anti-Acetyl-alpha-Tubulin (Lys40), Rabbit Monoclonal (RM318)

  REV-31-1204-00-R100 100 µl

Data Sheet:    

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All Vertebrates  

ICC, WB  

Rabbit  

This antibody reacts to alpha-Tubulin acetylated at Lysine 40. No cross reactