) ELISA Kit (4x96T) | 4x96T | YIF-LF-EK0219 | The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxido-reductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 ° 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1). | ||
| Chemicals, Biochemicals, Natural Products | |||||
| (+)-Etomoxir (sodium salt) | 10 mg | CAY-11969-10 | page | data sheet | An irreversible inhibitor of carnitine palmitoyltransferase 1, the mitochondrial enzyme involved in fatty acid β-oxidation (IC50 = 5-20 nM in rat liver); also acts as a direct agonist of PPARα |
| (+)-Etomoxir (sodium salt) | 25 mg | CAY-11969-25 | page | data sheet | An irreversible inhibitor of carnitine palmitoyltransferase 1, the mitochondrial enzyme involved in fatty acid β-oxidation (IC50 = 5-20 nM in rat liver); also acts as a direct agonist of PPARα |
| (+)-Etomoxir (sodium salt) | 50 mg | CAY-11969-50 | page | data sheet | An irreversible inhibitor of carnitine palmitoyltransferase 1, the mitochondrial enzyme involved in fatty acid β-oxidation (IC50 = 5-20 nM in rat liver); also acts as a direct agonist of PPARα |
| (+)-Etomoxir (sodium salt) | 5 mg | CAY-11969-5 | page | data sheet | An irreversible inhibitor of carnitine palmitoyltransferase 1, the mitochondrial enzyme involved in fatty acid β-oxidation (IC50 = 5-20 nM in rat liver); also acts as a direct agonist of PPARα |
| 20-Hydroxyecdysone | 50 mg | AG-CN2-0072-M050 | page | data sheet | C27H44O7. CAS: 5289-74-7. MW: 480.6. A member of the ecdysteroid family. Ecdysone receptor (EcR) agonist. More potent than ecdysone. Induces the expression of genes coding for proteins that the larva requires, and it causes chromosome puffs (sites of high expression) to form in polytene chromosomes. Plays a key role in insect development, cell proliferaton, growth and apoptosis by controlling gene expression involved in moulting and metamorphosis. It acts through a heterodimeric receptor comprising the ecdysone receptor and the ultraspiracle proteins (USP). Regulates lipolysis in insects. Appears in many plants mostly as a protection agent (toxins or antifeedants) against herbivorous insects. Used for controlled gene expression in scientific research, agriculture and medicine. Used for the development of selective insect growth regulators for use as environmentally benign insecticides. Shows biological effects on mammalian species. Neurosteroid. Antiepileptic. Acts on the modulatory site of the GABAA receptor and potentiates GABAergic inhibition in rat. Was shown to stimulate and modulate neutrophil production. Antidiabetic and antiobesity. Could be used as a nutritional supplement for the prevention and treatment of obesity and obesity-associated disorders. May protect PC12 cells against CoCl(2)-induced cell injury by inhibiting ROS production and modulating components of the mitochondrial apoptosis pathway. Does not have potent anabolic properties, however, a muscle-specific increase is observed and genes are identified to provide an explanation for the muscle accretion. Potential fibrosis antagonist for renal proximal tubule cells. Acts through suppressing post-receptor signaling of TGF-beta1 and blocking the expression of Snail. |
| 20-Hydroxyecdysone | 5 mg | AG-CN2-0072-M005 | page | data sheet | C27H44O7. CAS: 5289-74-7. MW: 480.6. A member of the ecdysteroid family. Ecdysone receptor (EcR) agonist. More potent than ecdysone. Induces the expression of genes coding for proteins that the larva requires, and it causes chromosome puffs (sites of high expression) to form in polytene chromosomes. Plays a key role in insect development, cell proliferaton, growth and apoptosis by controlling gene expression involved in moulting and metamorphosis. It acts through a heterodimeric receptor comprising the ecdysone receptor and the ultraspiracle proteins (USP). Regulates lipolysis in insects. Appears in many plants mostly as a protection agent (toxins or antifeedants) against herbivorous insects. Used for controlled gene expression in scientific research, agriculture and medicine. Used for the development of selective insect growth regulators for use as environmentally benign insecticides. Shows biological effects on mammalian species. Neurosteroid. Antiepileptic. Acts on the modulatory site of the GABAA receptor and potentiates GABAergic inhibition in rat. Was shown to stimulate and modulate neutrophil production. Antidiabetic and antiobesity. Could be used as a nutritional supplement for the prevention and treatment of obesity and obesity-associated disorders. May protect PC12 cells against CoCl(2)-induced cell injury by inhibiting ROS production and modulating components of the mitochondrial apoptosis pathway. Does not have potent anabolic properties, however, a muscle-specific increase is observed and genes are identified to provide an explanation for the muscle accretion. Potential fibrosis antagonist for renal proximal tubule cells. Acts through suppressing post-receptor signaling of TGF-beta1 and blocking the expression of Snail. |
| 20-Hydroxyecdysone | 10 mg | AG-CN2-0072-M010 | page | data sheet | C27H44O7. CAS: 5289-74-7. MW: 480.6. A member of the ecdysteroid family. Ecdysone receptor (EcR) agonist. More potent than ecdysone. Induces the expression of genes coding for proteins that the larva requires, and it causes chromosome puffs (sites of high expression) to form in polytene chromosomes. Plays a key role in insect development, cell proliferaton, growth and apoptosis by controlling gene expression involved in moulting and metamorphosis. It acts through a heterodimeric receptor comprising the ecdysone receptor and the ultraspiracle proteins (USP). Regulates lipolysis in insects. Appears in many plants mostly as a protection agent (toxins or antifeedants) against herbivorous insects. Used for controlled gene expression in scientific research, agriculture and medicine. Used for the development of selective insect growth regulators for use as environmentally benign insecticides. Shows biological effects on mammalian species. Neurosteroid. Antiepileptic. Acts on the modulatory site of the GABAA receptor and potentiates GABAergic inhibition in rat. Was shown to stimulate and modulate neutrophil production. Antidiabetic and antiobesity. Could be used as a nutritional supplement for the prevention and treatment of obesity and obesity-associated disorders. May protect PC12 cells against CoCl(2)-induced cell injury by inhibiting ROS production and modulating components of the mitochondrial apoptosis pathway. Does not have potent anabolic properties, however, a muscle-specific increase is observed and genes are identified to provide an explanation for the muscle accretion. Potential fibrosis antagonist for renal proximal tubule cells. Acts through suppressing post-receptor signaling of TGF-beta1 and blocking the expression of Snail. |
| 3,3'-Dipropylthiacarbocyanine iodide | 500 mg | CDX-D0007-M500 | page | data sheet | C23H25IN2S2. CAS: 53336-12-2. MW: 520.49. Carbocyanine dyes, particularly thiacyanines such as DiSC3(3) can inhibit respiration and may therefore be relatively cytotoxic. 3,3'-dipropyl-thiadicarbocyanine iodide is sensitive to membrane potential, fluorescence response to depolarization depends on the staining concentration and detection method. Selected applications are:-Calcium channels and other ion transport systems-Mitochondrial activity-Neurons and brain tissue-Membrane potential in intact yeast cells |
| 3,3'-Dipropylthiacarbocyanine iodide | 250 mg | CDX-D0007-M250 | page | data sheet | C23H25IN2S2. CAS: 53336-12-2. MW: 520.49. Carbocyanine dyes, particularly thiacyanines such as DiSC3(3) can inhibit respiration and may therefore be relatively cytotoxic. 3,3'-dipropyl-thiadicarbocyanine iodide is sensitive to membrane potential, fluorescence response to depolarization depends on the staining concentration and detection method. Selected applications are:-Calcium channels and other ion transport systems-Mitochondrial activity-Neurons and brain tissue-Membrane potential in intact yeast cells |
| 3-Guanidinopropionic Acid | 5 g | CAY-16725-5 | page | data sheet | A creatine analog that alters skeletal muscle energy expenditure; reduces cellular ATP, creatine, and phosphocreatine levels and stimulates AMPK, activating PGC-1α; increases the expression of genes for oxidative phosphorylation, electron transport chain, and mitochondrial biogenesis |
| 3-Guanidinopropionic Acid | 500 mg | CAY-16725-500 | page | data sheet | A creatine analog that alters skeletal muscle energy expenditure; reduces cellular ATP, creatine, and phosphocreatine levels and stimulates AMPK, activating PGC-1α; increases the expression of genes for oxidative phosphorylation, electron transport chain, and mitochondrial biogenesis |
| 3-Guanidinopropionic Acid | 1 g | CAY-16725-1 | page | data sheet | A creatine analog that alters skeletal muscle energy expenditure; reduces cellular ATP, creatine, and phosphocreatine levels and stimulates AMPK, activating PGC-1α; increases the expression of genes for oxidative phosphorylation, electron transport chain, and mitochondrial biogenesis |
| 3-Guanidinopropionic Acid | 10 g | CAY-16725-10 | page | data sheet | A creatine analog that alters skeletal muscle energy expenditure; reduces cellular ATP, creatine, and phosphocreatine levels and stimulates AMPK, activating PGC-1α; increases the expression of genes for oxidative phosphorylation, electron transport chain, and mitochondrial biogenesis |
| 3-Methyladenine | 25 mg | AG-CR1-3597-M025 | page | data sheet | C6H7N5. CAS: 5142-23-4. MW: 149.2. Potent cell permeable and selective inhibitor of phosphatidyl-inositol 3-kinase (PI3K). Blocks class I, class II and class III PI3Ks, including some downstream targets. Blocks class I PI3K persistently and class III PI3K transiently. Induces autophagy under nutrient-rich conditions and inhibits starvation-induced autophagy due to differential effects on class I versus class III PI3 kinase. Shows some limited Vps34 preference in vitro compared to PtdIns3Kgamma. However, it is typically employed in cellular studies at a concentration of 10 mM, which can inhibit all PtdIns3Ks. Can target other kinases and affect other cellular processes, such as glycogen metabolism, lysosomal acidification, endocytosis and mitochondrial permeability transition. Anticancer compound. Neuroprotective. PKA-activation dependent lipolytic agent. Enhances ATGL-dependent hydrolysis of triacylglycerols. |
| 3-Methyladenine | 100 mg | AG-CR1-3597-M100 | page | data sheet | C6H7N5. CAS: 5142-23-4. MW: 149.2. Potent cell permeable and selective inhibitor of phosphatidyl-inositol 3-kinase (PI3K). Blocks class I, class II and class III PI3Ks, including some downstream targets. Blocks class I PI3K persistently and class III PI3K transiently. Induces autophagy under nutrient-rich conditions and inhibits starvation-induced autophagy due to differential effects on class I versus class III PI3 kinase. Shows some limited Vps34 preference in vitro compared to PtdIns3Kgamma. However, it is typically employed in cellular studies at a concentration of 10 mM, which can inhibit all PtdIns3Ks. Can target other kinases and affect other cellular processes, such as glycogen metabolism, lysosomal acidification, endocytosis and mitochondrial permeability transition. Anticancer compound. Neuroprotective. PKA-activation dependent lipolytic agent. Enhances ATGL-dependent hydrolysis of triacylglycerols. |
| 3-Methyladenine | 250 mg | AG-CR1-3597-M250 | page | data sheet | C6H7N5. CAS: 5142-23-4. MW: 149.2. Potent cell permeable and selective inhibitor of phosphatidyl-inositol 3-kinase (PI3K). Blocks class I, class II and class III PI3Ks, including some downstream targets. Blocks class I PI3K persistently and class III PI3K transiently. Induces autophagy under nutrient-rich conditions and inhibits starvation-induced autophagy due to differential effects on class I versus class III PI3 kinase. Shows some limited Vps34 preference in vitro compared to PtdIns3Kgamma. However, it is typically employed in cellular studies at a concentration of 10 mM, which can inhibit all PtdIns3Ks. Can target other kinases and affect other cellular processes, such as glycogen metabolism, lysosomal acidification, endocytosis and mitochondrial permeability transition. Anticancer compound. Neuroprotective. PKA-activation dependent lipolytic agent. Enhances ATGL-dependent hydrolysis of triacylglycerols. |
| 3-Nitropropionic acid | 250 mg | BVN-2093-250 | page | data sheet | A plant and fungal toxin, 3-nitropropionic acid acts as an irreversible inactivator of succinate dehydrogenase. Selectively inhibits succinic dehydrogenase complex (Complex II) in the mitochondrial electron transport chain. Also shown to cause brain lesions similar to those of Huntington′s disease. |
| 3-Nitropropionic acid | 50 mg | BVN-2093-50 | page | data sheet | A plant and fungal toxin, 3-nitropropionic acid acts as an irreversible inactivator of succinate dehydrogenase. Selectively inhibits succinic dehydrogenase complex (Complex II) in the mitochondrial electron transport chain. Also shown to cause brain lesions similar to those of Huntington′s disease. |
| 4-Di-2-ASP | 5 g | CDX-D0012-G005 | page | data sheet | C18H23IN2. CAS: 105802-46-8. MW: 394.29. Some cationic mitochondrial dyes such as 4-Di-1-ASP and 4-Di-2-ASP stain presynaptic nerve terminals independent of neuronal activity. The photostable 4-Di-2-ASP dye, which is nontoxic to cells, has been employed to stain living nerve terminals in rabbit corneal epithelium, in rat epidermis and at mouse, snake and frog neuromuscular junctions, as well as to visualize the innervation of the human choroid and whole mounts of the gastrointestinal tract. Methods for using 4-Di-2-ASP to image neuronal cells in live animals have been described (Ex/Em = 488/607 nm). |
| 4-Di-2-ASP | 1 g | CDX-D0012-G001 | page | data sheet | C18H23IN2. CAS: 105802-46-8. MW: 394.29. Some cationic mitochondrial dyes such as 4-Di-1-ASP and 4-Di-2-ASP stain presynaptic nerve terminals independent of neuronal activity. The photostable 4-Di-2-ASP dye, which is nontoxic to cells, has been employed to stain living nerve terminals in rabbit corneal epithelium, in rat epidermis and at mouse, snake and frog neuromuscular junctions, as well as to visualize the innervation of the human choroid and whole mounts of the gastrointestinal tract. Methods for using 4-Di-2-ASP to image neuronal cells in live animals have been described (Ex/Em = 488/607 nm). |
| AdipoRon | 10 mg | AG-CR1-0154-M010 | page | data sheet | C27H28N2O3. CAS: 924416-43-3. MW: 428.5. Orally-active adiponectin receptor (AdipoR) agonist. Binds to AdipoR1 and AdipoR2 at low µm concentration. Activates 5'-adenosine monophosphate-activated protein kinase (AMPK) in cultured mammalian cells. Activates peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1alpha) which boosts mitochondrial proliferation and energy metabolism. Improves diabetes, glucose and lipid metabolism and insulin sensitivity in cultured cells and in mice by AdipoR-dependent mechanisms. Rescued the shortened lifespan of db/db mice (AdipoRs KO) on high-fat diet. Reduces expression levels of genes encoding inflammatory cytokines such as TNF-alpha, IL-6 and CCL-2 in WAT of WT mice but not db/db mice. |
| AdipoRon | 50 mg | AG-CR1-0154-M050 | page | data sheet | C27H28N2O3. CAS: 924416-43-3. MW: 428.5. Orally-active adiponectin receptor (AdipoR) agonist. Binds to AdipoR1 and AdipoR2 at low µm concentration. Activates 5'-adenosine monophosphate-activated protein kinase (AMPK) in cultured mammalian cells. Activates peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1alpha) which boosts mitochondrial proliferation and energy metabolism. Improves diabetes, glucose and lipid metabolism and insulin sensitivity in cultured cells and in mice by AdipoR-dependent mechanisms. Rescued the shortened lifespan of db/db mice (AdipoRs KO) on high-fat diet. Reduces expression levels of genes encoding inflammatory cytokines such as TNF-alpha, IL-6 and CCL-2 in WAT of WT mice but not db/db mice. |
| AdipoRon . HCl (water soluble) | 50 mg | AG-CR1-0156-M050 | page | data sheet | C27H28N2O3 . HCl . H2O. CAS: 924416-43-3 (free base). MW: 428.5 . 36.5 . 18.0. Orally-active adiponectin receptor (AdipoR) agonist. Binds to AdipoR1 and AdipoR2 at low µm concentration. Activates 5'-adenosine monophosphate-activated protein kinase (AMPK) in cultured mammalian cells. Activates peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1alpha) which boosts mitochondrial proliferation and energy metabolism. Improves diabetes, glucose and lipid metabolism and insulin sensitivity in cultured cells and in mice by AdipoR-dependent mechanisms. Rescued the shortened lifespan of db/db mice (AdipoRs KO) on high-fat diet. Reduces expression levels of genes encoding inflammatory cytokines such as TNF-alpha, IL-6 and CCL-2 in WAT of WT mice but not db/db mice. |
| AdipoRon . HCl (water soluble) | 10 mg | AG-CR1-0156-M010 | page | data sheet | C27H28N2O3 . HCl . H2O. CAS: 924416-43-3 (free base). MW: 428.5 . 36.5 . 18.0. Orally-active adiponectin receptor (AdipoR) agonist. Binds to AdipoR1 and AdipoR2 at low µm concentration. Activates 5'-adenosine monophosphate-activated protein kinase (AMPK) in cultured mammalian cells. Activates peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1alpha) which boosts mitochondrial proliferation and energy metabolism. Improves diabetes, glucose and lipid metabolism and insulin sensitivity in cultured cells and in mice by AdipoR-dependent mechanisms. Rescued the shortened lifespan of db/db mice (AdipoRs KO) on high-fat diet. Reduces expression levels of genes encoding inflammatory cytokines such as TNF-alpha, IL-6 and CCL-2 in WAT of WT mice but not db/db mice. |
| Aftin-4 | 1 mg | MR-C0014-M001 | page | data sheet | C20H28N6O. CAS: 866893-90-5. MW: 368.5. Roscovitine-related purine with no activity on CDKs (used as control for roscovitine). Selectively and potently increases production of extracellular Abeta42 and decreases production of extracellular Abeta38 in cultured cells. Extracellular Abeta40 levels remain stable. Intracellular levels of these amyloids appear to remain stable. Alzheimer's Disease (AD) accelerator that interacts with VDAC1, prohibitin and mitofilin, possibly interfering with subcellular compartmentalization and lipid rafts properties, shifting gamma-secretase activity toward Abeta42 generation. Induces a reversible mitochondrial phenotype reminiscent of the one observed in AD brains. Tool to detect inhibitors of Aftin-induced actions (potential anti-AD compounds). Binds pyridoxal kinase. |
| Aftin-4 | 5 mg | BVN-2574-5 | page | data sheet | A Roscovitine-related purine derivative that selectively and potently increases production of extracellular Aβ42 and decreases production of extracellular Aβ38 in cultured cells. Extracellular Aβ40 levels remain stable. Intracellular levels of these amyloids appear to remain stable. Alzheimer's Disease (AD) accelerator that interacts with VDAC1, prohibitin and mitofilin, possibly interfering with subcellular compartmentalization and lipid rafts properties, shifting γ-secretase activity toward Aβ42 generation. Induces a reversible mitochondrial phenotype reminiscent of the one observed in AD brains. |
| Aftin-4 | 5 mg | MR-C0014-M005 | page | data sheet | C20H28N6O. CAS: 866893-90-5. MW: 368.5. Roscovitine-related purine with no activity on CDKs (used as control for roscovitine). Selectively and potently increases production of extracellular Abeta42 and decreases production of extracellular Abeta38 in cultured cells. Extracellular Abeta40 levels remain stable. Intracellular levels of these amyloids appear to remain stable. Alzheimer's Disease (AD) accelerator that interacts with VDAC1, prohibitin and mitofilin, possibly interfering with subcellular compartmentalization and lipid rafts properties, shifting gamma-secretase activity toward Abeta42 generation. Induces a reversible mitochondrial phenotype reminiscent of the one observed in AD brains. Tool to detect inhibitors of Aftin-induced actions (potential anti-AD compounds). Binds pyridoxal kinase. |
| Aftin-4 | 25 mg | MR-C0014-M025 | page | data sheet | C20H28N6O. CAS: 866893-90-5. MW: 368.5. Roscovitine-related purine with no activity on CDKs (used as control for roscovitine). Selectively and potently increases production of extracellular Abeta42 and decreases production of extracellular Abeta38 in cultured cells. Extracellular Abeta40 levels remain stable. Intracellular levels of these amyloids appear to remain stable. Alzheimer's Disease (AD) accelerator that interacts with VDAC1, prohibitin and mitofilin, possibly interfering with subcellular compartmentalization and lipid rafts properties, shifting gamma-secretase activity toward Abeta42 generation. Induces a reversible mitochondrial phenotype reminiscent of the one observed in AD brains. Tool to detect inhibitors of Aftin-induced actions (potential anti-AD compounds). Binds pyridoxal kinase. |
| Aftin-4 | 1 mg | BVN-2574-1 | page | data sheet | A Roscovitine-related purine derivative that selectively and potently increases production of extracellular Aβ42 and decreases production of extracellular Aβ38 in cultured cells. Extracellular Aβ40 levels remain stable. Intracellular levels of these amyloids appear to remain stable. Alzheimer's Disease (AD) accelerator that interacts with VDAC1, prohibitin and mitofilin, possibly interfering with subcellular compartmentalization and lipid rafts properties, shifting γ-secretase activity toward Aβ42 generation. Induces a reversible mitochondrial phenotype reminiscent of the one observed in AD brains. |
| Aftin-5 | 1 mg | BVN-2575-1 | page | data sheet | Roscovitine-related purine with no activity on CDKS. Selectively and potently increases production of extracellular Aβ42 and decreases production of extracellular Aβ38 in cultured cells. Extracellular Aβ40 levels remain stable. Intracellular levels of these amyloids appear to remain stable. Alzheimer's Disease (AD) accelerator that interacts with VDAC1, prohibitin and mitofilin, possibly interfering with subcellular compartmentalization and lipid rafts properties, shifting γ-secretase activity toward Aβ42 generation. Induces a reversible mitochondrial phenotype reminiscent of the one observed in AD brains. |
| Aftin-5 | 1 mg | MR-C0015-M001 | page | data sheet | C19H26N6O. CAS: . MW: 354.5. Roscovitine-related purine with no activity on CDKs (used as control for roscovitine). Selectively and potently increases production of extracellular Abeta42 and decreases production of extracellular Abeta38 in cultured cells. Extracellular Abeta40 levels remain stable. Intracellular levels of these amyloids appear to remain stable. Alzheimer's Disease (AD) accelerator that interacts with VDAC1, prohibitin and mitofilin, possibly interfering with subcellular compartmentalization and lipid rafts properties, shifting gamma-secretase activity toward Abeta42 generation. Induces a reversible mitochondrial phenotype reminiscent of the one observed in AD brains. Tool to detect inhibitors of Aftin-induced actions (potential anti-AD compounds). |
| Aftin-5 | 5 mg | MR-C0015-M005 | page | data sheet | C19H26N6O. CAS: . MW: 354.5. Roscovitine-related purine with no activity on CDKs (used as control for roscovitine). Selectively and potently increases production of extracellular Abeta42 and decreases production of extracellular Abeta38 in cultured cells. Extracellular Abeta40 levels remain stable. Intracellular levels of these amyloids appear to remain stable. Alzheimer's Disease (AD) accelerator that interacts with VDAC1, prohibitin and mitofilin, possibly interfering with subcellular compartmentalization and lipid rafts properties, shifting gamma-secretase activity toward Abeta42 generation. Induces a reversible mitochondrial phenotype reminiscent of the one observed in AD brains. Tool to detect inhibitors of Aftin-induced actions (potential anti-AD compounds). |
| Aftin-5 | 5 mg | BVN-2575-5 | page | data sheet | Roscovitine-related purine with no activity on CDKS. Selectively and potently increases production of extracellular Aβ42 and decreases production of extracellular Aβ38 in cultured cells. Extracellular Aβ40 levels remain stable. Intracellular levels of these amyloids appear to remain stable. Alzheimer's Disease (AD) accelerator that interacts with VDAC1, prohibitin and mitofilin, possibly interfering with subcellular compartmentalization and lipid rafts properties, shifting γ-secretase activity toward Aβ42 generation. Induces a reversible mitochondrial phenotype reminiscent of the one observed in AD brains. |
| Aftin-5 | 25 mg | MR-C0015-M025 | page | data sheet | C19H26N6O. CAS: . MW: 354.5. Roscovitine-related purine with no activity on CDKs (used as control for roscovitine). Selectively and potently increases production of extracellular Abeta42 and decreases production of extracellular Abeta38 in cultured cells. Extracellular Abeta40 levels remain stable. Intracellular levels of these amyloids appear to remain stable. Alzheimer's Disease (AD) accelerator that interacts with VDAC1, prohibitin and mitofilin, possibly interfering with subcellular compartmentalization and lipid rafts properties, shifting gamma-secretase activity toward Abeta42 generation. Induces a reversible mitochondrial phenotype reminiscent of the one observed in AD brains. Tool to detect inhibitors of Aftin-induced actions (potential anti-AD compounds). |
| Amiodarone Hydrochloride | 100 mg | BVN-1828-100 | page | data sheet | A non-selective ion channel blocker with broad fungicidal activity. Amiodarone induces an immediate influx of Ca2+ in Saccharomyces cerevisiae, followed by mitochondrial fragmentation and cell death. Also acts as an autophagy inducer. |
| Amiodarone Hydrochloride | 500 mg | BVN-1828-500 | page | data sheet | A non-selective ion channel blocker with broad fungicidal activity. Amiodarone induces an immediate influx of Ca2+ in Saccharomyces cerevisiae, followed by mitochondrial fragmentation and cell death. Also acts as an autophagy inducer. |
| Anthralin | 5 g | CDX-D0308-G005 | page | data sheet | C14H10O3. CAS: 1143-38-0. MW: 226.2. Anthralin is a leukotriene biosynthesis inhibitor. It inhibits LTB4 omega-oxidation and disrupts mitochondria function. Anthralin is used in the treatment of psoriasis, as a fungicide, in the treatment of ringworm infections and in chronic dermatoses. It accumulates in mitochondria where it interferes with the supply of energy to the cell, probably by the oxidation of dithranol releasing free radicals. This impedes DNA replication and so slows the excessive cell division that occurs in psoriatic plaques. Numerous studies have demonstrated anti-proliferative and anti-inflammatory effects of anthralin on psoriatic and normal skin. It is also used as matrix substance for MALDI-MS (matrix-assisted laser desorption ionization MS). |
| Anthralin | 1 g | CDX-D0308-G001 | page | data sheet | C14H10O3. CAS: 1143-38-0. MW: 226.2. Anthralin is a leukotriene biosynthesis inhibitor. It inhibits LTB4 omega-oxidation and disrupts mitochondria function. Anthralin is used in the treatment of psoriasis, as a fungicide, in the treatment of ringworm infections and in chronic dermatoses. It accumulates in mitochondria where it interferes with the supply of energy to the cell, probably by the oxidation of dithranol releasing free radicals. This impedes DNA replication and so slows the excessive cell division that occurs in psoriatic plaques. Numerous studies have demonstrated anti-proliferative and anti-inflammatory effects of anthralin on psoriatic and normal skin. It is also used as matrix substance for MALDI-MS (matrix-assisted laser desorption ionization MS). |
| Antimycin A | 10 mg | BVN-2247-10 | page | data sheet | Antimycin A, isolated from Streptomyces sp., is a mixture of Antimycins A1, A2, A3 and A4. Inhibits mitochondrial electron transport, specifically between cytochromes b and c1. Induces apoptosis, which is not prevented by the presence of Bcl-2. |
| Antimycin A | 50 mg | BVN-2247-50 | page | data sheet | Antimycin A, isolated from Streptomyces sp., is a mixture of Antimycins A1, A2, A3 and A4. Inhibits mitochondrial electron transport, specifically between cytochromes b and c1. Induces apoptosis, which is not prevented by the presence of Bcl-2. |
| Asteltoxin | 250 µg | AG-CN2-0441-C250 | page | data sheet | C23H30O7. CAS: 79663-49-3. MW: 418.5. Mycotoxin. Strong inhibitor of ATPase activity of BF1 from E. coli. Mitochondrial respiration inhibitor. Inhibits the energy transfer system in mitochondria, specifically the Mg+ -ATPase activity. |
| AT-101 | 25 mg | BVN-2380-25 | page | data sheet | AT-101 is the R-(-) enantiomer of Gossypol that acts as an inhibitor of the antiapoptotic Bcl proteins (Bcl-2, Bcl-XL, Bcl-W, and Mcl-1) and an inducer of the pro-apoptotic proteins noxa and puma. It induces apoptosis in drug-resistant multiple myeloma cell lines. Apoptosis is activated by the mitochondrial pathway. |
| AT-101 | 5 mg | BVN-2380-5 | page | data sheet | AT-101 is the R-(-) enantiomer of Gossypol that acts as an inhibitor of the antiapoptotic Bcl proteins (Bcl-2, Bcl-XL, Bcl-W, and Mcl-1) and an inducer of the pro-apoptotic proteins noxa and puma. It induces apoptosis in drug-resistant multiple myeloma cell lines. Apoptosis is activated by the mitochondrial pathway. |
| Atpenin A5 | 1 mg | AG-CN2-0100-M001 | page | data sheet | C15H21Cl2NO5. CAS: 119509-24-9. MW: 366.2. Antibiotic. Antifungal. Potent and specific mitochondrial complex II (succinate-ubiquinone oxidoreductase) inhibitor. Mitochondrial ATP-sensitive potassium (mK(ATP)) channel activator. Cardioprotective. Modulates mitochondrial ROS generation during cardioprotection. |
| Atpenin A5 | 250 µg | AG-CN2-0100-C250 | page | data sheet | C15H21Cl2NO5. CAS: 119509-24-9. MW: 366.2. Antibiotic. Antifungal. Potent and specific mitochondrial complex II (succinate-ubiquinone oxidoreductase) inhibitor. Mitochondrial ATP-sensitive potassium (mK(ATP)) channel activator. Cardioprotective. Modulates mitochondrial ROS generation during cardioprotection. |
| Atpenin A5 (Synthetic) | 1 mg | BVN-2210-1000 | page | data sheet | Synthetic. Originally isolated from Penicillium sp. strain. An antibiotic and antifungal agent. Potent and specific mitochondrial complex II (succinate-ubiquinone oxidoreductase) inhibitor and mitochondrial ATP-sensitive potassium (mK(ATP)) channel activator. Modulates mitochondrial ROS generation during cardioprotection. |
| Atpenin A5 (Synthetic) | 250 µg | BVN-2210-250 | page | data sheet | Synthetic. Originally isolated from Penicillium sp. strain. An antibiotic and antifungal agent. Potent and specific mitochondrial complex II (succinate-ubiquinone oxidoreductase) inhibitor and mitochondrial ATP-sensitive potassium (mK(ATP)) channel activator. Modulates mitochondrial ROS generation during cardioprotection. |
| Atractyloside (potassium salt) | 1 mg | CAY-14804-1 | page | data sheet | A natural heteroglucoside that blocks mitochondrial ADP/ATP translocases, inhibiting oxidative phosphorylation; binds with high affinity (Kd in the nanomolar range) to carrier sites on ADP/ATP translocases that are accessible from the intermembrane space |
| Atractyloside (potassium salt) | 500 µg | CAY-14804-500 | page | data sheet | A natural heteroglucoside that blocks mitochondrial ADP/ATP translocases, inhibiting oxidative phosphorylation; binds with high affinity (Kd in the nanomolar range) to carrier sites on ADP/ATP translocases that are accessible from the intermembrane space |
| Auranofin | 50 mg | BVN-2219-50 | page | data sheet | An anti-arthritic drug that inhibits various leukocyte activation pathways at multiple sites. Inhibits release of inflammatory mediators from human basophils, pulmonary mast cells and macrophages. Also inhibits human neutrophil 5-lipoxygenase. Inhibits IκB kinase (IKK) by modifying Cys179 of the IKKß subunit. Efficient inducer of mitochondrial membrane permeability transition via the inhibition of mitochondrial thioredoxin reductase (TrxR). |
| Auranofin | 10 mg | BVN-2219-10 | page | data sheet | An anti-arthritic drug that inhibits various leukocyte activation pathways at multiple sites. Inhibits release of inflammatory mediators from human basophils, pulmonary mast cells and macrophages. Also inhibits human neutrophil 5-lipoxygenase. Inhibits IκB kinase (IKK) by modifying Cys179 of the IKKß subunit. Efficient inducer of mitochondrial membrane permeability transition via the inhibition of mitochondrial thioredoxin reductase (TrxR). |
| Bakuchiol | 5 mg | BVN-2494-5 | page | data sheet | Isolated from plant Psoralea corylifolia. Acts as an inhibitor of protein tyrosine phosphatase 1B (PTB1B (IC₅₀ = 20.8±1.9 µM). Antioxidant and an inhibitor of mitochondrial lipid peroxidation. Also inhibits inducible nitric oxide synthase (iNOS; NOS II) expression. DNA polymerase inhibitor. Shows antimicrobial and cytotoxic activity. |
| Bakuchiol | 1 mg | BVN-2494-1 | page | data sheet | Isolated from plant Psoralea corylifolia. Acts as an inhibitor of protein tyrosine phosphatase 1B (PTB1B (IC₅₀ = 20.8±1.9 µM). Antioxidant and an inhibitor of mitochondrial lipid peroxidation. Also inhibits inducible nitric oxide synthase (iNOS; NOS II) expression. DNA polymerase inhibitor. Shows antimicrobial and cytotoxic activity. |
| BCl-2 Inhibitor GX15-070 | 5 mg | BVN-2040-5 | page | data sheet | Cell-permeable. A small molecule pan–Bcl-2 antagonist that mimics BH3-only proteins by binding to multiple antiapoptotic Bcl-2 members. GX15-070 has been shown to overcome Bcl-2–, Bcl-xl–, Bcl-w–, and Mcl-1–mediated resistance to Bax or Bak. It potently interferes with the direct interaction between Mcl-1 and Bak in intact outer mitochondrial membrane and inhibits the association between Mcl-1 and Bak in intact cells. |
| Beauvericin | 5 mg | AG-CN2-0043-M005 | page | data sheet | C45H57N3O9. CAS: 26048-05-5. MW: 784. Antibiotic. Apoptosis inducer. Acyl-CoA:cholesterol acyltransferase (ACAT) inhibitor. Anticancer compound. Antihaptotactic and antimetastatic. Antiangiogenic compound. Antibacterial, antiprotozal, antiviral and antifungal compound. Shows ionophoric properties. Cytotoxic. Genotoxic. Potently interacts with ABCB1 and ABCG2 transport functions. Causes mitochondrial dysfunction. |
| Beauvericin | 1 mg | AG-CN2-0043-M001 | page | data sheet | C45H57N3O9. CAS: 26048-05-5. MW: 784. Antibiotic. Apoptosis inducer. Acyl-CoA:cholesterol acyltransferase (ACAT) inhibitor. Anticancer compound. Antihaptotactic and antimetastatic. Antiangiogenic compound. Antibacterial, antiprotozal, antiviral and antifungal compound. Shows ionophoric properties. Cytotoxic. Genotoxic. Potently interacts with ABCB1 and ABCG2 transport functions. Causes mitochondrial dysfunction. |
| Betulinic acid | 100 mg | BPS-27739-3 | page | Betulinic acid is a natural pentacyclic triterpenoid that selectively induces apoptosis in tumor cells by directly activating the mitochondrial pathway of apoptosis through a p53- and CD95-independent mechanism. Betulinic acid also displays TGR5 agonist activity (EC50 =1.04 µM). Betulinic acid is used to study its potential cardiovascular role in the modulation of endothelium-dependent relaxation. Betulinic acid displays anti-HIV and antitumor activity. | |
| Betulinic acid | 50 mg | BPS-27739-2 | page | Betulinic acid is a natural pentacyclic triterpenoid that selectively induces apoptosis in tumor cells by directly activating the mitochondrial pathway of apoptosis through a p53- and CD95-independent mechanism. Betulinic acid also displays TGR5 agonist activity (EC50 =1.04 µM). Betulinic acid is used to study its potential cardiovascular role in the modulation of endothelium-dependent relaxation. Betulinic acid displays anti-HIV and antitumor activity. | |
| Betulinic acid | 25 mg | BPS-27739-1 | page | Betulinic acid is a natural pentacyclic triterpenoid that selectively induces apoptosis in tumor cells by directly activating the mitochondrial pathway of apoptosis through a p53- and CD95-independent mechanism. Betulinic acid also displays TGR5 agonist activity (EC50 =1.04 µM). Betulinic acid is used to study its potential cardiovascular role in the modulation of endothelium-dependent relaxation. Betulinic acid displays anti-HIV and antitumor activity. | |
| Bilobalide | 10 mg | AG-CN2-0026-M010 | page | data sheet | C15H18O8. CAS: 33570-04-6. MW: 326.3. Neuroprotective. Mitochondrial gene expression regulator. ROS scavenger. Competitive GABA(A) receptor antagonist. Apoptosis inhibitor. CREB phosphorylation enhancer. Stimulates neurogenesis and synaptogenesis. Hepatic cytochrome P450 inducer. Activates the phosphatidylinositol 3-kinase (PI3K) dependent pathway. Potent anti-inflammatory and antihyperalgesic agent. |
| Bilobalide | 50 mg | BVN-2028-50 | page | data sheet | A neuroprotective agent and mitochondrial gene regulator. Also acts as a ROS (reactive oxygen species) scavenger and apoptosis inhibitor. In addition, Bilabolide activates the phosphatidylinositol 3-kinase (PI3K) dependent pathway. |
| Bilobalide | 50 mg | AG-CN2-0026-M050 | page | data sheet | C15H18O8. CAS: 33570-04-6. MW: 326.3. Neuroprotective. Mitochondrial gene expression regulator. ROS scavenger. Competitive GABA(A) receptor antagonist. Apoptosis inhibitor. CREB phosphorylation enhancer. Stimulates neurogenesis and synaptogenesis. Hepatic cytochrome P450 inducer. Activates the phosphatidylinositol 3-kinase (PI3K) dependent pathway. Potent anti-inflammatory and antihyperalgesic agent. |
| Bilobalide | 10 mg | BVN-2028-10 | page | data sheet | A neuroprotective agent and mitochondrial gene regulator. Also acts as a ROS (reactive oxygen species) scavenger and apoptosis inhibitor. In addition, Bilabolide activates the phosphatidylinositol 3-kinase (PI3K) dependent pathway. |
| Birinapant | 5 mg | BVN-2597-5 | page | data sheet | Birinapant is a SMAC (synthetic small molecule and peptidomimetic of second mitochondrial-derived activator of caspases) mimetic and IAP (Inhibitor of Apoptosis Protein) antagonist with potential antineoplastic activity. Birinapant binds to and inhibits the activity of IAPs, such as X chromosome-linked IAP (XIAP) and cellular IAPs 1 and 2. Since IAPs shield cancer cells from the apoptosis process, this agent may restore and promote the induction of apoptosis through apoptotic signaling pathways in cancer cells. |
| Birinapant | 1 mg | BVN-2597-1 | page | data sheet | Birinapant is a SMAC (synthetic small molecule and peptidomimetic of second mitochondrial-derived activator of caspases) mimetic and IAP (Inhibitor of Apoptosis Protein) antagonist with potential antineoplastic activity. Birinapant binds to and inhibits the activity of IAPs, such as X chromosome-linked IAP (XIAP) and cellular IAPs 1 and 2. Since IAPs shield cancer cells from the apoptosis process, this agent may restore and promote the induction of apoptosis through apoptotic signaling pathways in cancer cells. |
| Bongkrekic Acid, Triammonium Salt | 100 µg | BVN-1820-100 | page | data sheet | A potent inhibitory ligand of the mitochondrial adenine nucleotide translocase (ANT). Inhibits mitochondrial permeability transition pore opening. Also blocks NMDA receptor-mediated apoptosis of cerebrocortical neurons. |
| Bovine Heart Mitochondria Assay Reagent | 100 µl | CAY-700019-100 | data sheet | ||
| Celastrol | 25 mg | BVN-1940-25 | page | data sheet | Cell-permeable. An Antioxidant, anti-inflammatory and immunosuppressive agent. Suppresses LPS-induced cytokine release in macrophages and monocytes (IC₅₀ = 40 nM for IL-1β and IL-1α, 80 nM for IL-6, 110 nM for prostaglandin E2 and 210 nM for IL-8 and TNF-α). Suppresses nitric oxide (NO) production (IC₅₀ = 230 nM) and LPS-induced NF-κB activation (IC₅₀ = 270 nM). Inhibits chymotrypsin-like activity of 20S proteasome (IC₅₀ = 2.5 µM) and lipid peroxidation induced by ADP and Fe²⁺ in rat liver mitochondria (IC₅₀ = 7 µM). |
| Celastrol | 5 mg | BVN-1940-5 | page | data sheet | Cell-permeable. An Antioxidant, anti-inflammatory and immunosuppressive agent. Suppresses LPS-induced cytokine release in macrophages and monocytes (IC₅₀ = 40 nM for IL-1β and IL-1α, 80 nM for IL-6, 110 nM for prostaglandin E2 and 210 nM for IL-8 and TNF-α). Suppresses nitric oxide (NO) production (IC₅₀ = 230 nM) and LPS-induced NF-κB activation (IC₅₀ = 270 nM). Inhibits chymotrypsin-like activity of 20S proteasome (IC₅₀ = 2.5 µM) and lipid peroxidation induced by ADP and Fe²⁺ in rat liver mitochondria (IC₅₀ = 7 µM). |
| Chelerythrine chloride | 5 mg | BVN-2064-5 | page | data sheet | Cell-permeable. A selective protein kinase C (PKC) inhibitor (IC₅₀ =0.66 µM). Chelerythrine is at least 100-fold more selective for PKCs than for other kinases. It induces apoptotic cell death in polymorphonuclear leukocyte through activation of caspase-3. In addition, Chelerythrine treated cells underwent apoptosis, with features that suggest involvement of the mitochondrial pathway, and through a mechanism that involves inhibition of the anti-apoptotic inhibitor BclXL. |
| Citrinin | 25 mg | AG-CN2-0101-M025 | page | data sheet | C13H14O5. CAS: 518-75-2. MW: 250.3. Antibiotic. Antiprotozoal. Antimicrobial. Cytotoxic and genotoxic in various mammalian cells. Mitochondrial permeability transition pore (MPTP) activator. Apoptosis inducer. ERK and JNK signaling pathways activator. Nephrotoxic mycotoxin. Suppresses NO and iNOS expression via inhibition of the JAK/STAT-1alpha and NF-kappaB signaling pathways. Tubulin polymerization and mitotic spindle assembly inhibitor. Increases reactive oxygen species (ROS). Induces cell cycle arrest at the G0/G1 and G2/M phase. |
| Citrinin | 5 mg | AG-CN2-0101-M005 | page | data sheet | C13H14O5. CAS: 518-75-2. MW: 250.3. Antibiotic. Antiprotozoal. Antimicrobial. Cytotoxic and genotoxic in various mammalian cells. Mitochondrial permeability transition pore (MPTP) activator. Apoptosis inducer. ERK and JNK signaling pathways activator. Nephrotoxic mycotoxin. Suppresses NO and iNOS expression via inhibition of the JAK/STAT-1alpha and NF-kappaB signaling pathways. Tubulin polymerization and mitotic spindle assembly inhibitor. Increases reactive oxygen species (ROS). Induces cell cycle arrest at the G0/G1 and G2/M phase. |
| Citrinin | 1 mg | AG-CN2-0101-M001 | page | data sheet | C13H14O5. CAS: 518-75-2. MW: 250.3. Antibiotic. Antiprotozoal. Antimicrobial. Cytotoxic and genotoxic in various mammalian cells. Mitochondrial permeability transition pore (MPTP) activator. Apoptosis inducer. ERK and JNK signaling pathways activator. Nephrotoxic mycotoxin. Suppresses NO and iNOS expression via inhibition of the JAK/STAT-1alpha and NF-kappaB signaling pathways. Tubulin polymerization and mitotic spindle assembly inhibitor. Increases reactive oxygen species (ROS). Induces cell cycle arrest at the G0/G1 and G2/M phase. |
| Coenzyme Q9 | 500 µg | CAY-16866-500 | page | data sheet | A nine isoprenyl group-containing member of the mitochondrial ubiquinone family thought to be necessary for the biosynthesis of CoQ10 in humans; enables electron transport through the mitochondrial respiratory chain and demonstrates antioxidant functions in mice and C. elegans |
| Coenzyme Q9 | 5 mg | CAY-16866-5 | page | data sheet | A nine isoprenyl group-containing member of the mitochondrial ubiquinone family thought to be necessary for the biosynthesis of CoQ10 in humans; enables electron transport through the mitochondrial respiratory chain and demonstrates antioxidant functions in mice and C. elegans |
| Coenzyme Q9 | 10 mg | CAY-16866-10 | page | data sheet | A nine isoprenyl group-containing member of the mitochondrial ubiquinone family thought to be necessary for the biosynthesis of CoQ10 in humans; enables electron transport through the mitochondrial respiratory chain and demonstrates antioxidant functions in mice and C. elegans |
| Coenzyme Q9 | 1 mg | CAY-16866-1 | page | data sheet | A nine isoprenyl group-containing member of the mitochondrial ubiquinone family thought to be necessary for the biosynthesis of CoQ10 in humans; enables electron transport through the mitochondrial respiratory chain and demonstrates antioxidant functions in mice and C. elegans |
| Cyclosporin A | 1 g | AG-CN2-0079-G001 | page | data sheet | C62H111N11O12. CAS: 59865-13-3. MW: 1202.6. Potent immunosuppressant (same as FK-506 (Prod. No. AG-CN2-0047) and rapamycin (Prod. No. AG-CN2-0025)). Forms a complex with cyclophilin. Inhibits the activity of the calcium/calmodulin-dependent protein phosphatase 2B (PP2B; calcineurin). Prevents the dephosphorylation of nuclear factor of activated T cells (NFAT) transcription factor, leading to disruption of T cell activation. Suppresses proliferation of cytotoxic T cells and inhibits the production of T cell-derived mediators such as interleukin-2 (IL-2). Prevents rejection of transplanted organs. Anti-inflammatory compound in the treatment of several inflammatory skin diseases (e. g. atopic dermatitis) and with potential anti-rheumatic activity (rheumatoid arthritis). Antibacterial. Antifungal. Antiparasitic. Apoptosis inhibitor. Inhibits the mitochondrial permeability transition pore (MPTP) from opening, thus inhibiting cytochrome c release. NF-kappaB suppressor by induction of unfolded protein response (UPR). Anti-cancer compound. Apoptosis and autophagy inducer. Inhibits nitric oxide synthesis induced by interleukin-1alpha, lipopolysaccharides and TNF-alpha. Potently induces highly cardiogenic progenitors from embryonic stem (ES) cells. |
| Cyclosporin A | 100 mg | AG-CN2-0079-M100 | page | data sheet | C62H111N11O12. CAS: 59865-13-3. MW: 1202.6. Potent immunosuppressant (same as FK-506 (Prod. No. AG-CN2-0047) and rapamycin (Prod. No. AG-CN2-0025)). Forms a complex with cyclophilin. Inhibits the activity of the calcium/calmodulin-dependent protein phosphatase 2B (PP2B; calcineurin). Prevents the dephosphorylation of nuclear factor of activated T cells (NFAT) transcription factor, leading to disruption of T cell activation. Suppresses proliferation of cytotoxic T cells and inhibits the production of T cell-derived mediators such as interleukin-2 (IL-2). Prevents rejection of transplanted organs. Anti-inflammatory compound in the treatment of several inflammatory skin diseases (e. g. atopic dermatitis) and with potential anti-rheumatic activity (rheumatoid arthritis). Antibacterial. Antifungal. Antiparasitic. Apoptosis inhibitor. Inhibits the mitochondrial permeability transition pore (MPTP) from opening, thus inhibiting cytochrome c release. NF-kappaB suppressor by induction of unfolded protein response (UPR). Anti-cancer compound. Apoptosis and autophagy inducer. Inhibits nitric oxide synthesis induced by interleukin-1alpha, lipopolysaccharides and TNF-alpha. Potently induces highly cardiogenic progenitors from embryonic stem (ES) cells. |
| Cyclosporin A | 5 x 100 mg | AG-CN2-0079-5100 | page | data sheet | C62H111N11O12. CAS: 59865-13-3. MW: 1202.6. Potent immunosuppressant (same as FK-506 (Prod. No. AG-CN2-0047) and rapamycin (Prod. No. AG-CN2-0025)). Forms a complex with cyclophilin. Inhibits the activity of the calcium/calmodulin-dependent protein phosphatase 2B (PP2B; calcineurin). Prevents the dephosphorylation of nuclear factor of activated T cells (NFAT) transcription factor, leading to disruption of T cell activation. Suppresses proliferation of cytotoxic T cells and inhibits the production of T cell-derived mediators such as interleukin-2 (IL-2). Prevents rejection of transplanted organs. Anti-inflammatory compound in the treatment of several inflammatory skin diseases (e. g. atopic dermatitis) and with potential anti-rheumatic activity (rheumatoid arthritis). Antibacterial. Antifungal. Antiparasitic. Apoptosis inhibitor. Inhibits the mitochondrial permeability transition pore (MPTP) from opening, thus inhibiting cytochrome c release. NF-kappaB suppressor by induction of unfolded protein response (UPR). Anti-cancer compound. Apoptosis and autophagy inducer. Inhibits nitric oxide synthesis induced by interleukin-1alpha, lipopolysaccharides and TNF-alpha. Potently induces highly cardiogenic progenitors from embryonic stem (ES) cells. |
| DAF-2 | 10 mg | CDX-D0084-M010 | page | data sheet | C20H14N2O5. CAS: 205391-01-1. MW: 362.34. DAF-2 is highly sensitive reagent for NO detection and determination of nitric oxide synthase activity. DAF-2, however, remains essentially nonfluorescent until it reacts with the nitrosonium cation (produced by spontaneous oxidation of nitric oxide) to form a fluorescent heterocycle, which becomes trapped in the cell's cytoplasm. This sensitive fluorescent probe has been used to identify individual nitric oxide-producing neurons in brain slices, in mitochondria and in living plant cells. |
| DAF-2 | 1 mg | CDX-D0084-M001 | page | data sheet | C20H14N2O5. CAS: 205391-01-1. MW: 362.34. DAF-2 is highly sensitive reagent for NO detection and determination of nitric oxide synthase activity. DAF-2, however, remains essentially nonfluorescent until it reacts with the nitrosonium cation (produced by spontaneous oxidation of nitric oxide) to form a fluorescent heterocycle, which becomes trapped in the cell's cytoplasm. This sensitive fluorescent probe has been used to identify individual nitric oxide-producing neurons in brain slices, in mitochondria and in living plant cells. |
| DAF-2 | 5 mg | CDX-D0084-M005 | page | data sheet | C20H14N2O5. CAS: 205391-01-1. MW: 362.34. DAF-2 is highly sensitive reagent for NO detection and determination of nitric oxide synthase activity. DAF-2, however, remains essentially nonfluorescent until it reacts with the nitrosonium cation (produced by spontaneous oxidation of nitric oxide) to form a fluorescent heterocycle, which becomes trapped in the cell's cytoplasm. This sensitive fluorescent probe has been used to identify individual nitric oxide-producing neurons in brain slices, in mitochondria and in living plant cells. |
| Daunorubicin.HCl | 500 mg | BVN-1524-500 | page | data sheet | Potent anti-cancer agent whose potential target site may be mitochondrial cytochrome c oxidase. Inhibits RNA and DNA synthesis. Also inhibits eukaryotic topoisomerase I & II. Induces DNA single strand breaks and apoptosis in HeLaS3 tumor cells. |
| Daunorubicin.HCl | 10 mg | BVN-1524-10 | page | data sheet | Potent anti-cancer agent whose potential target site may be mitochondrial cytochrome c oxidase. Inhibits RNA and DNA synthesis. Also inhibits eukaryotic topoisomerase I & II. Induces DNA single strand breaks and apoptosis in HeLaS3 tumor cells. |
| Daunorubicin.HCl | 50 mg | BVN-1524-50 | page | data sheet | Potent anti-cancer agent whose potential target site may be mitochondrial cytochrome c oxidase. Inhibits RNA and DNA synthesis. Also inhibits eukaryotic topoisomerase I & II. Induces DNA single strand breaks and apoptosis in HeLaS3 tumor cells. |
| Decylubiquinone | 1 mg | BVN-2099-1 | page | data sheet | A synthetic substrate of cytochrome and mitochondrial permeability transition pore (MPTP) inhibitor. |
| Decylubiquinone | 10 mg | BVN-2099-10 | page | data sheet | A synthetic substrate of cytochrome and mitochondrial permeability transition pore (MPTP) inhibitor. |
| Dihydrorhodamine 123 | 125 mg | CDX-D0134-M125 | page | data sheet | C21H18N2O3. CAS: 109244-58-8. MW: 346.38. Cell-permeable non-fluorescent reactive oxygen species (ROS) indicator. Passively diffuse across membranes where it is oxidized by peroxynitrite to rhodamine 123 which localizes in the mitochondria and exhibits green fluorescence (Ex/Em wavelengths of 500 and 536 nm). Used to investigate reactive oxygen intermediates produced by human and murine phagocytes, activated rat mast cells and cultured endothelial cells. In addition, it has been used together with Fura Red calcium indicator to simultaneously measure oxidative bursts and Ca2+ fluxes in monocytes and granulocytes. Dihydrorhodamine 123 has been shown to be a more sensitive probe than H2DCFDA for detecting granulocyte respiratory bursts. |
| Dihydrorhodamine 123 | 2 mg | CDX-D0134-M002 | page | data sheet | C21H18N2O3. CAS: 109244-58-8. MW: 346.38. Cell-permeable non-fluorescent reactive oxygen species (ROS) indicator. Passively diffuse across membranes where it is oxidized by peroxynitrite to rhodamine 123 which localizes in the mitochondria and exhibits green fluorescence (Ex/Em wavelengths of 500 and 536 nm). Used to investigate reactive oxygen intermediates produced by human and murine phagocytes, activated rat mast cells and cultured endothelial cells. In addition, it has been used together with Fura Red calcium indicator to simultaneously measure oxidative bursts and Ca2+ fluxes in monocytes and granulocytes. Dihydrorhodamine 123 has been shown to be a more sensitive probe than H2DCFDA for detecting granulocyte respiratory bursts. |
| Dihydrorhodamine 123 | 10 mg | CDX-D0134-M010 | page | data sheet | C21H18N2O3. CAS: 109244-58-8. MW: 346.38. Cell-permeable non-fluorescent reactive oxygen species (ROS) indicator. Passively diffuse across membranes where it is oxidized by peroxynitrite to rhodamine 123 which localizes in the mitochondria and exhibits green fluorescence (Ex/Em wavelengths of 500 and 536 nm). Used to investigate reactive oxygen intermediates produced by human and murine phagocytes, activated rat mast cells and cultured endothelial cells. In addition, it has been used together with Fura Red calcium indicator to simultaneously measure oxidative bursts and Ca2+ fluxes in monocytes and granulocytes. Dihydrorhodamine 123 has been shown to be a more sensitive probe than H2DCFDA for detecting granulocyte respiratory bursts. |
| Dynasore | 5 mg | BVN-1900-5 | page | data sheet | Cell-permeable. A reversible, noncompetitive inhibitor of dynamin that interferes in vitro with the GTPase activity of dynamin1, dynamin2, and Drp1, the mitochondrial dynamin, but not of other small GTPases. Dynasore acts as a potent inhibitor of endocytic pathways known to depend on dynamin by rapidly blocking coated vesicle formation within seconds of dynasore addition. |
| Dynasore | 25 mg | BVN-1900-25 | page | data sheet | Cell-permeable. A reversible, noncompetitive inhibitor of dynamin that interferes in vitro with the GTPase activity of dynamin1, dynamin2, and Drp1, the mitochondrial dynamin, but not of other small GTPases. Dynasore acts as a potent inhibitor of endocytic pathways known to depend on dynamin by rapidly blocking coated vesicle formation within seconds of dynasore addition. |
| Elesclomol (STA-4783) | 5 mg | BPS-27748-1 | page | Elesclomol is a HSP-90 Inhibitor with pro-apoptotic and potential antineoplastic activities. Elesclomol induces oxidative stress and triggers mitochondrial-induced apoptosis in cancer cells. | |
| Elesclomol (STA-4783) | 10 mg | BPS-27748-2 | page | Elesclomol induces oxidative stress and triggers mitochondrial-induced apoptosis in cancer cells. | |
| Erastin | 1 mg | BVN-2231-1 | page | data sheet | Erastin is a selective antitumor agent that displays greater lethality in human tumour cells harbouring mutations in the oncogenes HRAS, KRAS or BRAF. It binds to mitochondrial volatage-dependent anion channels (VDAC) proteins, more specifically on VDAC2 and alters its gating. Erastin rapidly induces an oxidative, non-apoptotic cell death in several human tumors harboring activating mutations in the RAS-RAF-MEK signaling. |
| Erastin | 5 mg | BVN-2231-5 | page | data sheet | Erastin is a selective antitumor agent that displays greater lethality in human tumour cells harbouring mutations in the oncogenes HRAS, KRAS or BRAF. It binds to mitochondrial volatage-dependent anion channels (VDAC) proteins, more specifically on VDAC2 and alters its gating. Erastin rapidly induces an oxidative, non-apoptotic cell death in several human tumors harboring activating mutations in the RAS-RAF-MEK signaling. |
| FCCP | 5 mg | BVN-2398-5 | page | data sheet | FCCP is a potent and reversible inhibitor of mitochondrial oxidative phosphorylation. It depolarizes mitochondrial membrane potential and induces apoptosis |
| FCCP | 25 mg | BVN-2398-25 | page | data sheet | FCCP is a potent and reversible inhibitor of mitochondrial oxidative phosphorylation. It depolarizes mitochondrial membrane potential and induces apoptosis |
| Ferulenol | 10 mg | AG-CN2-0011-M010 | page | data sheet | C24H30O3. CAS: 6805-34-1. MW: 366.5. Prenylated 4-hydroxycoumarin. Anti-tumor compound. Cytotoxic. Stimulator of tubulin polymerisation in vitro. Inhibitor of colchicine binding to tubulin. Antitubercular antibiotic with potent antibacterial activity. Anti-coagulant, pro-haemorrhagic compound with higher activity than warfarin. Shows hepatocyte toxicity. Disrupts mitochondrial membrane potential. |
| Ferulenol | 1 mg | AG-CN2-0011-M001 | page | data sheet | C24H30O3. CAS: 6805-34-1. MW: 366.5. Prenylated 4-hydroxycoumarin. Anti-tumor compound. Cytotoxic. Stimulator of tubulin polymerisation in vitro. Inhibitor of colchicine binding to tubulin. Antitubercular antibiotic with potent antibacterial activity. Anti-coagulant, pro-haemorrhagic compound with higher activity than warfarin. Shows hepatocyte toxicity. Disrupts mitochondrial membrane potential. |
| Ferulenol | 5 mg | AG-CN2-0011-M005 | page | data sheet | C24H30O3. CAS: 6805-34-1. MW: 366.5. Prenylated 4-hydroxycoumarin. Anti-tumor compound. Cytotoxic. Stimulator of tubulin polymerisation in vitro. Inhibitor of colchicine binding to tubulin. Antitubercular antibiotic with potent antibacterial activity. Anti-coagulant, pro-haemorrhagic compound with higher activity than warfarin. Shows hepatocyte toxicity. Disrupts mitochondrial membrane potential. |
| Ferutinin (high purity) | 1 mg | AG-CN2-0007-M001 | page | data sheet | C22H30O4. CAS: 41743-44-6. MW: 358.5. Potent, naturally occuring non-steroid estrogenic compound. Tool to promote mitochondrial calcium overload and to promote calcium-dependent opening of the mitochondrial permeability transition pore (mPTP). Strong agonist for estrogen receptor (ER)alpha and agonist/antagonist for ERbeta. Calcium ionophoretic. Antiproliferative. Increases nitric oxide synthase activity and phosphoinositides breakdown in nervous tissue. Shows aphrodisiac and anti-sexual impotence activities. Anti-osteoporotic. Prevents osteoporosis caused by severe estrogen deficiency. Modest AChE inhibitor. |
| Ferutinin (high purity) | 10 mg | AG-CN2-0007-M010 | page | data sheet | C22H30O4. CAS: 41743-44-6. MW: 358.5. Potent, naturally occuring non-steroid estrogenic compound. Tool to promote mitochondrial calcium overload and to promote calcium-dependent opening of the mitochondrial permeability transition pore (mPTP). Strong agonist for estrogen receptor (ER)alpha and agonist/antagonist for ERbeta. Calcium ionophoretic. Antiproliferative. Increases nitric oxide synthase activity and phosphoinositides breakdown in nervous tissue. Shows aphrodisiac and anti-sexual impotence activities. Anti-osteoporotic. Prevents osteoporosis caused by severe estrogen deficiency. Modest AChE inhibitor. |
| Ferutinin (high purity) | 5 mg | AG-CN2-0007-M005 | page | data sheet | C22H30O4. CAS: 41743-44-6. MW: 358.5. Potent, naturally occuring non-steroid estrogenic compound. Tool to promote mitochondrial calcium overload and to promote calcium-dependent opening of the mitochondrial permeability transition pore (mPTP). Strong agonist for estrogen receptor (ER)alpha and agonist/antagonist for ERbeta. Calcium ionophoretic. Antiproliferative. Increases nitric oxide synthase activity and phosphoinositides breakdown in nervous tissue. Shows aphrodisiac and anti-sexual impotence activities. Anti-osteoporotic. Prevents osteoporosis caused by severe estrogen deficiency. Modest AChE inhibitor. |
| Forskolin | 1 mg | AG-CN2-0089-M001 | page | data sheet | C22H34O7. CAS: 66428-89-5 | 66575-29-9. MW: 410.5. Potent, cell permeable adenylyl cyclase activator. Increases intracellular cAMP levels. Widely used tool to investigate cAMP as a second messenger. Inotropic and antihypertensive. Smooth muscle relaxant/vasodilator. Glucose transporter inhibitor. Platelet aggregation inhibitor. Stimulates lipolysis in fat cells. Non-competitive nicotinic acetylcholine receptors inhibitor. MAP kinase inhibitor. Upregulates mitochondrial uncoupling protein (UCP) mRNA levels in brown adipose tissue. Autophagy inhibitor. Hedgehog signaling inhibitor. Has antiglaucoma potential. Promotes neuronal differentiation of NSCs. |
| Forskolin | 5 mg | AG-CN2-0089-M005 | page | data sheet | C22H34O7. CAS: 66428-89-5 | 66575-29-9. MW: 410.5. Potent, cell permeable adenylyl cyclase activator. Increases intracellular cAMP levels. Widely used tool to investigate cAMP as a second messenger. Inotropic and antihypertensive. Smooth muscle relaxant/vasodilator. Glucose transporter inhibitor. Platelet aggregation inhibitor. Stimulates lipolysis in fat cells. Non-competitive nicotinic acetylcholine receptors inhibitor. MAP kinase inhibitor. Upregulates mitochondrial uncoupling protein (UCP) mRNA levels in brown adipose tissue. Autophagy inhibitor. Hedgehog signaling inhibitor. Has antiglaucoma potential. Promotes neuronal differentiation of NSCs. |
| Forskolin | 25 mg | AG-CN2-0089-M025 | page | data sheet | C22H34O7. CAS: 66428-89-5 | 66575-29-9. MW: 410.5. Potent, cell permeable adenylyl cyclase activator. Increases intracellular cAMP levels. Widely used tool to investigate cAMP as a second messenger. Inotropic and antihypertensive. Smooth muscle relaxant/vasodilator. Glucose transporter inhibitor. Platelet aggregation inhibitor. Stimulates lipolysis in fat cells. Non-competitive nicotinic acetylcholine receptors inhibitor. MAP kinase inhibitor. Upregulates mitochondrial uncoupling protein (UCP) mRNA levels in brown adipose tissue. Autophagy inhibitor. Hedgehog signaling inhibitor. Has antiglaucoma potential. Promotes neuronal differentiation of NSCs. |
| Forskolin | 50 mg | AG-CN2-0089-M050 | page | data sheet | C22H34O7. CAS: 66428-89-5 | 66575-29-9. MW: 410.5. Potent, cell permeable adenylyl cyclase activator. Increases intracellular cAMP levels. Widely used tool to investigate cAMP as a second messenger. Inotropic and antihypertensive. Smooth muscle relaxant/vasodilator. Glucose transporter inhibitor. Platelet aggregation inhibitor. Stimulates lipolysis in fat cells. Non-competitive nicotinic acetylcholine receptors inhibitor. MAP kinase inhibitor. Upregulates mitochondrial uncoupling protein (UCP) mRNA levels in brown adipose tissue. Autophagy inhibitor. Hedgehog signaling inhibitor. Has antiglaucoma potential. Promotes neuronal differentiation of NSCs. |
| Fuscin | 2.5 mg | AG-CN2-0138-MM25 | page | data sheet | C15H16O5. CAS: 83-85-2. MW: 276.3. Mycotoxin. Antibacterial agent. ADP transport inhibitor. Mitochondrial respiration and oxidative phosphorylation inhibitor. Human CCR5 receptor antagonist. Anti-HIV compound. |
| Fuscin | 1 mg | AG-CN2-0138-M001 | page | data sheet | C15H16O5. CAS: 83-85-2. MW: 276.3. Mycotoxin. Antibacterial agent. ADP transport inhibitor. Mitochondrial respiration and oxidative phosphorylation inhibitor. Human CCR5 receptor antagonist. Anti-HIV compound. |
| Ganglioside GD3 . disodium salt (bovine brain) | 1 mg | AG-CN2-9005-M001 | page | data sheet | C70H123N3O29 . 2Na. CAS: 62010-37-1. MW: 1470.8 . 46.0 (calculated on sphingosine C18:1 and stearic acid). Gangliosides are acidic glycosphingolipids that form lipid rafts in the outer leaflet of the cell plasma membrane, especially in neuronal cells in the central nervous system. They participate in cellular proliferation, differentiation, adhesion, signal transduction, cell-to-cell interactions, tumorigenesis and metastasis. The accumulation of gangliosides has been linked to several diseases. Ganglioside GD3 induces mitochondrial permeability transition (MPT) without requiring elevated Ca2+ levels and thus triggers Fas-mediated apoptosis. It modulates the activity of Src-family tyrosine kinase Lyn and cell apoptosis. It is involved in several tumor processes and is high abundant in proliferating cells and in the first stage of neuronal differentiation. |
| Ganglioside GD3 . disodium salt (bovine brain) | 500 µg | AG-CN2-9005-C500 | page | data sheet | C70H123N3O29 . 2Na. CAS: 62010-37-1. MW: 1470.8 . 46.0 (calculated on sphingosine C18:1 and stearic acid). Gangliosides are acidic glycosphingolipids that form lipid rafts in the outer leaflet of the cell plasma membrane, especially in neuronal cells in the central nervous system. They participate in cellular proliferation, differentiation, adhesion, signal transduction, cell-to-cell interactions, tumorigenesis and metastasis. The accumulation of gangliosides has been linked to several diseases. Ganglioside GD3 induces mitochondrial permeability transition (MPT) without requiring elevated Ca2+ levels and thus triggers Fas-mediated apoptosis. It modulates the activity of Src-family tyrosine kinase Lyn and cell apoptosis. It is involved in several tumor processes and is high abundant in proliferating cells and in the first stage of neuronal differentiation. |
| GSH-OEt | 5 g | CDX-G0006-G005 | page | data sheet | C12H21N3O6S. CAS: 92614-59-0. MW: 335.38. GSH-OEt is cellpermeable and has been used to protect cells against radiation damage, oxidants and various toxic compounds including heavy metals. GSH-OEt is a protective agent against cellular damage, such as cataracts and mitochondrial degeneration. It undergoes hydrolysis by intracellular esterases thereby increasing intracellular GSH concentration in many tissues and cell types. Glutathione monoethyl ester may be used to supplement cellular pools of GSH in vitro and in vivo and can prevent ROS formation, neutralize toxic products and block apoptosis pathway. The effect of glutathione (GSH) and glutathione ethyl ester (GSH-OEt) supplementation on GSH homeostasis and exercise-induced oxidative stress was also examined. Glutathione ethyl ester protects against cisplatin-induced ototoxicity in the rat. |
| GSH-OEt | 100 mg | CDX-G0006-M100 | page | data sheet | C12H21N3O6S. CAS: 92614-59-0. MW: 335.38. GSH-OEt is cellpermeable and has been used to protect cells against radiation damage, oxidants and various toxic compounds including heavy metals. GSH-OEt is a protective agent against cellular damage, such as cataracts and mitochondrial degeneration. It undergoes hydrolysis by intracellular esterases thereby increasing intracellular GSH concentration in many tissues and cell types. Glutathione monoethyl ester may be used to supplement cellular pools of GSH in vitro and in vivo and can prevent ROS formation, neutralize toxic products and block apoptosis pathway. The effect of glutathione (GSH) and glutathione ethyl ester (GSH-OEt) supplementation on GSH homeostasis and exercise-induced oxidative stress was also examined. Glutathione ethyl ester protects against cisplatin-induced ototoxicity in the rat. |
| GSH-OEt | 500 mg | CDX-G0006-M500 | page | data sheet | C12H21N3O6S. CAS: 92614-59-0. MW: 335.38. GSH-OEt is cellpermeable and has been used to protect cells against radiation damage, oxidants and various toxic compounds including heavy metals. GSH-OEt is a protective agent against cellular damage, such as cataracts and mitochondrial degeneration. It undergoes hydrolysis by intracellular esterases thereby increasing intracellular GSH concentration in many tissues and cell types. Glutathione monoethyl ester may be used to supplement cellular pools of GSH in vitro and in vivo and can prevent ROS formation, neutralize toxic products and block apoptosis pathway. The effect of glutathione (GSH) and glutathione ethyl ester (GSH-OEt) supplementation on GSH homeostasis and exercise-induced oxidative stress was also examined. Glutathione ethyl ester protects against cisplatin-induced ototoxicity in the rat. |
| Harzianopyridone | 250 µg | AG-CN2-0149-C250 | page | data sheet | C14H19NO5. CAS: 126637-69-2. MW: 281.3. Antibiotic. Antifungal and antibacterial compound. Specific mitochondrial complex II (succinate ubiquinone oxidoreductase; succinate dehydrogenase) inhibitor. Herbicidal activity. Anthelmintic compound. Inhibits NADH-fumarate reductase activity of adult Ascaris suum mitochondria. |
| Harzianopyridone | 1 mg | AG-CN2-0149-M001 | page | data sheet | C14H19NO5. CAS: 126637-69-2. MW: 281.3. Antibiotic. Antifungal and antibacterial compound. Specific mitochondrial complex II (succinate ubiquinone oxidoreductase; succinate dehydrogenase) inhibitor. Herbicidal activity. Anthelmintic compound. Inhibits NADH-fumarate reductase activity of adult Ascaris suum mitochondria. |
| Hydramethylnon | 100 mg | CDX-H0096-M100 | page | data sheet | C25H24F6N4. CAS: 67485-29-4. MW: 494.5. Insecticide primarily used against cockroaches and ants. Chemical class called trifluoromethyl aminohydrazone, which is a metabolic inhibitor. It works by inhibiting complex III in the mitochondrial inner membrane and leads to a halting of oxidative phosphorylation. Compound can be used as analytical reference material. |
| Hydramethylnon | 1 g | CDX-H0096-G001 | page | data sheet | C25H24F6N4. CAS: 67485-29-4. MW: 494.5. Insecticide primarily used against cockroaches and ants. Chemical class called trifluoromethyl aminohydrazone, which is a metabolic inhibitor. It works by inhibiting complex III in the mitochondrial inner membrane and leads to a halting of oxidative phosphorylation. Compound can be used as analytical reference material. |
| Ingenol-3-angelate | 10 mg | CAY-16207-10 | page | data sheet | A hydrophobic diterpene ester that rapidly induces cell death in proliferating keratinocytes through plasma membrane and mitochondrial disruption; causes inflammation due, at least in part, to activation of PKC, leading to antibody-dependent cellular cytotoxicity |
| Ingenol-3-angelate | 500 µg | CAY-16207-500 | page | data sheet | A hydrophobic diterpene ester that rapidly induces cell death in proliferating keratinocytes through plasma membrane and mitochondrial disruption; causes inflammation due, at least in part, to activation of PKC, leading to antibody-dependent cellular cytotoxicity |
| Ingenol-3-angelate | 5 mg | CAY-16207-5 | page | data sheet | A hydrophobic diterpene ester that rapidly induces cell death in proliferating keratinocytes through plasma membrane and mitochondrial disruption; causes inflammation due, at least in part, to activation of PKC, leading to antibody-dependent cellular cytotoxicity |
| Ingenol-3-angelate | 1 mg | CAY-16207-1 | page | data sheet | A hydrophobic diterpene ester that rapidly induces cell death in proliferating keratinocytes through plasma membrane and mitochondrial disruption; causes inflammation due, at least in part, to activation of PKC, leading to antibody-dependent cellular cytotoxicity |
| IPAM | 1 g | BVN-1817-1000 | page | data sheet | A cell-permeable indole derivative that acts as an antioxidant and mitochondrial metabolism modifier. IPAM binds to the rate-limiting component of oxidative phosphorylation in complex I of the respiratory chain and acts as a stabilizer of energy metabolism, thereby reducing the production of reactive oxygen species (ROS). |
| IPAM | 100 mg | BVN-1817-100 | page | data sheet | A cell-permeable indole derivative that acts as an antioxidant and mitochondrial metabolism modifier. IPAM binds to the rate-limiting component of oxidative phosphorylation in complex I of the respiratory chain and acts as a stabilizer of energy metabolism, thereby reducing the production of reactive oxygen species (ROS). |
| IPAM | 500 mg | BVN-1817-500 | page | data sheet | A cell-permeable indole derivative that acts as an antioxidant and mitochondrial metabolism modifier. IPAM binds to the rate-limiting component of oxidative phosphorylation in complex I of the respiratory chain and acts as a stabilizer of energy metabolism, thereby reducing the production of reactive oxygen species (ROS). |
| Iromycin A | 500 µg | BVT-0262-C500 |
C19H29NO2. CAS: 213137-53-2. MW: 303.4. Pyridone metabolite. Nitric oxide synthase (NOS) inhibitor, showing selectivity for eNOS (NOS III) versus nNOS (NOS I). Thaxtomine biosynthesis inhibitor. Mitochondrial electron transport chain inhibitor. |
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| Iromycin A | 5 mg | BVT-0262-M005 |
C19H29NO2. CAS: 213137-53-2. MW: 303.4. Pyridone metabolite. Nitric oxide synthase (NOS) inhibitor, showing selectivity for eNOS (NOS III) versus nNOS (NOS I). Thaxtomine biosynthesis inhibitor. Mitochondrial electron transport chain inhibitor. |
||
| Iromycin A | 1 mg | BVT-0262-M001 |
C19H29NO2. CAS: 213137-53-2. MW: 303.4. Pyridone metabolite. Nitric oxide synthase (NOS) inhibitor, showing selectivity for eNOS (NOS III) versus nNOS (NOS I). Thaxtomine biosynthesis inhibitor. Mitochondrial electron transport chain inhibitor. |
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| JC-1 | 5 x 1 mg | AG-CR1-3568-5001 | page | data sheet | C25H27Cl4IN4. CAS: 3520-43-2 | 47729-63-5. MW: 652.2. The membrane-permeant dual-emission potential-sensitive JC-1 dye is widely used in apoptosis studies to monitor mitochondrial health by flow cytometry, fluorescence microscopy and in microplate-based fluorescent assays. JC-1 dye can be used as an indicator of mitochondrial membrane potential in a variety of cell types, including myocytes and neurons, as well as in intact tissues and isolated mitochondria. JC-1 accumulates in mitochondria, selectively generating an orange J-aggregate emission profile (590 nm) in healthy cells. After cell injury, as membrane potential decreases, JC-1 monomers are generated, resulting in a shift to green emission (529 nm). The principal advantage of JC-1 relative to other commonly employed fluorescent probes of mitochondrial membrane potential is that it allows qualitative visualization, considering the shift from orange to green fluorescence emission, and quantitative detection, considering the fluorescence intensity ratio. |
| JC-1 | 1 mg | AG-CR1-3568-M001 | page | data sheet | C25H27Cl4IN4. CAS: 3520-43-2 | 47729-63-5. MW: 652.2. The membrane-permeant dual-emission potential-sensitive JC-1 dye is widely used in apoptosis studies to monitor mitochondrial health by flow cytometry, fluorescence microscopy and in microplate-based fluorescent assays. JC-1 dye can be used as an indicator of mitochondrial membrane potential in a variety of cell types, including myocytes and neurons, as well as in intact tissues and isolated mitochondria. JC-1 accumulates in mitochondria, selectively generating an orange J-aggregate emission profile (590 nm) in healthy cells. After cell injury, as membrane potential decreases, JC-1 monomers are generated, resulting in a shift to green emission (529 nm). The principal advantage of JC-1 relative to other commonly employed fluorescent probes of mitochondrial membrane potential is that it allows qualitative visualization, considering the shift from orange to green fluorescence emission, and quantitative detection, considering the fluorescence intensity ratio. |
| JC-1 | 5 mg | BVN-1130-5 | page | data sheet | JC-1 is a mitochondrial dye that stains mitochondria in living cells in a membrane potential-dependent fashion. JC-1 monomer is in equilibrium with so called J-aggregates, which are favored at higher mitochondrial membrane potential. The monomer JC-1 has green fluorescence (lem = 527 nm), while the J-aggregates have red fluorescence (lem = 590 nm). Therefore, it has been possible to use fluorescence ratioing technique to study mitochondrial membrane potential. JC-1 is particularly useful for apoptosis studies. In apoptotic cells, the dye stays in the cytoplasm and fluoresces green, while in healthy cells, the dye aggregates in the mitochondria and fluoresces red. |
| JC-1 | 10 mg | CDX-T0046-M010 | page | data sheet | C25H27Cl4IN4. CAS: 3520-43-2. MW: 652.23. A dual-emission potential-sensitive probe that can be used to measure mitochondrial membrane potential. JC-1 is a green-fluorescent monomer at low membrane potential. At higher potentials, JC-1 forms red-fluorescent "J-aggregates," which exhibit broad excitation and very narrow emission spectra. The ratio of red to green fluorescence of JC-1 is dependent only on membrane potential, and not influenced by mitochondrial size, shape, or density. |
| JC-1 | 100 mg | CDX-T0046-M100 | page | data sheet | C25H27Cl4IN4. CAS: 3520-43-2. MW: 652.23. A dual-emission potential-sensitive probe that can be used to measure mitochondrial membrane potential. JC-1 is a green-fluorescent monomer at low membrane potential. At higher potentials, JC-1 forms red-fluorescent "J-aggregates," which exhibit broad excitation and very narrow emission spectra. The ratio of red to green fluorescence of JC-1 is dependent only on membrane potential, and not influenced by mitochondrial size, shape, or density. |
| JC-1 | 5 mg | AG-CR1-3568-M005 | page | data sheet | C25H27Cl4IN4. CAS: 3520-43-2 | 47729-63-5. MW: 652.2. The membrane-permeant dual-emission potential-sensitive JC-1 dye is widely used in apoptosis studies to monitor mitochondrial health by flow cytometry, fluorescence microscopy and in microplate-based fluorescent assays. JC-1 dye can be used as an indicator of mitochondrial membrane potential in a variety of cell types, including myocytes and neurons, as well as in intact tissues and isolated mitochondria. JC-1 accumulates in mitochondria, selectively generating an orange J-aggregate emission profile (590 nm) in healthy cells. After cell injury, as membrane potential decreases, JC-1 monomers are generated, resulting in a shift to green emission (529 nm). The principal advantage of JC-1 relative to other commonly employed fluorescent probes of mitochondrial membrane potential is that it allows qualitative visualization, considering the shift from orange to green fluorescence emission, and quantitative detection, considering the fluorescence intensity ratio. |
| Kaempferol | 50 mg | BVN-2523-50 | page | data sheet | A naturally occurring polyphenol antioxidant that displays a wide range of pharmacological activities, including antioxidant, anti-inflammatory, antimicrobial, anticancer, cardioprotective, neuroprotective, antidiabetic, anti-osteoporotic, estrogenic/antiestrogenic, anxiolytic, analgesic and antiallergic activities. It reduces cell cycle progression in HT-29 cells. Kaempferol increases chromatin condensation, DNA fragmentation and the number of early apoptotic cells in HT-29 cells in a dose-dependent manner. In addition, kaempferol increases the levels of cleaved caspase-9, caspase-3 and caspase-7 as well as those of cleaved poly (ADP-ribose) polymerase. Moreover, it increases mitochondrial membrane permeability and cytosolic cytochrome c concentrations. |
| Kaempferol | 250 mg | BVN-2523-250 | page | data sheet | A naturally occurring polyphenol antioxidant that displays a wide range of pharmacological activities, including antioxidant, anti-inflammatory, antimicrobial, anticancer, cardioprotective, neuroprotective, antidiabetic, anti-osteoporotic, estrogenic/antiestrogenic, anxiolytic, analgesic and antiallergic activities. It reduces cell cycle progression in HT-29 cells. Kaempferol increases chromatin condensation, DNA fragmentation and the number of early apoptotic cells in HT-29 cells in a dose-dependent manner. In addition, kaempferol increases the levels of cleaved caspase-9, caspase-3 and caspase-7 as well as those of cleaved poly (ADP-ribose) polymerase. Moreover, it increases mitochondrial membrane permeability and cytosolic cytochrome c concentrations. |
| Kaempferol | 20 mg | BPS-27757 | page | Naturally occurring flavonoid found in Gingko biloba and red wines that activates the mitochondrial Ca2+ uniporter (EC50 = 7 µM). Induces caspase-9-mediated apoptosis in a variety of cancer cell lines via downregulation of polo-like kinase 1 (PLK1) expression. Exhibits antioxidant activity and attenuates osteoclastic bone reabsorption in vitro. Pan-HDAC inhibitor; in vitro profiling of all conserved human HDACs of class I, II and IV showed that kaempferol inhibited all tested HDACs. | |
| L-Acetylcarnitine (chloride) | 1 g | CAY-16948-1 | page | data sheet | An acetylated form of L-carnitine that facilitates the uptake of acetyl CoA into mitochondria during fatty acid oxidation, enhances acetylcholine production, and stimulates protein and membrane phospholipid synthesis |
| L-Acetylcarnitine (chloride) | 10 g | CAY-16948-10 | page | data sheet | An acetylated form of L-carnitine that facilitates the uptake of acetyl CoA into mitochondria during fatty acid oxidation, enhances acetylcholine production, and stimulates protein and membrane phospholipid synthesis |
| L-Acetylcarnitine (chloride) | 25 g | CAY-16948-25 | page | data sheet | An acetylated form of L-carnitine that facilitates the uptake of acetyl CoA into mitochondria during fatty acid oxidation, enhances acetylcholine production, and stimulates protein and membrane phospholipid synthesis |
| L-Acetylcarnitine (chloride) | 5 g | CAY-16948-5 | page | data sheet | An acetylated form of L-carnitine that facilitates the uptake of acetyl CoA into mitochondria during fatty acid oxidation, enhances acetylcholine production, and stimulates protein and membrane phospholipid synthesis |
| Levosimendan | 100 mg | CAY-16128-100 | page | data sheet | A calcium sensitizer that causes increased cardiac contractility by binding troponin C (EC50 = 9 nM), promotes vasodilation by activating ATP-sensitive potassium channels on vascular smooth muscle cells (EC50 = 0.28 µM), and performs a cardioprotective function by prompting the opening of mitochondrial potassium channels in cardiomyocytes; also inhibits phosphodiesterases 3 and 4 (IC50s =2.5 nM and 25 µM, respectively) |
| Levosimendan | 250 mg | CAY-16128-250 | page | data sheet | A calcium sensitizer that causes increased cardiac contractility by binding troponin C (EC50 = 9 nM), promotes vasodilation by activating ATP-sensitive potassium channels on vascular smooth muscle cells (EC50 = 0.28 µM), and performs a cardioprotective function by prompting the opening of mitochondrial potassium channels in cardiomyocytes; also inhibits phosphodiesterases 3 and 4 (IC50s =2.5 nM and 25 µM, respectively) |
| Levosimendan | 500 mg | CAY-16128-500 | page | data sheet | A calcium sensitizer that causes increased cardiac contractility by binding troponin C (EC50 = 9 nM), promotes vasodilation by activating ATP-sensitive potassium channels on vascular smooth muscle cells (EC50 = 0.28 µM), and performs a cardioprotective function by prompting the opening of mitochondrial potassium channels in cardiomyocytes; also inhibits phosphodiesterases 3 and 4 (IC50s =2.5 nM and 25 µM, respectively) |
| Levosimendan | 50 mg | CAY-16128-50 | page | data sheet | A calcium sensitizer that causes increased cardiac contractility by binding troponin C (EC50 = 9 nM), promotes vasodilation by activating ATP-sensitive potassium channels on vascular smooth muscle cells (EC50 = 0.28 µM), and performs a cardioprotective function by prompting the opening of mitochondrial potassium channels in cardiomyocytes; also inhibits phosphodiesterases 3 and 4 (IC50s =2.5 nM and 25 µM, respectively) |
| LY573636 | 25 mg | BVN-2297-25 | page | data sheet | A potent anti-tumor agent, which causes growth arrest and apoptosis of a variety of human solid tumors in vitro and in vivo. LY573636-induced apoptosis occurs by a mitochondrial-targeted mechanism. |
| LY573636 | 5 mg | BVN-2297-5 | page | data sheet | A potent anti-tumor agent, which causes growth arrest and apoptosis of a variety of human solid tumors in vitro and in vivo. LY573636-induced apoptosis occurs by a mitochondrial-targeted mechanism. |
| Mdivi -1 | 5 mg | BVN-2441-5 | page | data sheet | Cell-permeable. A selective inhibitor of Dnm1 GTPase (IC₅₀ =1-10 µM). Inhibits mitochondrial outer membrane permeabilization. Inhibits mitochondrial division and apoptosis. |
| Mdivi -1 | 25 mg | BVN-2441-25 | page | data sheet | Cell-permeable. A selective inhibitor of Dnm1 GTPase (IC₅₀ =1-10 µM). Inhibits mitochondrial outer membrane permeabilization. Inhibits mitochondrial division and apoptosis. |
| N4-Acetylsulfamethoxazole | 10 mg | CDX-A0291-M010 | page | data sheet | C12H13N3O4S. CAS: 21312-10-7. MW: 295.3. This is a metabolite of the sulfonamide bacteriostatic antibiotic sulfamethoxazole. Sulfamethoxazole is metabolized via acetylation, catalyzed by liver extramitochondrial N-acetyl transferases. Acetyl-Sulfamethoxazole is excreted in urine. Both compounds can be used as a probe for the molecular percentage enrichement of liver extramitochondrial acetyl-CoA. Acetyl-Sulfamethoxazole can also be used as a reference for sulfamethoxazole impurity and waste determination. |
| N4-Acetylsulfamethoxazole | 50 mg | CDX-A0291-M050 | page | data sheet | C12H13N3O4S. CAS: 21312-10-7. MW: 295.3. This is a metabolite of the sulfonamide bacteriostatic antibiotic sulfamethoxazole. Sulfamethoxazole is metabolized via acetylation, catalyzed by liver extramitochondrial N-acetyl transferases. Acetyl-Sulfamethoxazole is excreted in urine. Both compounds can be used as a probe for the molecular percentage enrichement of liver extramitochondrial acetyl-CoA. Acetyl-Sulfamethoxazole can also be used as a reference for sulfamethoxazole impurity and waste determination. |
| Necrosis Inhibitor, Necrox-2 | 5 mg | BVN-2228-5 | page | data sheet | A cell-permeable necrosis inhibitor that displays antioxidant property. It localizes mostly in the mitochondria. Selectively blocks oxidative stress-induced necrotic cell death (0.1 µM NecroX-2 prevented ~50% cell death in H9C2 cells exposed to 400 µM t-BuOOH for 2 hours). Does not protect against staurosporine or etoposide-induced apoptosis. Protects cells against cold shock, hypoxia and oxidative stress in vitro. |
| Necrosis Inhibitor, Necrox-2 | 1 mg | BVN-2228-1 | page | data sheet | A cell-permeable necrosis inhibitor that displays antioxidant property. It localizes mostly in the mitochondria. Selectively blocks oxidative stress-induced necrotic cell death (0.1 µM NecroX-2 prevented ~50% cell death in H9C2 cells exposed to 400 µM t-BuOOH for 2 hours). Does not protect against staurosporine or etoposide-induced apoptosis. Protects cells against cold shock, hypoxia and oxidative stress in vitro. |
| Necrosis Inhibitor, Necrox-5 | 1 mg | BVN-2229-1 | page | data sheet | A cell-permeable necrosis inhibitor that displays antioxidant property. It localizes mostly in the mitochondria. Selectively blocks oxidative stress-induced necrotic cell death (0.1 µM NecroX-5 prevented ~50% cell death in H9C2 cells exposed to 400 µM t-BuOOH for 2 hours). Does not protect against staurosporine or etoposide-induced apoptosis. Protects cells against cold shock, hypoxia and oxidative stress in vitro, as well as CCl4 -induced acute liver injury and chronic liver fibrosis in rodent models. |
| Necrosis Inhibitor, Necrox-5 | 5 mg | BVN-2229-5 | page | data sheet | A cell-permeable necrosis inhibitor that displays antioxidant property. It localizes mostly in the mitochondria. Selectively blocks oxidative stress-induced necrotic cell death (0.1 µM NecroX-5 prevented ~50% cell death in H9C2 cells exposed to 400 µM t-BuOOH for 2 hours). Does not protect against staurosporine or etoposide-induced apoptosis. Protects cells against cold shock, hypoxia and oxidative stress in vitro, as well as CCl4 -induced acute liver injury and chronic liver fibrosis in rodent models. |
| Nigericin . sodium salt | 5 mg | AG-CN2-0020-M005 | page | data sheet | C40H67O11 . Na. CAS: 28643-80-3. MW: 724.0 . 23.0. Antibiotic. High affinity ionophore for monovalent cations such as H+, K+, Na+, Pb2+. Shows antibacterial (Gram-positive), antifungal, antitumor and antiviral activity. Disrupts membrane potential of mitochondria. NLRP3/NALP3 activator. Signals through pannexin-1 to induce caspase-1 maturation and IL-1beta processing and release. Autophagy modulator [13] |
| Nigericin . sodium salt | 25 mg | AG-CN2-0020-M025 | page | data sheet | C40H67O11 . Na. CAS: 28643-80-3. MW: 724.0 . 23.0. Antibiotic. High affinity ionophore for monovalent cations such as H+, K+, Na+, Pb2+. Shows antibacterial (Gram-positive), antifungal, antitumor and antiviral activity. Disrupts membrane potential of mitochondria. NLRP3/NALP3 activator. Signals through pannexin-1 to induce caspase-1 maturation and IL-1beta processing and release. Autophagy modulator [13] |
| Nigericin sodium salt | 5 mg | BVN-2096-5 | page | data sheet | Nigericin is a polyether ionophore which disrupts membrane potential and stimulates ATPase activity in mitochondria. Ion selectivity is K⁺> Rb⁺ Cs⁺>> Na⁺. Also activates NLRP3/NALP3 and signals through pannexin-1 to induce caspase-1 maturation and IL-1β processing and release. |
| Nigericin sodium salt | 25 mg | BVN-2096-25 | page | data sheet | Nigericin is a polyether ionophore which disrupts membrane potential and stimulates ATPase activity in mitochondria. Ion selectivity is K⁺> Rb⁺ Cs⁺>> Na⁺. Also activates NLRP3/NALP3 and signals through pannexin-1 to induce caspase-1 maturation and IL-1β processing and release. |
| Nitrotetrazolium blue chloride | 1 g | CDX-N0009-G001 | page | data sheet | C40H30Cl2N10O6. CAS: 298-83-9. MW: 817.2. NADPH-diaphorase substrate that competitively inhibits NOS (nitric oxide synthase). Well-known scavenger of superoxide anions. Dye that is used for detection of alkaline phosphatase in combination with 5-bromo-4-chloro-3-indoxyl phosphate (BCIP). This substrate system produces an insoluble NBT diformazan end product that is blue in color and can be observed visually. When used with BCIP, it is suitable for detection of alkaline phosphatase in western blots, for immunohistological staining procedures and for colorimetric indication of bacterial infection in blood samples. Used as a redox indicator for enzymatic reactions including dehydrogenases, threonine deaminase, glucose-6-phosphate dehydrogenase, phosphofructokinase on polyacrylamide gels, oxidases on polyacrylamide gels and pentose shunt dehydrogenses. The NBT/BCIP reaction is also used for colorimetric/spectrophotometric activity assays of oxidoreductases. One application is in activity stains in gel electrophoresis, such as with the mitochondrial electron transport chain complexes. |
| Nitrotetrazolium blue chloride | 100 mg | CDX-N0009-M100 | page | data sheet | C40H30Cl2N10O6. CAS: 298-83-9. MW: 817.2. NADPH-diaphorase substrate that competitively inhibits NOS (nitric oxide synthase). Well-known scavenger of superoxide anions. Dye that is used for detection of alkaline phosphatase in combination with 5-bromo-4-chloro-3-indoxyl phosphate (BCIP). This substrate system produces an insoluble NBT diformazan end product that is blue in color and can be observed visually. When used with BCIP, it is suitable for detection of alkaline phosphatase in western blots, for immunohistological staining procedures and for colorimetric indication of bacterial infection in blood samples. Used as a redox indicator for enzymatic reactions including dehydrogenases, threonine deaminase, glucose-6-phosphate dehydrogenase, phosphofructokinase on polyacrylamide gels, oxidases on polyacrylamide gels and pentose shunt dehydrogenses. The NBT/BCIP reaction is also used for colorimetric/spectrophotometric activity assays of oxidoreductases. One application is in activity stains in gel electrophoresis, such as with the mitochondrial electron transport chain complexes. |
| Phenformin hydrochloride | 1 g | BVN-1889-1000 | page | data sheet | An anti-diabetic drug of the biguanide class. Increases AMPK activity without increasing AMP/ATP. Also acts as a mitochondrial complex I inhibitor. |
| Phenformin hydrochloride | 100 mg | BVN-1889-100 | page | data sheet | An anti-diabetic drug of the biguanide class. Increases AMPK activity without increasing AMP/ATP. Also acts as a mitochondrial complex I inhibitor. |
| Phytosphingosine | 50 mg | BVN-2426-50 | page | data sheet | Phytosphingosine is a phospholipid structurally similar to Sphingosine (Cat. No. 2425). The physiological roles of phytosphingosine are largely unknown. Phytosphingosine induces apoptosis in human T-cell lymphoma and non-small cell lung cancer cells, and induces caspase-independent cytochrome c release from mitochondria. In the presence of caspase inhibitors, phytosphingosine-induced apoptosis is almost completely suppressed, suggesting that phytosphingosine-induced apoptosis is largely dependent on caspase activities. |
| Phytosphingosine | 250 mg | BVN-2426-250 | page | data sheet | Phytosphingosine is a phospholipid structurally similar to Sphingosine (Cat. No. 2425). The physiological roles of phytosphingosine are largely unknown. Phytosphingosine induces apoptosis in human T-cell lymphoma and non-small cell lung cancer cells, and induces caspase-independent cytochrome c release from mitochondria. In the presence of caspase inhibitors, phytosphingosine-induced apoptosis is almost completely suppressed, suggesting that phytosphingosine-induced apoptosis is largely dependent on caspase activities. |
| PK 11195 | 50 mg | BVN-2054-50 | page | data sheet | Cell-permeable. A Selective peripheral benzodiazepine antagonist. Enhances apoptosis and induces mitochondria cytochrome c release. Inhibits insulin secretion induced by glucose. Also displays anticancer activity. |
| PK 11195 | 10 mg | AG-CR1-0008-M010 | page | data sheet | C21H21ClN2O. CAS: 85532-75-8. MW: 352.9. Selective peripheral benzodiazepine antagonist. Apoptosis enhancer. Glucose-induced insulin secretion inhibitor. Induces mitochondria cytochrome c release. Anticancer compound. Antiproliferative. Pharmacological tool in autophagy. |
| PK 11195 | 10 mg | BVN-2054-10 | page | data sheet | Cell-permeable. A Selective peripheral benzodiazepine antagonist. Enhances apoptosis and induces mitochondria cytochrome c release. Inhibits insulin secretion induced by glucose. Also displays anticancer activity. |
| PK 11195 | 50 mg | AG-CR1-0008-M050 | page | data sheet | C21H21ClN2O. CAS: 85532-75-8. MW: 352.9. Selective peripheral benzodiazepine antagonist. Apoptosis enhancer. Glucose-induced insulin secretion inhibitor. Induces mitochondria cytochrome c release. Anticancer compound. Antiproliferative. Pharmacological tool in autophagy. |
| Propionyl-L-carnitine . HCl | 500 mg | AG-CR1-3595-M500 | page | data sheet | C10H19NO4 . HCl. CAS: 119793-66-7. MW: 217.3 . 36.5. Naturally occurring carnitine derivative formed by carnitine acetyltransferase during beta-oxidation of uneven chain fatty acids, with high affinity for muscular carnitine transferase. Increases cellular carnitine content, allowing free fatty acid transport into the mitochondria. Stimulates energy production in ischaemic muscles by increasing citric acid cycle flux and stimulating pyruvate dehydrogenase activity. Important for mitochondrial metabolism and energy regulation. Regulates the metabolism of both carbohydrates and lipids, leading to an increase of ATP generation. Selectively inhibits in vitro and ex vivo platelet-activating factor (PAF) synthesis from human neutrophils. Antioxidant. Shows free radical scavenging activity. Decreases the expression of inducible nitric oxide synthase (iNOS/NOS II) and NADPH-oxidase 4-mediated reactive oxygen species production in human umbilical vascular endothelial cells. Shows beneficial cardiovascular effects. Improves body weight, food intake, adiposity and insulin resistance in Type 2 diabetes. Stimulates endothelial nitric oxide (eNOS/NOS III) and increased NO production, via AMPK/Src-mediated signaling that leads to activation of PI3 kinase and Akt. |
| Propionyl-L-carnitine . HCl | 25 mg | AG-CR1-3595-M025 | page | data sheet | C10H19NO4 . HCl. CAS: 119793-66-7. MW: 217.3 . 36.5. Naturally occurring carnitine derivative formed by carnitine acetyltransferase during beta-oxidation of uneven chain fatty acids, with high affinity for muscular carnitine transferase. Increases cellular carnitine content, allowing free fatty acid transport into the mitochondria. Stimulates energy production in ischaemic muscles by increasing citric acid cycle flux and stimulating pyruvate dehydrogenase activity. Important for mitochondrial metabolism and energy regulation. Regulates the metabolism of both carbohydrates and lipids, leading to an increase of ATP generation. Selectively inhibits in vitro and ex vivo platelet-activating factor (PAF) synthesis from human neutrophils. Antioxidant. Shows free radical scavenging activity. Decreases the expression of inducible nitric oxide synthase (iNOS/NOS II) and NADPH-oxidase 4-mediated reactive oxygen species production in human umbilical vascular endothelial cells. Shows beneficial cardiovascular effects. Improves body weight, food intake, adiposity and insulin resistance in Type 2 diabetes. Stimulates endothelial nitric oxide (eNOS/NOS III) and increased NO production, via AMPK/Src-mediated signaling that leads to activation of PI3 kinase and Akt. |
| Propionyl-L-carnitine . HCl | 100 mg | AG-CR1-3595-M100 | page | data sheet | C10H19NO4 . HCl. CAS: 119793-66-7. MW: 217.3 . 36.5. Naturally occurring carnitine derivative formed by carnitine acetyltransferase during beta-oxidation of uneven chain fatty acids, with high affinity for muscular carnitine transferase. Increases cellular carnitine content, allowing free fatty acid transport into the mitochondria. Stimulates energy production in ischaemic muscles by increasing citric acid cycle flux and stimulating pyruvate dehydrogenase activity. Important for mitochondrial metabolism and energy regulation. Regulates the metabolism of both carbohydrates and lipids, leading to an increase of ATP generation. Selectively inhibits in vitro and ex vivo platelet-activating factor (PAF) synthesis from human neutrophils. Antioxidant. Shows free radical scavenging activity. Decreases the expression of inducible nitric oxide synthase (iNOS/NOS II) and NADPH-oxidase 4-mediated reactive oxygen species production in human umbilical vascular endothelial cells. Shows beneficial cardiovascular effects. Improves body weight, food intake, adiposity and insulin resistance in Type 2 diabetes. Stimulates endothelial nitric oxide (eNOS/NOS III) and increased NO production, via AMPK/Src-mediated signaling that leads to activation of PI3 kinase and Akt. |
| Pseudoanguillosporin A | 500 µg | BVT-0311-C500 | C17H26O3. CAS: 1159392-22-9. MW: 278.4. Antifungal. Respiration inhibitor. Inhibits mitochondrial respiration in fungi. Binds at the Q0-centre on cytochrome b and blocks the electron transfer between cytochrome b and cytochrome c1. | ||
| Pseudoanguillosporin A | 1 mg | BVT-0311-M001 | C17H26O3. CAS: 1159392-22-9. MW: 278.4. Antifungal. Respiration inhibitor. Inhibits mitochondrial respiration in fungi. Binds at the Q0-centre on cytochrome b and blocks the electron transfer between cytochrome b and cytochrome c1. | ||
| Puromycin . 2HCl | 100 mg | AG-CN2-0078-M100 | page | data sheet | C22H29N7O5 . 2HCl. CAS: 58-58-2. MW: 471.5 . 73.0. Aminonucleoside antibiotic. Protein synthesis inhibitor. Disrupts peptide transfer on ribosomes (acting as an acyl-tRNA analog) causing premature chain termination during translation. Translational inhibitor in prokaryotic and eukaryotic cells in both in vitro and in vivo systems. Inhibits the transport of proteins into the mitochondria in vitro. Reversible inhibitor of dipeptidyl-peptidase II (serine peptidase) and cytosol alanyl aminopeptidase (metallopeptidase). Apoptosis inducer. Inhibits the growth of Gram-positive bacteria, various animal and insect cells. Fungi and Gram-negative bacteria are resistant due to the low permeability to the antibiotic. Antineoplastic agent. Used in cell biology as selective agent in cell culture systems. It allows selection for cells that contain the resistance gene puromycin N-acetyl-transferase (PAC). Puromycin has a fast mode of action, causing rapid cell death at low antibiotic concentrations. Adherent mammalian cells are sensitive to concentrations of 2 to 5 µg/ml, while cells in suspension are sensitive to concentrations as low as 0. 5 to 2 µg/ml. Puromycin-resistant stable mammalian cell lines can be generated in less than one week. |
| Puromycin . 2HCl | 500 mg | AG-CN2-0078-M500 | page | data sheet | C22H29N7O5 . 2HCl. CAS: 58-58-2. MW: 471.5 . 73.0. Aminonucleoside antibiotic. Protein synthesis inhibitor. Disrupts peptide transfer on ribosomes (acting as an acyl-tRNA analog) causing premature chain termination during translation. Translational inhibitor in prokaryotic and eukaryotic cells in both in vitro and in vivo systems. Inhibits the transport of proteins into the mitochondria in vitro. Reversible inhibitor of dipeptidyl-peptidase II (serine peptidase) and cytosol alanyl aminopeptidase (metallopeptidase). Apoptosis inducer. Inhibits the growth of Gram-positive bacteria, various animal and insect cells. Fungi and Gram-negative bacteria are resistant due to the low permeability to the antibiotic. Antineoplastic agent. Used in cell biology as selective agent in cell culture systems. It allows selection for cells that contain the resistance gene puromycin N-acetyl-transferase (PAC). Puromycin has a fast mode of action, causing rapid cell death at low antibiotic concentrations. Adherent mammalian cells are sensitive to concentrations of 2 to 5 µg/ml, while cells in suspension are sensitive to concentrations as low as 0. 5 to 2 µg/ml. Puromycin-resistant stable mammalian cell lines can be generated in less than one week. |
| Puromycin . 2HCl | 250 mg | AG-CN2-0078-M250 | page | data sheet | C22H29N7O5 . 2HCl. CAS: 58-58-2. MW: 471.5 . 73.0. Aminonucleoside antibiotic. Protein synthesis inhibitor. Disrupts peptide transfer on ribosomes (acting as an acyl-tRNA analog) causing premature chain termination during translation. Translational inhibitor in prokaryotic and eukaryotic cells in both in vitro and in vivo systems. Inhibits the transport of proteins into the mitochondria in vitro. Reversible inhibitor of dipeptidyl-peptidase II (serine peptidase) and cytosol alanyl aminopeptidase (metallopeptidase). Apoptosis inducer. Inhibits the growth of Gram-positive bacteria, various animal and insect cells. Fungi and Gram-negative bacteria are resistant due to the low permeability to the antibiotic. Antineoplastic agent. Used in cell biology as selective agent in cell culture systems. It allows selection for cells that contain the resistance gene puromycin N-acetyl-transferase (PAC). Puromycin has a fast mode of action, causing rapid cell death at low antibiotic concentrations. Adherent mammalian cells are sensitive to concentrations of 2 to 5 µg/ml, while cells in suspension are sensitive to concentrations as low as 0. 5 to 2 µg/ml. Puromycin-resistant stable mammalian cell lines can be generated in less than one week. |
| Puromycin . 2HCl | 1 g | AG-CN2-0078-G001 | page | data sheet | C22H29N7O5 . 2HCl. CAS: 58-58-2. MW: 471.5 . 73.0. Aminonucleoside antibiotic. Protein synthesis inhibitor. Disrupts peptide transfer on ribosomes (acting as an acyl-tRNA analog) causing premature chain termination during translation. Translational inhibitor in prokaryotic and eukaryotic cells in both in vitro and in vivo systems. Inhibits the transport of proteins into the mitochondria in vitro. Reversible inhibitor of dipeptidyl-peptidase II (serine peptidase) and cytosol alanyl aminopeptidase (metallopeptidase). Apoptosis inducer. Inhibits the growth of Gram-positive bacteria, various animal and insect cells. Fungi and Gram-negative bacteria are resistant due to the low permeability to the antibiotic. Antineoplastic agent. Used in cell biology as selective agent in cell culture systems. It allows selection for cells that contain the resistance gene puromycin N-acetyl-transferase (PAC). Puromycin has a fast mode of action, causing rapid cell death at low antibiotic concentrations. Adherent mammalian cells are sensitive to concentrations of 2 to 5 µg/ml, while cells in suspension are sensitive to concentrations as low as 0. 5 to 2 µg/ml. Puromycin-resistant stable mammalian cell lines can be generated in less than one week. |
| Puromycin . 2HCl | 25 mg | AG-CN2-0078-M025 | page | data sheet | C22H29N7O5 . 2HCl. CAS: 58-58-2. MW: 471.5 . 73.0. Aminonucleoside antibiotic. Protein synthesis inhibitor. Disrupts peptide transfer on ribosomes (acting as an acyl-tRNA analog) causing premature chain termination during translation. Translational inhibitor in prokaryotic and eukaryotic cells in both in vitro and in vivo systems. Inhibits the transport of proteins into the mitochondria in vitro. Reversible inhibitor of dipeptidyl-peptidase II (serine peptidase) and cytosol alanyl aminopeptidase (metallopeptidase). Apoptosis inducer. Inhibits the growth of Gram-positive bacteria, various animal and insect cells. Fungi and Gram-negative bacteria are resistant due to the low permeability to the antibiotic. Antineoplastic agent. Used in cell biology as selective agent in cell culture systems. It allows selection for cells that contain the resistance gene puromycin N-acetyl-transferase (PAC). Puromycin has a fast mode of action, causing rapid cell death at low antibiotic concentrations. Adherent mammalian cells are sensitive to concentrations of 2 to 5 µg/ml, while cells in suspension are sensitive to concentrations as low as 0. 5 to 2 µg/ml. Puromycin-resistant stable mammalian cell lines can be generated in less than one week. |
| Rocaglamide | 100 µg | BVN-1863-100 | page | data sheet | An immunosuppressant and a potent inhibitor of NF-κB activation in T cells, with an almost complete inhibition at 200 nM. Suppresses cytokine production (IFN-γ, TNF-α, IL-2 and IL-4) and inhibits NF-AT in peripheral blood T cells at concentrations that do not impair NF-κB and AP-1 activities. Also induces mitochondria-mediated apoptosis in leukemia cells and sensitizes CD95/CD95L-mediated apoptosis in malignant T-cells by differential regulation of CD95L and c-FLIP expression. |
| Rotenone | 250 mg | BVN-2248-250 | page | data sheet | A broad spectrum insecticide that is cell-permeable and brain-permeable. Acts as a mitochondrial electron transport chain inhibitor (IC₅₀ = 1.7 - 2.2 μM at complex I). Inhibits NADH oxidation by cardiac sarcoplasmic reticulum (IC₅₀ = 3.4 nM). Neurotoxic agent that has also been used successfully to reproduce Parkinsons-like characteristics in in-vitro slice culture models. |
| Rotenone | 1 g | BVN-2248-1000 | page | data sheet | A broad spectrum insecticide that is cell-permeable and brain-permeable. Acts as a mitochondrial electron transport chain inhibitor (IC₅₀ = 1.7 - 2.2 μM at complex I). Inhibits NADH oxidation by cardiac sarcoplasmic reticulum (IC₅₀ = 3.4 nM). Neurotoxic agent that has also been used successfully to reproduce Parkinsons-like characteristics in in-vitro slice culture models. |
| Rottlerin | 10 mg | BVN-1827-10 | page | data sheet | Originally reported as an inhibitor of Protein Kinase C isoforms with selectivity for PKCδ. However, more recent studies have shown Rottlerin did not block PKCδ activity but did block other kinase and non-kinase proteins in vitro and activated multiple Ca²⁺-sensitive K⁺ channels with high potency. It uncouples mitochondria and affects mitochondrial production of reactive oxygen species (ROS). Also induces autophagy through inhibition of mTORC1. |
| Ruthenium Red | 500 mg | BVN-2490-500 | page | data sheet | Ruthenium red is an inhibitor of mitochondrial Ca²⁺ uniporter; also blocks cell membrane-located capsaicin-activated cation channels (IC₅₀ = 14 nM) and voltage-sensitive Ca²⁺ channels to inhibit neurotransmitter release. In addition, it specifically blocks the curcumin-induced apoptosis in U937 cells. |
| Ruthenium Red | 100 mg | BVN-2490-100 | page | data sheet | Ruthenium red is an inhibitor of mitochondrial Ca²⁺ uniporter; also blocks cell membrane-located capsaicin-activated cation channels (IC₅₀ = 14 nM) and voltage-sensitive Ca²⁺ channels to inhibit neurotransmitter release. In addition, it specifically blocks the curcumin-induced apoptosis in U937 cells. |
| SMI-4a | 5 mg | AG-CR1-3503-M005 | page | data sheet | C11H6F3NO2S. CAS: 327033-36-3. MW: 273.2. Selective inhibitor of Pim-1 and Pim-2 protein kinases. Inducer of G1 phase cell cycle arrest. Inducer of p27Kip1. Inducer of apoptosis through the mitochondrial pathway. Inhibitor of the mammalian target of rapamycin C1 (mTORC1) pathway. Downregulates c-myc. Inhibitor of PRAS40 phosphorylation and mTOR activity. Potential anti-cancer compound. Blocks prostate cancer growth. |
| SRT1720 | 5 mg | BPS-27655-1 | page | SRT1720 is a small-molecule compound which has the ability of activating the sirtuin subtype SIRT1 in vitro. SRT1720 has similar activity in the body to the known SIRT1 activator resveratrol, but is 1000x more potent. It affects mitochondrial respiration in a Sirt1- and PGC-1α-dependent manner. SRT1720 has been demonstrated to enhance insulin sensitivity and improve measures of mitochondrial capacity and oxidative metabolism. Treatment of multiple myeloma (MM) cells with SRT1720 inhibits growth and induced apoptosis in MM cells resistant to conventional and bortezomib therapies without significantly affecting the viability of normal cells. SRT1720 is able to enhance the cytotoxic activity of bortezomib or dexamethasone. Anti-MM activity of SRT1720 is related to: 1) activation of caspase-8, caspase-9, caspase-3, poly(ADP) ribose polymerase; 2) increase in reactive oxygen species; 3) induction of phosphorylated ataxia telangiectasia mutated/checkpoint kinase 2 signaling; 4) decrease in vascular endothelial growth factor-induced migration of MM cells and associated angiogenesis; and 5) inhibition of nuclear factor-κB. | |
| SRT1720 | 10 mg | BPS-27655-2 | page | SRT1720 is a small-molecule compound which has the ability of activating the sirtuin subtype SIRT1 in vitro. SRT1720 has similar activity in the body to the known SIRT1 activator resveratrol, but is 1000x more potent. It affects mitochondrial respiration in a Sirt1- and PGC-1α-dependent manner. SRT1720 has been demonstrated to enhance insulin sensitivity and improve measures of mitochondrial capacity and oxidative metabolism. Treatment of multiple myeloma (MM) cells with SRT1720 inhibits growth and induced apoptosis in MM cells resistant to conventional and bortezomib therapies without significantly affecting the viability of normal cells. SRT1720 is able to enhance the cytotoxic activity of bortezomib or dexamethasone. Anti-MM activity of SRT1720 is related to: 1) activation of caspase-8, caspase-9, caspase-3, poly(ADP) ribose polymerase; 2) increase in reactive oxygen species; 3) induction of phosphorylated ataxia telangiectasia mutated/checkpoint kinase 2 signaling; 4) decrease in vascular endothelial growth factor-induced migration of MM cells and associated angiogenesis; and 5) inhibition of nuclear factor-κB. | |
| SRT1720 | 50 mg | BPS-27655-3 | page | SRT1720 is a small-molecule compound which has the ability of activating the sirtuin subtype SIRT1 in vitro. SRT1720 has similar activity in the body to the known SIRT1 activator resveratrol, but is 1000x more potent. It affects mitochondrial respiration in a Sirt1- and PGC-1α-dependent manner. SRT1720 has been demonstrated to enhance insulin sensitivity and improve measures of mitochondrial capacity and oxidative metabolism. Treatment of multiple myeloma (MM) cells with SRT1720 inhibits growth and induced apoptosis in MM cells resistant to conventional and bortezomib therapies without significantly affecting the viability of normal cells. SRT1720 is able to enhance the cytotoxic activity of bortezomib or dexamethasone. Anti-MM activity of SRT1720 is related to: 1) activation of caspase-8, caspase-9, caspase-3, poly(ADP) ribose polymerase; 2) increase in reactive oxygen species; 3) induction of phosphorylated ataxia telangiectasia mutated/checkpoint kinase 2 signaling; 4) decrease in vascular endothelial growth factor-induced migration of MM cells and associated angiogenesis; and 5) inhibition of nuclear factor-κB. | |
| Thapsigargin | 10 mg | AG-CN2-0003-M010 | page | data sheet | C34H50O12. CAS: 67526-95-8. MW: 650.8. Intracellular Ca2+ signaling probe. Specific and sensitive inhibitor of SERCA. Non-TPA/PMA tumor promoter. Histamine release inducer. Apoptosis inducer. Mitochondrial dysfunction inducer. NOS modulator. Angiogenesis inhibitor. Stimulator of arachidonic acid metabolism in macrophages. Autophagy inducer. TRAIL sensitizer. |
| Thapsigargin | 1 mg | AG-CN2-0003-M001 | page | data sheet | C34H50O12. CAS: 67526-95-8. MW: 650.8. Intracellular Ca2+ signaling probe. Specific and sensitive inhibitor of SERCA. Non-TPA/PMA tumor promoter. Histamine release inducer. Apoptosis inducer. Mitochondrial dysfunction inducer. NOS modulator. Angiogenesis inhibitor. Stimulator of arachidonic acid metabolism in macrophages. Autophagy inducer. TRAIL sensitizer. |
| Thapsigargin | 5 mg | AG-CN2-0003-M005 | page | data sheet | C34H50O12. CAS: 67526-95-8. MW: 650.8. Intracellular Ca2+ signaling probe. Specific and sensitive inhibitor of SERCA. Non-TPA/PMA tumor promoter. Histamine release inducer. Apoptosis inducer. Mitochondrial dysfunction inducer. NOS modulator. Angiogenesis inhibitor. Stimulator of arachidonic acid metabolism in macrophages. Autophagy inducer. TRAIL sensitizer. |
| Thifluzamide | 10 mg | CDX-T0118-M010 | page | data sheet | C13H6Br2F6N2O2S. CAS: 130000-40-7. MW: 528.1. Thiazole fungicide used in agrochemistry. Succinate dehydrogenase inhibitor (SDHI) which interferes with succinate ubiquinone reductase in the mitochondrial electron transport chain of fungi. Compound can be used as analytical reference material. |
| Thifluzamide | 50 mg | CDX-T0118-M050 | page | data sheet | C13H6Br2F6N2O2S. CAS: 130000-40-7. MW: 528.1. Thiazole fungicide used in agrochemistry. Succinate dehydrogenase inhibitor (SDHI) which interferes with succinate ubiquinone reductase in the mitochondrial electron transport chain of fungi. Compound can be used as analytical reference material. |
| Valinomycin | 10 mg | BVN-2238-10 | page | data sheet | A highly selective K⁺- ionophore. It binds potassium ions (K⁺) and facilitates their transfer across lipid bilayers. Inhibits Ca²⁺-ATPase activity and promotes cell death by mitochondrial swelling and autophagic processes, but not apoptosis. Antagonizes endothelin-induced vasoconstriction (IC₅₀ = 0.3 µM). |
| Valinomycin | 50 mg | BVN-2238-50 | page | data sheet | A highly selective K⁺- ionophore. It binds potassium ions (K⁺) and facilitates their transfer across lipid bilayers. Inhibits Ca²⁺-ATPase activity and promotes cell death by mitochondrial swelling and autophagic processes, but not apoptosis. Antagonizes endothelin-induced vasoconstriction (IC₅₀ = 0.3 µM). |
| Antibodies | |||||
| 2-Cys Peroxiredoxin mAb (6E5) | 100 ul | YIF-LF-MA0073 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation. |
| anti-Caspase-2, mAb (10C6) | 100 µg | AG-20T-0135-C100 | page | data sheet | Recognizes an epitope in the p19 subunit of human, mouse, rat, monkey and dog caspase-2. Caspase-2 is a Class I caspase with a long prodomain necessary for nuclear localization. Upon activation of the apoptotic pathway, the procaspase is cleaved into smaller fragments. Caspase-2 is the nuclear apoptotic respondent to cellular genotoxic stress or mitotic catastrophe and is involved in the activation cascade of caspases responsible for apoptosis execution. Activation occurs upon recruitment to a complex containing a p53-induced death domain protein, PIDD. This suggests caspase-2 can be a nuclear initiator caspase with a requirement for caspase-9 and caspase-3 activation in downstream apoptotic events. In apoptotic pathways resulting from UV-induced DNA damage, processing of caspase-2 occurs downstream of mitochondrial dysfunction and of caspase-9 and caspase-3 activation, extending a possible role for caspase-2 as a parallel effector caspase. |
| anti-Caspase-2, mAb (11B4) | 100 µg | AG-20T-0136-C100 | page | data sheet | Recognizes an epitope in the p19 subunit of human, mouse, rat, monkey and dog caspase-2. Detects bands of ~51kDa (procaspase-2), ~32kDa and ~18kDa (cleavage products) by Western blot. Caspase-2 is a Class I caspase with a long prodomain necessary for nuclear localization. Upon activation of the apoptotic pathway, the procaspase is cleaved into smaller fragments. Caspase-2 is the nuclear apoptotic respondent to cellular genotoxic stress or mitotic catastrophe and is involved in the activation cascade of caspases responsible for apoptosis execution. Activation occurs upon recruitment to a complex containing a p53-induced death domain protein, PIDD. This suggests caspase-2 can be a nuclear initiator caspase with a requirement for caspase-9 and caspase-3 activation in downstream apoptotic events. In apoptotic pathways resulting from UV-induced DNA damage, processing of caspase-2 occurs downstream of mitochondrial dysfunction and of caspase-9 and caspase-3 activation, extending a possible role for caspase-2 as a parallel effector caspase. |
| anti-Fis1, pAb | 100 µg | AG-25B-0007V-C100 | page | data sheet | Host: Rabbit. Recognizes human, mouse and rat Fis1. Fis1 promotes the fragmentation of the mitochondrial network and its perinuclear clustering. It can induce cytochrome c release from mitochondria to the cytosol, ultimately leading to apoptosis. It also mediates peroxisomal fission. |
| Bcl-2 (B Cell Lymphoma 2) pAb | 100 ul | YIF-LF-PA0178 | page | data sheet | Bcl-2 (B-cell lymphoma 2) family govern mitochondrial outer membrane permeabilization (MOMP) and can be either pro-apoptotic (Bax, BAD, Bak and Bok) or anti-apoptotic (Bcl-2, Bcl-xL, and Bcl-w). The mitochondrial release of cytochrome c through anion channel is regulated by Bcl-2 and Bcl-xL. The Bcl-2 family of proteins are key regulators of many signals leading to caspase, which when activated cause cellular destruction by cleaving a range of vital cellular substrates. The members of the Bcl-2 family share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains (named BH1, BH2, BH3 and BH4). The Bcl-2 gene has been implicated in a number of cancers, including melanoma, breast, prostate, and lung carcinomas, as well as schizophrenia and autoimmunity. It is also thought to be involved in resistance to conventional cancer treatment. Cancer is an important component of the sequence of events during which anticancer drugs induce an antitumor response. The molecular mechanism for drug-induced apoptosis is associated with a mitochondrial dysfunction that is characterized by an increase in MOMP and a release of cytochrome c from mitochondria, indicating that Bcl-2 plays a critical role in anticancer drug-induced apoptosis. Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). |
| Bcl-2 mAb (11C5) | 100 ul | YIF-LF-MA0200 | page | data sheet | Bcl-2 (B-cell lymphoma 2) family govern mitochondrial outer membrane permeabilization (MOMP) and can be either pro-apoptotic (Bax, BAD, Bak, Bid and Bok) or anti-apoptotic (Bcl-2, Bcl-xL, and Bcl-w). The mitochondrial release of cytochrome c through anion channel is regulated by Bcl-2 and Bcl-xL. The Bcl-2 family of proteins are key regulators of many signals leading to caspase, which when activated cause cellular destruction by cleaving a range of vital cellular substrates. The members of the Bcl-2 family share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains (named BH1, BH2, BH3 and BH4). The Bcl-2 gene has been implicated in a number of cancers, including melanoma, breast, prostate, and lung carcinomas, as well as schizophrenia and autoimmunity. It is also thought to be involved in resistance to conventional cancer treatment. Cancer is an important component of the sequence of events during which anticancer drugs induce an antitumor response. The molecular mechanism for drug-induced apoptosis is associated with a mitochondrial dysfunction that is characterized by an increase in MOMP and a release of cytochrome c from mitochondria, indicating that Bcl-2 plays a critical role in anticancer drug-induced apoptosis. Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). |
| Bcl-2 mAb (2B11) | 100 ul | YIF-LF-MA0199 | page | data sheet | Bcl-2 (B-cell lymphoma 2) family govern mitochondrial outer membrane permeabilization (MOMP) and can be either pro-apoptotic (Bax, BAD, Bak, Bid and Bok) or anti-apoptotic (Bcl-2, Bcl-xL, and Bcl-w). The mitochondrial release of cytochrome c through anion channel is regulated by Bcl-2 and Bcl-xL. The Bcl-2 family of proteins are key regulators of many signals leading to caspase, which when activated cause cellular destruction by cleaving a range of vital cellular substrates. The members of the Bcl-2 family share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains (named BH1, BH2, BH3 and BH4). The Bcl-2 gene has been implicated in a number of cancers, including melanoma, breast, prostate, and lung carcinomas, as well as schizophrenia and autoimmunity. It is also thought to be involved in resistance to conventional cancer treatment. Cancer is an important component of the sequence of events during which anticancer drugs induce an antitumor response. The molecular mechanism for drug-induced apoptosis is associated with a mitochondrial dysfunction that is characterized by an increase in MOMP and a release of cytochrome c from mitochondria, indicating that Bcl-2 plays a critical role in anticancer drug-induced apoptosis. Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). |
| Bid mAb (21F10) | 100 ul | YIF-LF-MA0208 | page | data sheet | Bcl-2 (B-cell lymphoma 2) family govern mitochondrial outer membrane permeabilization (MOMP) and can be either pro-apoptotic (Bax, BAD, Bak, Bid and Bok) or anti-apoptotic (Bcl-2, Bcl-xL, and Bcl-w). Mitochondrial membrane permeabilization and subsequent release of apoptotic factors are key mechanisms during this process. The members of the Bcl-2 family share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains (named BH1, BH2, BH3 and BH4). Bid consists of only one Bcl-2 homology domain, BH3. Bid cleavage to tBid (truncated Bid) activates apoptotic pathway at the mitochondrial level. Cleavage of cytosolic Bid and subsequent mitochondrial translocation have been detected in neuronal cell death related to acute or chronic neurodegeneration. Pharmacological inhibition of Bid can be a promising therapeutic strategy in neurological diseases where programmed cell death is prominent. After Bid activation and mitochondrial translocation, the most prominent downstream mechanisms of Bid-dependent neuronal apoptosis involve disruption of mitochondrial membrane integrity and intracellular calcium homoeostasis and the release of pro-apoptotic mitochondrial factors such as cytochrome c. The major proteolytic product p15 BID allows the release of cytochrome c. Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2. |
| Bid mAb (8D2) | 100 ul | YIF-LF-MA0207 | page | data sheet | Bcl-2 (B-cell lymphoma 2) family govern mitochondrial outer membrane permeabilization (MOMP) and can be either pro-apoptotic (Bax, BAD, Bak, Bid and Bok) or anti-apoptotic (Bcl-2, Bcl-xL, and Bcl-w). Mitochondrial membrane permeabilization and subsequent release of apoptotic factors are key mechanisms during this process. The members of the Bcl-2 family share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains (named BH1, BH2, BH3 and BH4). Bid consists of only one Bcl-2 homology domain, BH3. Bid cleavage to tBid (truncated Bid) activates apoptotic pathway at the mitochondrial level. Cleavage of cytosolic Bid and subsequent mitochondrial translocation have been detected in neuronal cell death related to acute or chronic neurodegeneration. Pharmacological inhibition of Bid can be a promising therapeutic strategy in neurological diseases where programmed cell death is prominent. After Bid activation and mitochondrial translocation, the most prominent downstream mechanisms of Bid-dependent neuronal apoptosis involve disruption of mitochondrial membrane integrity and intracellular calcium homoeostasis and the release of pro-apoptotic mitochondrial factors such as cytochrome c. The major proteolytic product p15 BID allows the release of cytochrome c. Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2. |
| Bid pAb | 100 ul | YIF-LF-PA0182 | page | data sheet | Bcl-2 (B-cell lymphoma 2) family govern mitochondrial outer membrane permeabilization (MOMP) and can be either pro-apoptotic (Bax, BAD, Bak, Bid and Bok) or anti-apoptotic (Bcl-2, Bcl-xL, and Bcl-w). Mitochondrial membrane permeabilization and subsequent release of apoptotic factors are key mechanisms during this process. The members of the Bcl-2 family share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains (named BH1, BH2, BH3 and BH4). Bid consists of only one Bcl-2 homology domain, BH3. Bid cleavage to tBid (truncated Bid) activates apoptotic pathway at the mitochondrial level. Cleavage of cytosolic Bid and subsequent mitochondrial translocation have been detected in neuronal cell death related to acute or chronic neurodegeneration. Pharmacological inhibition of Bid can be a promising therapeutic strategy in neurological diseases where programmed cell death is prominent. After Bid activation and mitochondrial translocation, the most prominent downstream mechanisms of Bid-dependent neuronal apoptosis involve disruption of mitochondrial membrane integrity and intracellular calcium homoeostasis and the release of pro-apoptotic mitochondrial factors such as cytochrome c. The major proteolytic product p15 BID allows the release of cytochrome c. Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2. |
| Bnip3L pAb | 0.5ml | SPB-E1684-2 | page | data sheet | Members in the BCL-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. BCL-2 homology 3 (BH3) domain is a potent death domain. BH3 domain containing pro-apoptotic proteins, including BAD, BAX, BID, BIK, HRK, NIP3, and BIM, form a growing subclass of the BCL-2 family. A novel BH3 domain containing protein was recently identified and designated Bnip3L, Bnip3, and NIX (for NIP3-like protein X). Bnip3L/Bnip3/Nix is a homolog of the E1B 19K/BCL-2 binding and pro-apoptotic protein Bnip3. Overexpression of Bnip3L induces apoptosis. Bnip3L interacts with and overcomes suppression by BCL-2 and BCL-XL. Bnip3L is localized in mitochondria. The messenger RNA of Bnip3L is ubiquitously expressed in human tissues. Bnip3L and Bnip3 form a new subfamily of the pro-apoptotic mitochondrial proteins |
| Bnip3L pAb | 0.1ml | SPB-E1684-0 | page | data sheet | Members in the BCL-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. BCL-2 homology 3 (BH3) domain is a potent death domain. BH3 domain containing pro-apoptotic proteins, including BAD, BAX, BID, BIK, HRK, NIP3, and BIM, form a growing subclass of the BCL-2 family. A novel BH3 domain containing protein was recently identified and designated Bnip3L, Bnip3, and NIX (for NIP3-like protein X). Bnip3L/Bnip3/Nix is a homolog of the E1B 19K/BCL-2 binding and pro-apoptotic protein Bnip3. Overexpression of Bnip3L induces apoptosis. Bnip3L interacts with and overcomes suppression by BCL-2 and BCL-XL. Bnip3L is localized in mitochondria. The messenger RNA of Bnip3L is ubiquitously expressed in human tissues. Bnip3L and Bnip3 form a new subfamily of the pro-apoptotic mitochondrial proteins |
| Bnip3L pAb | 1.0ml | SPB-E1684-4 | page | data sheet | Members in the BCL-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. BCL-2 homology 3 (BH3) domain is a potent death domain. BH3 domain containing pro-apoptotic proteins, including BAD, BAX, BID, BIK, HRK, NIP3, and BIM, form a growing subclass of the BCL-2 family. A novel BH3 domain containing protein was recently identified and designated Bnip3L, Bnip3, and NIX (for NIP3-like protein X). Bnip3L/Bnip3/Nix is a homolog of the E1B 19K/BCL-2 binding and pro-apoptotic protein Bnip3. Overexpression of Bnip3L induces apoptosis. Bnip3L interacts with and overcomes suppression by BCL-2 and BCL-XL. Bnip3L is localized in mitochondria. The messenger RNA of Bnip3L is ubiquitously expressed in human tissues. Bnip3L and Bnip3 form a new subfamily of the pro-apoptotic mitochondrial proteins |
| Bnip3L pAb (Prediluted) | 7.0ml | SPB-E1684-1 | page | data sheet | Members in the BCL-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. BCL-2 homology 3 (BH3) domain is a potent death domain. BH3 domain containing pro-apoptotic proteins, including BAD, BAX, BID, BIK, HRK, NIP3, and BIM, form a growing subclass of the BCL-2 family. A novel BH3 domain containing protein was recently identified and designated Bnip3L, Bnip3, and NIX (for NIP3-like protein X). Bnip3L/Bnip3/Nix is a homolog of the E1B 19K/BCL-2 binding and pro-apoptotic protein Bnip3. Overexpression of Bnip3L induces apoptosis. Bnip3L interacts with and overcomes suppression by BCL-2 and BCL-XL. Bnip3L is localized in mitochondria. The messenger RNA of Bnip3L is ubiquitously expressed in human tissues. Bnip3L and Bnip3 form a new subfamily of the pro-apoptotic mitochondrial proteins |
| anti-Cardif (human), mAb (Adri-1) | 100 µg | AG-20B-0004-C100 | page | data sheet | Recognizes human Cardif. RIG-I (retinoic acid-inducible gene I; Ddx58) and MDA5 (melanoma differentiation-associated gene 5, also known as Ifih1 or Helicard) are proteins that sense viral replication intermediates, such as double-stranded RNA and triggers the host antiviral programs. These molecules signal the downstream activation of NF-kappaB and IFN regulatory factor (IRF) -3, which coordinately regulate the expression of type-I interferons. Cardif (also called VISA/IPS-1/MAVS) is a new CARD (caspase activation and recruitment domain)-containing adaptor protein that interacts with the CARD domain of RIG-I and MDA5, leading to the activation of NF-kappaB and IRF3. Cardif is located to the mitochondrial outer membrane. Removal of the mitochondrial-targeting domain of cardif abolishes its ability to induce IFNs. Cardif is cleaved and inactivated by NS3-4A, a serine protease from hepatitis C virus known to block interferon-beta production. |
| Creatine Kinase-BB (CK-BB) mAb (3A6) | 100 ul | YIF-LF-MA0232 | page | data sheet | Creatine kinase (CK), also known as phosphocreatine kinase or creatine phosphokinase (CPK) is an enzyme expressed by various tissue types. It catalyzes the reversible transfer of the N-phosphoryl group from phosphocreatine (PCr) to ADP to regenerate ATP. Creatine kinase plays a key role in the energy homeostasis of cells with intermittently high, fluctuating energy requirements, such as skeletal and cardiac muscle cells, neurons, photoreceptors, spermatozoa and electrocytes. Creatine kinase consists of two subunits, which can be either B (brain type) or M (muscle type). Therefore, three different cytosolic isoenzymes exist: CK-MM, CK-BB and CK-MB. Cytosolic CK isoenzymes are always co-expressed in a tissue-specific fashion together with a mitochondrial isoform. Skeletal muscle expresses CK-MM (98%) and low levels of CK-MB (1%). The heart muscle expresses CK-MM at 70% and CK-MB at 25-30%. CK-BB is expressed in all tissues at low levels. Cytosolic CKs, in close conjunction with Ca2+-pumps, play a crucial role for the energetics of Ca2+-homeostasis. Octameric mitochondrial Mi-CK binds and crosslinks mitochondrial membranes. The CK system is regulated by AMP-activated protein kinase via PCr/Cr and ATP/AMP ratios. The cardiac-specific isoenzyme of creatine kinase, CK-MB, is a biomarker for myocardial infarction along with other markers such as cardiac Troponin I and myoglobin. The introduction of immunologic mass determination of CK-MB was a major breakthrough that replaced the traditional enzymatic assay. Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. |
| Creatine Kinase-M/B (CK-M/B) mAb (46A1) | 100 ul | YIF-LF-MA0233 | page | data sheet | Creatine kinase (CK), also known as phosphocreatine kinase or creatine phosphokinase (CPK) is an enzyme expressed by various tissue types. It catalyzes the reversible transfer of the N-phosphoryl group from phosphocreatine (PCr) to ADP to regenerate ATP. Creatine kinase plays a key role in the energy homeostasis of cells with intermittently high, fluctuating energy requirements, such as skeletal and cardiac muscle cells, neurons, photoreceptors, spermatozoa and electrocytes. Creatine kinase consists of two subunits, which can be either B (brain type) or M (muscle type). Therefore, three different cytosolic isoenzymes exist: CK-MM, CK-BB and CK-MB. Cytosolic CK isoenzymes are always co-expressed in a tissue-specific fashion together with a mitochondrial isoform. Skeletal muscle expresses CK-MM (98%) and low levels of CK-MB (1%). The heart muscle expresses CK-MM at 70% and CK-MB at 25-30%. CK-BB is expressed in all tissues at low levels. Cytosolic CKs, in close conjunction with Ca2+-pumps, play a crucial role for the energetics of Ca2+-homeostasis. Octameric mitochondrial Mi-CK binds and crosslinks mitochondrial membranes. The CK system is regulated by AMP-activated protein kinase via PCr/Cr and ATP/AMP ratios. The cardiac-specific isoenzyme of creatine kinase, CK-MB, is a biomarker for myocardial infarction along with other markers such as cardiac Troponin I and myoglobin. The introduction of immunologic mass determination of CK-MB was a major breakthrough that replaced the traditional enzymatic assay. Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. |
| Creatine Kinase-MM (CK-MM) mAb (2C5) | 100 ul | YIF-LF-MA0234 | page | data sheet | Creatine kinase (CK), also known as phosphocreatine kinase or creatine phosphokinase (CPK) is an enzyme expressed by various tissue types. It catalyzes the reversible transfer of the N-phosphoryl group from phosphocreatine (PCr) to ADP to regenerate ATP. Creatine kinase plays a key role in the energy homeostasis of cells with intermittently high, fluctuating energy requirements, such as skeletal and cardiac muscle cells, neurons, photoreceptors, spermatozoa and electrocytes. Creatine kinase consists of two subunits, which can be either B (brain type) or M (muscle type). Therefore, three different cytosolic isoenzymes exist: CK-MM, CK-BB and CK-MB. Cytosolic CK isoenzymes are always co-expressed in a tissue-specific fashion together with a mitochondrial isoform. Skeletal muscle expresses CK-MM (98%) and low levels of CK-MB (1%). The heart muscle expresses CK-MM at 70% and CK-MB at 25-30%. CK-BB is expressed in all tissues at low levels. Cytosolic CKs, in close conjunction with Ca2+-pumps, play a crucial role for the energetics of Ca2+-homeostasis. Octameric mitochondrial Mi-CK binds and crosslinks mitochondrial membranes. The CK system is regulated by AMP-activated protein kinase via PCr/Cr and ATP/AMP ratios. The cardiac-specific isoenzyme of creatine kinase, CK-MB, is a biomarker for myocardial infarction along with other markers such as cardiac Troponin I and myoglobin. The introduction of immunologic mass determination of CK-MB was a major breakthrough that replaced the traditional enzymatic assay. Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. |
| anti-CTRP5 (globular domain) (human), pAb | 100 µg | AG-25A-0096-C100 | page | data sheet | Host: Rabbit. Recognizes human CTRP5 (globular domain) and CTRP5 full-length protein. Detects a band of ~18kDa and ~30kDa by Western blot. CTRP5 (C1qTNF-related protein 5; C1QTNF5) belongs to a highly conserved family of adiponectin paralogs. CTRP5 mediates activation of AMP-activated protein kinase (AMPK) in muscle and liver cells, thereby regulating glucose and lipid metabolism. Serum levels of CTRP5 are significantly higher in obese/diabetic animal models compared to normal controls. Furthermore, CTRP5 may be a putative biomarker for mitochondrial dysfunction. Defects in C1QTNF5 are a cause of late-onset retinal degeneration (LORD). |
| anti-CTRP5 (human), pAb | 100 µg | AG-25A-0103-C100 | page | data sheet | Host: Rabbit. Recognizes the N-terminal half of CTRP5 full-length protein. Detects bands of ~15kDa and ~26kDa by Western blot. CTRP5 (C1qTNF-related protein 5; C1QTNF5) belongs to a highly conserved family of adiponectin paralogs. CTRP5 mediates activation of AMP-activated protein kinase (AMPK) in muscle and liver cells, thereby regulating glucose and lipid metabolism. Serum levels of CTRP5 are significantly higher in obese/diabetic animal models compared to normal controls. Furthermore, CTRP5 may be a putative biomarker for mitochondrial dysfunction. Defects in C1QTNF5 are a cause of late-onset retinal degeneration (LORD). |
| anti-CTRP5 (human), pAb | 100 µg | AG-25A-0116-C100 | page | data sheet | Host: Guinea pig. Recognizes a N-terminal region of CTRP5 full-length protein. Detects bands of ~15kDa and ~26kDa by Western blot. This antibody is CTRP5-specific. CTRP5 (C1qTNF-related protein 5; C1QTNF5) belongs to a highly conserved family of adiponectin paralogs. CTRP5 mediates activation of AMP-activated protein kinase (AMPK) in muscle and liver cells, thereby regulating glucose and lipid metabolism. Serum levels of CTRP5 are significantly higher in obese/diabetic animal models compared to normal controls. Furthermore, CTRP5 may be a putative biomarker for mitochondrial dysfunction. Defects in C1QTNF5 are a cause of late-onset retinal degeneration (LORD). |
| Cytochrome C mAb (14G6) | 100 ul | YIF-LF-MA0182 | page | data sheet | Cytochrome c is a small heme protein consisting electron-transport chain in mitochondria and transfers electrons between complex III and IV. It is highly conserved through diverse species from unicellular microorganisms to animals and plants. Cytochrome c is also an intermediate in apoptosis. Currently, it is widely accepted that mitochondria play a key role in the regulation of apoptosis. In mammalian cells, a major caspase activation pathway is the cytochrome c-initiated pathway. In this pathway, a variety of apoptotic stimuli cause cytochrome c release from mitochondria. In the cytosol, cytochrome c interacts with its adaptor molecule, Apaf-1, resulting in the recruitment, processing and activation of pro-caspase-9 in the presence of dATP or ATP. Caspase-9, in turn, cleaves and activates pro-caspase-3 and -7; these effector caspases are responsible for the cleavage of various proteins leading to biochemical and morphological features characteristic of apoptosis. Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases. |
| Cytochrome C pAb | 0.1ml | SPB-E1241-0 | page | data sheet | Cytochrome c is an electron transporting protein that resides within the inter-membrane space of the mitochondria, where it plays a critical role in the process of oxidative phosphorylation and production of cellular ATP. An increasing amount of interest has been directed toward the role which cytocrome c has been demonstrated to play in apoptotic processes. Following exposure to apoptotic stimuli, cytochrome c is rapidly released from the mitochondria into the cytosol, an event which may be required for the completion of apoptosis in some systems. Cytosolic cytochrome c functions in the activation of caspase-3, and ICE family molecule that is a key effector of apoptosis |
| Cytochrome C pAb | 0.5ml | SPB-E1241-2 | page | data sheet | Cytochrome c is an electron transporting protein that resides within the inter-membrane space of the mitochondria, where it plays a critical role in the process of oxidative phosphorylation and production of cellular ATP. An increasing amount of interest has been directed toward the role which cytocrome c has been demonstrated to play in apoptotic processes. Following exposure to apoptotic stimuli, cytochrome c is rapidly released from the mitochondria into the cytosol, an event which may be required for the completion of apoptosis in some systems. Cytosolic cytochrome c functions in the activation of caspase-3, and ICE family molecule that is a key effector of apoptosis |
| Cytochrome C pAb | 1.0ml | SPB-E1241-4 | page | data sheet | Cytochrome c is an electron transporting protein that resides within the inter-membrane space of the mitochondria, where it plays a critical role in the process of oxidative phosphorylation and production of cellular ATP. An increasing amount of interest has been directed toward the role which cytocrome c has been demonstrated to play in apoptotic processes. Following exposure to apoptotic stimuli, cytochrome c is rapidly released from the mitochondria into the cytosol, an event which may be required for the completion of apoptosis in some systems. Cytosolic cytochrome c functions in the activation of caspase-3, and ICE family molecule that is a key effector of apoptosis |
| Cytochrome C pAb (Prediluted) | 7.0ml | SPB-E1241-1 | page | data sheet | Cytochrome c is an electron transporting protein that resides within the inter-membrane space of the mitochondria, where it plays a critical role in the process of oxidative phosphorylation and production of cellular ATP. An increasing amount of interest has been directed toward the role which cytocrome c has been demonstrated to play in apoptotic processes. Following exposure to apoptotic stimuli, cytochrome c is rapidly released from the mitochondria into the cytosol, an event which may be required for the completion of apoptosis in some systems. Cytosolic cytochrome c functions in the activation of caspase-3, and ICE family molecule that is a key effector of apoptosis |
| Ferredoxin Reductase mAb (6C2) | 100 ul | YIF-LF-MA0033 | page | data sheet | Ferredoxin reductase is a ubiquitous flavoenzyme, containing noncovalently bound FAD as a prosthetic group (1). It plays a role in delivering NADPH or low potential one-electron donors such as ferredoxin and flavodoxin to redox-based metabolisms in plastids, mitochondria and bacteria (2). In mammals, ferredoxin reductase is loosely associated with the inner mitochondrial membrane and receives electrons from NADPH. These electrons are transferred to ferredoxin which shuttles electrons to cytochrome P450 in the adrenal cortex mitochondrial steroid hydroxylation systems (3). Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver. |
| Ferredoxin Reductase pAb | 100 ul | YIF-LF-PA0003 | page | data sheet | Ferredoxin reductase is a ubiquitous flavoenzyme, containing noncovalently bound FAD as a prosthetic group (1). It plays a role in delivering NADPH or low potential one-electron donors such as ferredoxin and flavodoxin to redox-based metabolisms in plastids, mitochondria and bacteria (2). In mammals, ferredoxin reductase is loosely associated with the inner mitochondrial membrane and receives electrons from NADPH. These electrons are transferred to ferredoxin which shuttles electrons to cytochrome P450 in the adrenal cortex mitochondrial steroid hydroxylation systems (3). Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver. |
| FPGS pAb | 0.1ml | SPB-E1834-0 | page | data sheet | Folylpoly-gamma-glutamate synthetase (FPGS) catalyzes the addition of several equivalents of glutamic acid to the gamma-carboxyl group in the side chain of folate cofactors and analogs. Folylpoly-gamma-glutamate synthetase has three functions in folate homeostasis in mammals: polyglutamation prevents efflux of folate cofactors from the cell, it increases the binding of folate cofactors to some of the enzymes of folate interconversion and biosynthesis, and it appears to allow the accumulation of folates in the mitochondria that are required for glycine synthesis. Folylpoly-gamma-glutamate synthetase is widely expressed in human tumors and is tightly linked either to proliferation or to a lack of differentiation. The cytotoxicity of both thymidylate synthase and purine inhibitors requires continued inhibition of target for greater than one generation time, so that the integrative function of FPGS adds considerably to the efficiency of folate antimetabolites |
| FPGS pAb | 1.0ml | SPB-E1834-4 | page | data sheet | Folylpoly-gamma-glutamate synthetase (FPGS) catalyzes the addition of several equivalents of glutamic acid to the gamma-carboxyl group in the side chain of folate cofactors and analogs. Folylpoly-gamma-glutamate synthetase has three functions in folate homeostasis in mammals: polyglutamation prevents efflux of folate cofactors from the cell, it increases the binding of folate cofactors to some of the enzymes of folate interconversion and biosynthesis, and it appears to allow the accumulation of folates in the mitochondria that are required for glycine synthesis. Folylpoly-gamma-glutamate synthetase is widely expressed in human tumors and is tightly linked either to proliferation or to a lack of differentiation. The cytotoxicity of both thymidylate synthase and purine inhibitors requires continued inhibition of target for greater than one generation time, so that the integrative function of FPGS adds considerably to the efficiency of folate antimetabolites |
| FPGS pAb | 0.5ml | SPB-E1834-2 | page | data sheet | Folylpoly-gamma-glutamate synthetase (FPGS) catalyzes the addition of several equivalents of glutamic acid to the gamma-carboxyl group in the side chain of folate cofactors and analogs. Folylpoly-gamma-glutamate synthetase has three functions in folate homeostasis in mammals: polyglutamation prevents efflux of folate cofactors from the cell, it increases the binding of folate cofactors to some of the enzymes of folate interconversion and biosynthesis, and it appears to allow the accumulation of folates in the mitochondria that are required for glycine synthesis. Folylpoly-gamma-glutamate synthetase is widely expressed in human tumors and is tightly linked either to proliferation or to a lack of differentiation. The cytotoxicity of both thymidylate synthase and purine inhibitors requires continued inhibition of target for greater than one generation time, so that the integrative function of FPGS adds considerably to the efficiency of folate antimetabolites |
| FPGS pAb (Prediluted) | 7.0ml | SPB-E1834-1 | page | data sheet | Folylpoly-gamma-glutamate synthetase (FPGS) catalyzes the addition of several equivalents of glutamic acid to the gamma-carboxyl group in the side chain of folate cofactors and analogs. Folylpoly-gamma-glutamate synthetase has three functions in folate homeostasis in mammals: polyglutamation prevents efflux of folate cofactors from the cell, it increases the binding of folate cofactors to some of the enzymes of folate interconversion and biosynthesis, and it appears to allow the accumulation of folates in the mitochondria that are required for glycine synthesis. Folylpoly-gamma-glutamate synthetase is widely expressed in human tumors and is tightly linked either to proliferation or to a lack of differentiation. The cytotoxicity of both thymidylate synthase and purine inhibitors requires continued inhibition of target for greater than one generation time, so that the integrative function of FPGS adds considerably to the efficiency of folate antimetabolites |
| Glutathione Peroxidase 1 mAb (2A10) | 100 ul | YIF-LF-MA0090 | page | data sheet | Glutathione peroxidases (Gpxs) are ubiquitously expressed proteins which catalyze the reduction of hydrogen peroxides and organic hydroperoxides by glutathione. There are several isoforms which differ in their primary structure and localization. The classical cytosolic /mitochondrial GPx1 (cGPx) is a selenium-dependent enzyme, first of the GPx family to be discovered. GPx2, also known as gastrointestinal GPx (GI-GPx), is an intracellular enzyme expressed only at the epithelium of the gastrointestinal tract (1). Extracellular plasma GPx (pGPx or GPx3) is mainly expressed by the kidney from where it is released into the blood circulation (2). Phospholipid hydroperoxide GPx4 (PH-GPx) expressed in most tissues, can reduce many hydroperoxides including hydroperoxides integrated in membranes, hydroperoxy lipids in low density lipoprotein or thymine (3). All mammalian GPx family members, except for the recently described Cys containing GPx3 and epididymis-specific secretory GPx (eGPx or GPx5) isoforms, possess selenocysteine at the active site (4-5). |
| Glutathione Peroxidase 1 mAb (42C9) | 100 ul | YIF-LF-MA0091 | page | data sheet | Glutathione peroxidases (Gpxs) are ubiquitously expressed proteins which catalyze the reduction of hydrogen peroxides and organic hydroperoxides by glutathione. There are several isoforms which differ in their primary structure and localization. The classical cytosolic /mitochondrial GPx1 (cGPx) is a selenium-dependent enzyme, first of the GPx family to be discovered. GPx2, also known as gastrointestinal GPx (GI-GPx), is an intracellular enzyme expressed only at the epithelium of the gastrointestinal tract (1). Extracellular plasma GPx (pGPx or GPx3) is mainly expressed by the kidney from where it is released into the blood circulation (2). Phospholipid hydroperoxide GPx4 (PH-GPx) expressed in most tissues, can reduce many hydroperoxides including hydroperoxides integrated in membranes, hydroperoxy lipids in low density lipoprotein or thymine (3). All mammalian GPx family members, except for the recently described Cys containing GPx3 and epididymis-specific secretory GPx (eGPx or GPx5) isoforms, possess selenocysteine at the active site (4-5). |
| Glutathione Peroxidase 3 mAb (23B1) | 100 ul | YIF-LF-MA0114 | page | data sheet | Glutathione peroxidases (Gpxs) are ubiquitously expressed proteins which catalyze the reduction of hydrogen peroxides and organic hydroperoxides by glutathione. There are several isoforms which differ in their primary structure and localization. The classical cytosolic/ mitochondrial GPx1 (cGPx) is a selenium-dependent enzyme, first of the GPx family to be discovered. GPx2, also known as gastrointestinal GPx (GI-GPx), is an intracellular enzyme expressed only at the epithelium of the gastrointestinal tract. Extracellular plasma GPx (pGPx or GPx3) is mainly expressed by the kidney from where it is released into the blood circulation. Phospholipid hydroperoxide GPx4 (PH-GPx) expressed in most tissues, can reduce many hydroperoxides including hydroperoxides integrated in membranes, hydroperoxy lipids in low density lipoprotein or thymine. All mammalian GPx family members, except for the recently described Cys containing GPx3 and epididymis-specific secretory GPx (eGPx or GPx5) isoforms, possess selenocysteine at the active site. Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. |
| Glutathione Peroxidase 3 mAb (55A) | 100 ul | YIF-LF-MA0145 | page | data sheet | Glutathione peroxidases (Gpxs) are ubiquitously expressed proteins which catalyze the reduction of hydrogen peroxides and organic hydroperoxides by glutathione. There are several isoforms which differ in their primary structure and localization. The classical cytosolic /mitochondrial GPx1 (cGPx) is a selenium-dependent enzyme, first of the GPx family to be discovered. GPx2, also known as gastrointestinal GPx (GI-GPx), is an intracellular enzyme expressed only at the epithelium of the gastrointestinal tract (1). Extracellular plasma GPx (pGPx or GPx3) is mainly expressed by the kidney from where it is released into the blood circulation (2). Phospholipid hydroperoxide GPx4 (PH-GPx) expressed in most tissues, can reduce many hydroperoxides including hydroperoxides integrated in membranes, hydroperoxy lipids in low density lipoprotein or thymine (3). All mammalian GPx family members, except for the recently described Cys containing GPx3 and epididymis-specific secretory GPx (eGPx or GPx5) isoforms, possess selenocysteine at the active site (4-5). Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. |
| Glutathione Peroxidase 4 mAb (1H11) | 100 ul | YIF-LF-MA0085 | page | data sheet | Glutathione peroxidases (Gpxs) are ubiquitously expressed proteins which catalyze the reduction of hydrogen peroxides and organic hydroperoxides by glutathione. There are several isoforms which differ in their primary structure and localization. The classical cytosolic /mitochondrial GPx1 (cGPx) is a selenium-dependent enzyme, first of the GPx family to be discovered. GPx2, also known as gastrointestinal GPx (GI-GPx), is an intracellular enzyme expressed only at the epithelium of the gastrointestinal tract (1). Extracellular plasma GPx (pGPx or GPx3) is mainly expressed by the kidney from where it is released into the blood circulation (2). Phospholipid hydroperoxide GPx4 (PH-GPx) expressed in most tissues, can reduce many hydroperoxides including hydroperoxides integrated in membranes, hydroperoxy lipids in low density lipoprotein or thymine (3). All mammalian GPx family members, except for the recently described Cys containing GPx3 and epididymis-specific secretory GPx (eGPx or GPx5) isoforms, possess selenocysteine at the active site (4-5). Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage. |
| Glutathione Peroxidase 4 mAb (7A4) | 100 ul | YIF-LF-MA0059 | page | data sheet | GPx's are ubiquitously expressed proteins which catalyze the reduction of hydrogen peroxides and organic hydroperoxides by glutathione. There are several isoforms which differ in their primary structure and localization. The classical cytosolic/mitochondrial GPx1 (cGPx) is a selenium-dependent enzyme, first of the GPx family to be discovered. GPx2, also known as gastrointestinal GPx (GI-GPx), is an intracellular enzyme expressed only at the epithelium of the gastrointestinal tract (1). Extracellular plasma GPx (pGPx or GPx3) is mainly expressed by the kidney from where it is released into the blood circulation (2). Phospholipid hydroperoxide GPx4 (PH-GPx) expressed in most tissues, can reduce many hydroperoxides including hydroperoxides integrated in membranes, hydroperoxy lipids in low density lipoprotein or thymine (3). All mammalian GPx family members, except for the recently described Cys containing GPx3 and epididymis-specific secretory GPx (eGPx or GPx5) isoforms, possess selenocysteine at the active site (4-5). Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage |
| Glutathione Peroxidase I mAb (13B2AF) | 100 ul | YIF-LF-MA0206 | page | data sheet | Glutathione peroxidases (Gpxs) are ubiquitously expressed proteins which catalyze the reduction of hydrogen peroxides and organic hydroperoxides by glutathione. There are several isoforms which differ in their primary structure and localization. The classical cytosolic/mitochondrial GPx1 (cGPx) is a selenium-dependent enzyme, first of the GPxfamily to be discovered. GPx2, also known as gastrointestinal GPx(GI-GPx), is an intracellular enzyme expressed only at the epithelium of the gastrointestinal tract (1). Extracellular plasma GPx(pGPx or GPx3) is mainly expressed by the kidney from where it is released into the blood circulation (2). Phospholipid hydroperoxide GPx4 (PH-GPx) expressed in most tissues, can reduce many hydroperoxides including hydroperoxides integrated in membranes, hydroperoxylipids in low density lipoprotein orthymine (3). All mammalian GPx family members, except for the recently described Cys containing GPx3 and epididymis-specific secretory GPx (eGPx or GPx5) isoforms, possess selenocysteine at the active site (4-5). |
| GRP75 pAb | 0.1ml | SPB-E1249-0 | page | data sheet | The HSP70 family is composed of four highly conserved proteins: HSP70, HSC70, GRP75 and GRP78. These proteins serve a variety of roles. GRP75 expression is restricted to the mitochondrial matrix and aids in the translocation and folding of nascent polypeptide chains of both nuclear and mitochondrial origin. GRP75 and GRP78 are unresponsive to heat stress and are induced by glucose deprivation |
| GRP75 pAb | 0.5ml | SPB-E1249-2 | page | data sheet | The HSP70 family is composed of four highly conserved proteins: HSP70, HSC70, GRP75 and GRP78. These proteins serve a variety of roles. GRP75 expression is restricted to the mitochondrial matrix and aids in the translocation and folding of nascent polypeptide chains of both nuclear and mitochondrial origin. GRP75 and GRP78 are unresponsive to heat stress and are induced by glucose deprivation |
| GRP75 pAb | 1.0ml | SPB-E1249-4 | page | data sheet | The HSP70 family is composed of four highly conserved proteins: HSP70, HSC70, GRP75 and GRP78. These proteins serve a variety of roles. GRP75 expression is restricted to the mitochondrial matrix and aids in the translocation and folding of nascent polypeptide chains of both nuclear and mitochondrial origin. GRP75 and GRP78 are unresponsive to heat stress and are induced by glucose deprivation |
| GRP75 pAb (Prediluted) | 7.0ml | SPB-E1249-1 | page | data sheet | The HSP70 family is composed of four highly conserved proteins: HSP70, HSC70, GRP75 and GRP78. These proteins serve a variety of roles. GRP75 expression is restricted to the mitochondrial matrix and aids in the translocation and folding of nascent polypeptide chains of both nuclear and mitochondrial origin. GRP75 and GRP78 are unresponsive to heat stress and are induced by glucose deprivation |
| GST Tag mAb (LF4G2) | 100 ul | YIF-LF-MA0052 | page | data sheet | Well known as detoxification enzymes, the glutathione transferases(GST) also function in prostaglandin and steroid hormone synthesis. The enzymes are dimmers of 25kDa subunits. There are three major groups of GSTs: canonical(or cytosolic) GSTs(cGSTs), mitochondrial GSTs, and microsomal GSTs. GSTs play a role in the metabolism of drugs, pesticides and other xenobiotics. GST is also a widely used fusion partner, since it offers both an easily detectable tag and a simple purification process that has a minimal with little effect on the biological function of the protein of interest. Recombinant hybrids containing a polypeptide fusion partner (termed °affinity tag°) to facilitate the purification of the target polypeptides are widely used. Epitope tags are useful for the labeling and detection of proteins using immunoblotting, IP and immunostaining techniques. Due to their small size, they are unlikely to affect the tagged protein°s biochemical properities. Numerous vectors containing GST-tags have been developed for both prokaryotic and eukaryotic systems over the past decade. |
| GST tag pAb | 100 ul | YIF-LF-PA0189 | page | data sheet | Well known as detoxification enzymes, the glutathione transferases (GST) also function in prostaglandin and steroid hormone synthesis. The enzymes are dimmers of 25kDa subunits. There are three major groups of GSTs: canonical (or cytosolic) GSTs (cGSTs), mitochondrial GSTs, and microsomal GSTs. GSTs play a role in the metabolism of drugs, pesticides and other xenobiotics. GST is also a widely used fusion partner, since it offers both an easily detectable tag and a simple purification process that has a minimal effect on the biological function of the protein of interest. Recombinant hybrids containing a polypeptide fusion partner (termed °affinity tag°) to facilitate the purification of the target polypeptides are widely used. Epitope tags are useful for the labeling and detection of proteins using immunoblotting, IP and immunostaining techniques. Due to their small size, they are unlikely to affect the tagged protein°s biochemical properities. Numerous vectors containing GST-tags have been developed for both prokaryotic and eukaryotic systems over the past decade. |
| hENT1 | 1.0ml | SPB-M4204 | data sheet | Human equilibrative nucleoside transporter 1 (hENT1) is a member of the equilibrative nucleoside transporter family. It is a transmembrane glycoprotein that localizes to the plasma and mitochondrial membranes and mediates the cellular uptake of nucleoside | |
| hENT1 | 0.1ml | SPB-M4200 | data sheet | Human equilibrative nucleoside transporter 1 (hENT1) is a member of the equilibrative nucleoside transporter family. It is a transmembrane glycoprotein that localizes to the plasma and mitochondrial membranes and mediates the cellular uptake of nucleoside | |
| hENT1 | 0.5ml | SPB-M4202 | data sheet | Human equilibrative nucleoside transporter 1 (hENT1) is a member of the equilibrative nucleoside transporter family. It is a transmembrane glycoprotein that localizes to the plasma and mitochondrial membranes and mediates the cellular uptake of nucleoside | |
| hENT1 | 7.0ml | SPB-M4201 | data sheet | Human equilibrative nucleoside transporter 1 (hENT1) is a member of the equilibrative nucleoside transporter family. It is a transmembrane glycoprotein that localizes to the plasma and mitochondrial membranes and mediates the cellular uptake of nucleoside | |
| anti-HSP60, mAb (264233) | 50 µg | AG-20T-0201-C050 | page | data sheet | Recognizes human, mouse and rat HSP60. Heat shock proteins (HSPs) are a family of highly conserved stress response proteins. Heat shock proteins function primarily as molecular chaperones by facilitating the folding of other cellular proteins, preventing protein aggregation or targeting improperly folded proteins to specific degradative pathways. HSPs are typically expressed at low levels under normal physiological conditions but are dramatically up-regulated in response to cellular stress. Heat Shock Protein 60 (HSP60), also known as Chaperonin 60 (CPN60), is a mitochondrial matrix protein belonging to a highly conserved family of molecular chaperone and stress response proteins. HSP60 plays a role in stabilizing and refolding proteins in response to heat shock or other cellular stress. |
| HSP70 mAb (16A12) | 100 ul | YIF-LF-MA0101 | page | data sheet | The Heat shock protein 70 (HSP70) family was found in many intracellular compartments. Members of this protein occur in chloroplasts, endoplasmic reticulum, mitochondria, and cytosol. These proteins are induced by a variety of biological stresses, including heat stress, in every organism. HSP70 serves a variety of roles: 1) It acts as molecular chaperones facilitating the assembly of multi-protein complexes, 2) It participates in the translocation of polypeptides across cell membranes and to the nucleus 3) It aids in the proper folding of nascent polypeptide chains. HSP70 is mitochondrial import machinery and plays key roles in the cytosolic endoplasmic reticulum. Recently, extracellular localized HSP have been found to play key roles in the induction of a cellular immune response. In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. |
| Mitofusin 2 Antibody | 100 µg | BVN-3882-100 | page | data sheet | Mitofusin 2 (Mfn 2) is mostly expressed in the heart and muscle tissues. It is a transmembrane protein that mediates mitochondria fusion and plays a central role in the maintenance of mitochondrial morphology. A GTPase domain is required for the function of Mitofusin proteins. Mutations in Mfn2 can lead to Charcot-Marie-Tooth disease, a common inherited disorder of the peripheral nervous system. Mfn2 may also be associated with obesity and/or apoptosis. |
| anti-NS3 (HCV), mAb (1B6) | 100 µg | AG-20B-0001-C100 | page | data sheet | Recognizes HCV NS3 (genotype 1a and 1b) (epitope mapped to NS3 aa 160-193), recognizes NS3 alone or the NS3-4A complex. Does not cross-react with HCV NS3 (genotype 2a). t The NS3 serine protease, in association with NS4A, is responsible for the cleavages of the Hepatitis C virus protease complexes NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS5B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication. Hepatitis C virus protease NS3-NS4A colocalizes with IPS-1/VISA/MAVS/Cardif in the mitochondrial membrane and has been shown to cleave the TLR3 adapter TRIF and Cardif to eliminate the antiviral signaling pathways. NS3-NS4A represents an important target for anti-HCV drugs. |
| anti-NS5B (HCV), mAb (5B-3B1) | 100 µg | AG-20B-0002-C100 | page | data sheet | Recognizes HCV NS5B (epitope mapped to NS5B aa 372-382). It recognizes genotype 1 a and also 1b (albeit with lower affinity). It does not recognize genotype 2a. The NS3 serine protease, in association with NS4A, is responsible for the cleavages of the Hepatitis C virus protease complexes NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS5B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication. Hepatitis C virus protease NS3-NS4A colocalizes with IPS-1/VISA/MAVS/Cardif in the mitochondrial membrane and has been shown to cleave the TLR3 adapter TRIF and Cardif to eliminate the antiviral signaling pathways. NS3-NS4A represents an important target for anti-HCV drugs. |
| anti-NS5B (HCV), mAb (blocking) (5B-12B7) | 100 µg | AG-20B-0003-C100 | page | data sheet | Recognizes HCV NS5B from HCV genotype 1 (epitope mapped to NS5B aa 139-392). Does not react with genotype 2. The NS3 serine protease, in association with NS4A, is responsible for the cleavages of the Hepatitis C virus protease complexes NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS5B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication. Hepatitis C virus protease NS3-NS4A colocalizes with IPS-1/VISA/MAVS/Cardif in the mitochondrial membrane and has been shown to cleave the TLR3 adapter TRIF and Cardif to eliminate the antiviral signaling pathways. NS3-NS4A represents an important target for anti-HCV drugs. |
| Peroxiredoxin 2 (Prx2) mAb (12B1) | 100 ul | YIF-LF-MA0369 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. |
| Peroxiredoxin 2 (Prx2) mAb (9A1) | 100 ul | YIF-LF-MA0368 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. |
| Peroxiredoxin 5 pAb | 100 ul | YIF-LF-PA0210 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling. |
| Peroxiredoxin 6 pAb | 100 ul | YIF-LF-PA0211 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 - 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Involved in redox regulation of the cell. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. |
| Peroxiredoxin I mAb (13E7) | 100 ul | YIF-LF-MA0069 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation. |
| Peroxiredoxin I mAb (2A4) | 100 ul | YIF-LF-MA0068 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation. |
| Peroxiredoxin I mAb (3G5) | 100 ul | YIF-LF-MA0214 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1- Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxindependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation. |
| Peroxiredoxin I mAb (9D2) | 100 ul | YIF-LF-MA0031 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation. |
| Peroxiredoxin I pAb | 100 ul | YIF-LF-PA0095 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1- Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxindependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation. |
| Peroxiredoxin I pAb | 100 ul | YIF-LF-PA0086 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation. |
| Peroxiredoxin II mAb (1E8) | 100 ul | YIF-LF-MA0144 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. |
| Peroxiredoxin II pAb | 100 ul | YIF-LF-PA0091 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1- Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxindependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. |
| Peroxiredoxin III (mouse) mAb (AF17D2FF) | 100 ul | YIF-LF-MA0329 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology particularly amino terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20-30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. |
| Peroxiredoxin III mAb (12B) | 100 ul | YIF-LF-MA0044 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol. |
| Peroxiredoxin III mAb (2B11) | 100 ul | YIF-LF-MA0043 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol. |
| Peroxiredoxin III mAb (4G10) | 100 ul | YIF-LF-MA0045 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol. |
| Peroxiredoxin III pAb | 100 ul | YIF-LF-PA0030 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol. |
| Peroxiredoxin IV mAb (1A1) | 100 ul | YIF-LF-MA0005 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation. |
| Peroxiredoxin IV mAb (3A1) | 100 ul | YIF-LF-MA0006 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation. |
| Peroxiredoxin IV mAb (7A1) | 100 ul | YIF-LF-MA0014 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation. |
| Peroxiredoxin IV pAb | 100 ul | YIF-LF-PA0009 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 4 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation. |
| Peroxiredoxin V mAb (12A) | 100 ul | YIF-LF-MA0017 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling. |
| Peroxiredoxin V mAb (3F11) | 100 ul | YIF-LF-MA0002 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling. |
| Peroxiredoxin V mAb (4C3) | 100 ul | YIF-LF-MA0001 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling. |
| Peroxiredoxin VI mAb (1A11) | 100 ul | YIF-LF-MA0013 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. |
| Peroxiredoxin VI mAb (4A3) | 100 ul | YIF-LF-MA0018 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. |
| Peroxiredoxin VI mAb (5E1) | 100 ul | YIF-LF-MA0067 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1). Involved in redox regulation of the cell. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. |
| Peroxiredoxin VI mAb (6H5) | 100 ul | YIF-LF-MA0104 | page | data sheet | Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx 6 belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 ° 30 kilodalton in molecular size and vary in subcellular localization: Prx 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol. Involved in redox regulation of the cell. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. |
| Prohibitin pAb | 1.0ml | SPB-E1775-4 | page | data sheet | Prohibitin is an evolutionarily conserved protein located in the inner membrane of mitochondria. Prohibitin appears to be a very reliable marker of mitochondria. Prohibitin shows antiproliferative activity and has been proposed to play a role in normal cell cycle regulation, replicative senescence, cellular immortalization, and tumor suppression |
| Prohibitin pAb | 0.5ml | SPB-E1775-2 | page | data sheet | Prohibitin is an evolutionarily conserved protein located in the inner membrane of mitochondria. Prohibitin appears to be a very reliable marker of mitochondria. Prohibitin shows antiproliferative activity and has been proposed to play a role in normal cell cycle regulation, replicative senescence, cellular immortalization, and tumor suppression |
| Prohibitin pAb | 0.1ml | SPB-E1775-0 | page | data sheet | Prohibitin is an evolutionarily conserved protein located in the inner membrane of mitochondria. Prohibitin appears to be a very reliable marker of mitochondria. Prohibitin shows antiproliferative activity and has been proposed to play a role in normal cell cycle regulation, replicative senescence, cellular immortalization, and tumor suppression |
| Prohibitin pAb (Prediluted) | 7.0ml | SPB-E1775-1 | page | data sheet | Prohibitin is an evolutionarily conserved protein located in the inner membrane of mitochondria. Prohibitin appears to be a very reliable marker of mitochondria. Prohibitin shows antiproliferative activity and has been proposed to play a role in normal cell cycle regulation, replicative senescence, cellular immortalization, and tumor suppression |
| Quercetin . dihydrate | 1 g | AG-CN2-0409-G001 | page | data sheet | C15H10O7 . 2H20. CAS: 6151-25-3. MW: 302.2 . 36.0. Multipotent flavonoid antioxidant. Potent free radical scavenger. Neuroprotective. Anticancer compound with chemosensitizing activity. Cell cycle arrest, apoptosis and autophagy inducer. Proteasome inhibitor. Pleiotropic kinase inhibitor, including tyrosine protein kinase (Trk), mitochondrial ATPase, cAMP- and cGMP-phosphodiesterases, PI3-kinase activity, phospholipase A2 and protein kinase C (PKC). DNA topoisomerases inhibitor. SIRT1 activator. Heat shock proteins inhibitor. Reversible fatty acid synthase inhibitor. Antithrombotic, antihistaminic and anti-inflammatory agent. Monoamine oxidase inhibitor. Vasodilatory compound. anti-diabetic compound. |
| Quercetin . dihydrate | 5 g | AG-CN2-0409-G005 | page | data sheet | C15H10O7 . 2H20. CAS: 6151-25-3. MW: 302.2 . 36.0. Multipotent flavonoid antioxidant. Potent free radical scavenger. Neuroprotective. Anticancer compound with chemosensitizing activity. Cell cycle arrest, apoptosis and autophagy inducer. Proteasome inhibitor. Pleiotropic kinase inhibitor, including tyrosine protein kinase (Trk), mitochondrial ATPase, cAMP- and cGMP-phosphodiesterases, PI3-kinase activity, phospholipase A2 and protein kinase C (PKC). DNA topoisomerases inhibitor. SIRT1 activator. Heat shock proteins inhibitor. Reversible fatty acid synthase inhibitor. Antithrombotic, antihistaminic and anti-inflammatory agent. Monoamine oxidase inhibitor. Vasodilatory compound. anti-diabetic compound. |
| anti-SLP-2, pAb | 100 µg | AG-25B-0019-C100 | page | data sheet | Host: Rabbit. Recognizes human, mouse and rat SLP-2. SLP-2 (stomatin-like protein 2) is an unusual stomatin homolog. IT is a mitochondrial protein and functions in energy process by MMP maintenance, and subsequently affecting cell motility, proliferation and chemosensitivity. SLP-2 was identified as a cancer-related gene overexpressed in human ESCC, lung cancer, laryngeal cancer, and endometrial adenocarcinoma. In tumor cells, SLP-2 promotes cell growth, cell adhesion, and tumorigenesis. |
| Smac/Diablo pAb | 100 ul | YIF-LF-PA0045 | page | data sheet | The mitochondrial protein Smac/DIABLO (second mitochondria-derived activator) performs a critical function in apoptosis by eliminating the inhibitory effect of IAPs (inhibitor of apoptosis proteins) on caspases. The newly synthesized Smac protein contains 239 amino acids. Its N-terminal 55 residues encode the mitochondrial-targeting sequence and are proteolytically removed in the mature Smac protein. In the intrinsic cell death pathway, the key event leading to the activation of caspases is the release of several pro-apoptotic proteins such as Smac/DIABLO from the intermembrane space of mitochondria into the cytosol. During apoptosis, Smac is released from mitochondria and re-activates the processed initiator and effector caspases by relieving IAP-mediated inhibition. Furthermore, Smac/DIABLO plays an important regulatory role in the sensitization of cancer cells to both immune-and drug-induced apoptosis. Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). |
| SOD1 pAb | 100 ul | YIF-LF-PA0213 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Destroys radicals which are normally produced within the cells and which are toxic to biological systems. |
| SOD2 pAb | 100 ul | YIF-LF-PA0214 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. |
| Superoxide Dismutase 1 mAb (72B1) | 100 ul | YIF-LF-MA0023 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Destroys radicals which are normally produced within the cells and which are toxic to biological systems. |
| Superoxide Dismutase 1 mAb (8A1) | 100 ul | YIF-LF-MA0029 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Destroys radicals which are normally produced within the cells and which are toxic to biological systems. |
| Superoxide Dismutase 1 pAb | 100 ul | YIF-LF-PA0013 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Destroys radicals which are normally produced within the cells and which are toxic to biological systems. |
| Superoxide Dismutase 2 mAb (1E8) | 100 ul | YIF-LF-MA0035 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Destroys radicals which are normally produced within the cells and which are toxic to biological systems |
| Superoxide Dismutase 2 mAb (23G5) | 100 ul | YIF-LF-MA0066 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Destroys radicals which are normally produced within the cells and which are toxic to biological systems |
| Superoxide Dismutase 2 mAb (2A1) | 100 ul | YIF-LF-MA0030 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Destroys radicals which are normally produced within the cells and which are toxic to biological systems |
| Superoxide Dismutase 2 mAb (4F10) | 100 ul | YIF-LF-MA0065 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Destroys radicals which are normally produced within the cells and which are toxic to biological systems |
| Superoxide Dismutase 2 pAb | 100 ul | YIF-LF-PA0021 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Destroys radicals which are normally produced within the cells and which are toxic to biological systems |
| Superoxide Dismutase 3 mAb (1H12) | 100 ul | YIF-LF-MA0121 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen. |
| Superoxide Dismutase 4 mAb (11G1) | 100 ul | YIF-LF-MA0019 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Delivers copper to copper zinc superoxide dismutase (SOD1). |
| Superoxide Dismutase 4 mAb (2A1) | 100 ul | YIF-LF-MA0016 | page | data sheet |
Superoxide dismutase (SOD) is an antioxidant
enzyme involved in the defense system against
reactive oxygen species (ROS). SOD catalyzes the
dismutation reaction of superoxide radical anion
(O2-) to hydrogen peroxide, which is then
catalyzed to innocuous O2 and H2O by glutathione
peroxidase and catalase. Several classes of SOD
have been identified. These include
intracellular copper, zinc SOD (Cu,
Zn-SOD/SOD-1), mitochondrial manganese SOD
(Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD
(EC-SOD/SOD-3) (1). SOD1 is found in all
eukaryotic species as a homodimeric 32 kDa
enzyme containing one each of Cu and Zn ion per
subunit (2). The manganese containing 80 kDa
tetrameric enzyme SOD2, is located in the
mitochondrial matrix in close proximity to a
primary endogenous source of superoxide, the
mitochondrial respiratory chain (3). SOD3 is a
heparin-binding multimer of disulfide-linked
dimers, primarily expressed in human lungs,
vessel walls and airways (4). SOD4 is a copper
chaperone for superoxide dismutase (CCS), which
specifically delivers Cu to copper/zinc
superoxide dismutase. CCS may activate
copper/zinc superoxide dismutase through direct
insertion of the Cu cofactor. Delivers copper to copper zinc superoxide dismutase (SOD1). |
| Superoxide Dismutase 4 mAb (3A1) | 100 ul | YIF-LF-MA0042 | page | data sheet | Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Delivers copper to copper zinc superoxide dismutase (SOD1). |
| Thioredoxin 1 mAb (3A1) | 100 ul | YIF-LF-MA0055 | page | data sheet | The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxido-reductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 ° 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1). Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55). |
| Thioredoxin 2 mAb (4C5) | 100 ul | YIF-LF-MA0079 | page | data sheet | Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds (1). Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations (2). Specific protein disulfide targets for reduction by Trx include protein disulfide°isomerase (PDI) (3) and a number of transcription factors such as p53 (4), NF-kappaB (5) and AP-1 (T1-151). Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins (6-7). Has an anti-apoptotic function and plays an important role in the regulation of mitochondrial membrane potential. Could be involved in the resistance to anti-tumor agents. Possesses a dithiol-reducing activity. |
| Thioredoxin 2 mAb (71G4) | 100 ul | YIF-LF-MA0080 | page | data sheet | Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds (1). Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations (2). Specific protein disulfide targets for reduction by Trx include protein disulfide°isomerase (PDI) (3) and a number of transcription factors such as p53 (4), NF-kappaB (5) and AP-1 (T1-151). Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins (6-7). Has an anti-apoptotic function and plays an important role in the regulation of mitochondrial membrane potential. Could be involved in the resistance to anti-tumor agents. Possesses a dithiol-reducing activity. |
| Thioredoxin 2 pAb | 100 ul | YIF-LF-PA0012 | page | data sheet | Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cystein residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds (1). Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations (2). Specific protein disulfide targets for reduction by Trx include protein disulfide °isomerase (PDI) (3) and a number of transcription factors such as p53 (4), NF-kappaB (5) and AP-1 (T1-151). Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins (6-7). Has an anti-apoptotic function and plays an important role in the regulation of mitochondrial membrane potential. Could be involved in the resistance to anti-tumor agents. Possesses a dithiol-reducing activity. |
| Thioredoxin Reductase 1 mAb (19A1) | 100 ul | YIF-LF-MA0015 | page | data sheet | The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxido-reductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 ° 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1). Plays a central role as a glucosyl donor in cellular metabolic pathways. |
| Thioredoxin Reductase 1 mAb (5A5) | 100 ul | YIF-LF-MA0020 | page | data sheet | The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxido-reductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 ° 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1). Plays a central role as a glucosyl donor in cellular metabolic pathways. |
| Thioredoxin Reductase 2 (TrxR2) pAb | 0.1ml | SPB-E361-0 | page | data sheet | The reduced form of thioredoxin serves as a hydrogen donor, contributes to the up-regulation of various transcription factors and binds to and inhibits MAPKKK activity. Oxidized thioredoxin is converted back to the reduced form by Thioredoxin Reductase (TrxR2), a redox active enzyme. There are two distinct isoforms in mammalian cells, TrxR1, a cytosolic protein and TrxR2, almost exclusively a mitochondrial protein. TrxR expression is induced in several tumors |
| Thioredoxin Reductase 2 (TrxR2) pAb | 1.0ml | SPB-E361-4 | page | data sheet | The reduced form of thioredoxin serves as a hydrogen donor, contributes to the up-regulation of various transcription factors and binds to and inhibits MAPKKK activity. Oxidized thioredoxin is converted back to the reduced form by Thioredoxin Reductase (TrxR2), a redox active enzyme. There are two distinct isoforms in mammalian cells, TrxR1, a cytosolic protein and TrxR2, almost exclusively a mitochondrial protein. TrxR expression is induced in several tumors |
| Thioredoxin Reductase 2 (TrxR2) pAb | 0.5ml | SPB-E361-2 | page | data sheet | The reduced form of thioredoxin serves as a hydrogen donor, contributes to the up-regulation of various transcription factors and binds to and inhibits MAPKKK activity. Oxidized thioredoxin is converted back to the reduced form by Thioredoxin Reductase (TrxR2), a redox active enzyme. There are two distinct isoforms in mammalian cells, TrxR1, a cytosolic protein and TrxR2, almost exclusively a mitochondrial protein. TrxR expression is induced in several tumors |
| Thioredoxin Reductase 2 (TrxR2) pAb (Prediluted) | 7.0ml | SPB-E361-1 | page | data sheet | The reduced form of thioredoxin serves as a hydrogen donor, contributes to the up-regulation of various transcription factors and binds to and inhibits MAPKKK activity. Oxidized thioredoxin is converted back to the reduced form by Thioredoxin Reductase (TrxR2), a redox active enzyme. There are two distinct isoforms in mammalian cells, TrxR1, a cytosolic protein and TrxR2, almost exclusively a mitochondrial protein. TrxR expression is induced in several tumors |
| Thioredoxin Reductase 2 mAb (25B3) | 100 ul | YIF-LF-MA0054 | page | data sheet | The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxido-reductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 ° 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1). Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling. |
| Thioredoxin Reductase 2 mAb (7B2) | 100 ul | YIF-LF-MA0025 | page | data sheet | The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxido-reductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 ° 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1). Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling. |
| Thioredoxin Reductase 2 pAb | 100 ul | YIF-LF-PA0024 | page | data sheet | The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxidoreductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 ° 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1). Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling. |
| TR1 pAb | 100 ul | YIF-LF-PA0023 | page | data sheet | The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxidoreductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 - 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1). Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid. |
| TR2 pAb | 100 ul | YIF-LF-PA0216 | page | data sheet | The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxidoreductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 - 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1). Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling. |
| URI mAb (SP215) | 0.5ml | SPB-M515-2 | page | data sheet | Unconventional prefoldin RPB5 interactor (URI) is an oncogene required for the survival of some human carcinomas and is often amplified and over-expressed in subsets of carcinomas from ovary, breast, stomach, and lung. Activation of URI contributes an important mechanism for activating mitochondrial S6K1-BAD signaling and promoting cell survival through disabling PP1γ-dependent negative feedback inhibition. URI can negatively modulate RNA polymerase II subunit 5 (RPB5) and mediates resistance of cells to cisplatin. |
| URI mAb (SP215) | 1.0ml | SPB-M515-4 | page | data sheet | Unconventional prefoldin RPB5 interactor (URI) is an oncogene required for the survival of some human carcinomas and is often amplified and over-expressed in subsets of carcinomas from ovary, breast, stomach, and lung. Activation of URI contributes an important mechanism for activating mitochondrial S6K1-BAD signaling and promoting cell survival through disabling PP1γ-dependent negative feedback inhibition. URI can negatively modulate RNA polymerase II subunit 5 (RPB5) and mediates resistance of cells to cisplatin. |
| URI mAb (SP215) | 0.1ml | SPB-M515-0 | page | data sheet | Unconventional prefoldin RPB5 interactor (URI) is an oncogene required for the survival of some human carcinomas and is often amplified and over-expressed in subsets of carcinomas from ovary, breast, stomach, and lung. Activation of URI contributes an important mechanism for activating mitochondrial S6K1-BAD signaling and promoting cell survival through disabling PP1γ-dependent negative feedback inhibition. URI can negatively modulate RNA polymerase II subunit 5 (RPB5) and mediates resistance of cells to cisplatin. |
| URI mAb (SP215) (Prediluted) | 7.0ml | SPB-M515-1 | page | data sheet | Unconventional prefoldin RPB5 interactor (URI) is an oncogene required for the survival of some human carcinomas and is often amplified and over-expressed in subsets of carcinomas from ovary, breast, stomach, and lung. Activation of URI contributes an important mechanism for activating mitochondrial S6K1-BAD signaling and promoting cell survival through disabling PP1γ-dependent negative feedback inhibition. URI can negatively modulate RNA polymerase II subunit 5 (RPB5) and mediates resistance of cells to cisplatin. |
| Ursodeoxycholic acid | 5 g | AG-CN2-0411-G005 | page | data sheet | C24H40O4. CAS: 128-13-2. MW: 392.6. Endogenous hydrophilic bile acid. Antioxidant. Cytoprotective against oxidative stress and cell death. Hepatoprotective at cellular and molecular level, including stabilization of membranes. Protects hepatocytes against bile acid-induced apoptosis. Antiapoptotic and antinecrotic. Targets the mitochondrial function and integrity, reduction of endoplasmatic stress and interactions with survival signals in cAMP, Akt, NF-kappaB, MAPK and PI3K signaling pathways. Modulator and finetuner of the p53-Mdm-2 complex. Chemopreventive against colorectal cancer by countering the tumor-promoting effects of secondary bile acids. Shows also effects on epidermal growth factor receptor (EGFR) signaling and COX-2 expression. Immunomodulator and anti-inflammatory compound. Modifies TLR4 and TLR9 signaling pathways and downregulates the production of proinflammatory tumor necrosis factor-alpha (TNF-alpha). Pregnane X receptor agonist. Neuroprotective. Inhibits neuronal apoptosis. Glucocorticoid Receptor (GR) agonist. Anticholestatic agent. Used to reduce cholesterol absorption and for cholesterol gallstone dissolution. Used to treat primary biliary cirrhosis (PBC). Interferes with the progression of non-alcoholic fatty liver disease (NAFLD)/NASH. Reduces CXCR3 expression. TIMP-1 inducer. ADAM17 inhibitor. |
| Ursodeoxycholic acid | 1 g | AG-CN2-0411-G001 | page | data sheet | C24H40O4. CAS: 128-13-2. MW: 392.6. Endogenous hydrophilic bile acid. Antioxidant. Cytoprotective against oxidative stress and cell death. Hepatoprotective at cellular and molecular level, including stabilization of membranes. Protects hepatocytes against bile acid-induced apoptosis. Antiapoptotic and antinecrotic. Targets the mitochondrial function and integrity, reduction of endoplasmatic stress and interactions with survival signals in cAMP, Akt, NF-kappaB, MAPK and PI3K signaling pathways. Modulator and finetuner of the p53-Mdm-2 complex. Chemopreventive against colorectal cancer by countering the tumor-promoting effects of secondary bile acids. Shows also effects on epidermal growth factor receptor (EGFR) signaling and COX-2 expression. Immunomodulator and anti-inflammatory compound. Modifies TLR4 and TLR9 signaling pathways and downregulates the production of proinflammatory tumor necrosis factor-alpha (TNF-alpha). Pregnane X receptor agonist. Neuroprotective. Inhibits neuronal apoptosis. Glucocorticoid Receptor (GR) agonist. Anticholestatic agent. Used to reduce cholesterol absorption and for cholesterol gallstone dissolution. Used to treat primary biliary cirrhosis (PBC). Interferes with the progression of non-alcoholic fatty liver disease (NAFLD)/NASH. Reduces CXCR3 expression. TIMP-1 inducer. ADAM17 inhibitor. |
| VDAC 1 pAb | 100 ul | YIF-LF-PA0155 | page | data sheet | Voltage-dependent anion channel(VDAC) proteins are abundant, pore-forming proteins belonging to the eukaryotic mitochondrial porins. It was discovered in the mitochondrial outer membrane. It also is expressed in the plasma membrane. At least three different VDAC genes have been identified in vertebrates. VDAC proteins are known to play an essential role in cellular metabolism and in the early stages of apoptosis. For example, VDAC contitutes a major pathway by which metabolites such as ADP/ATP, succinate and citrate are exchanged between the cytosol and mitochondria. And VDAC1 in the plasma membrane establishes a novel level of apoptosis regulation putatively via its redox activity. Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis. |
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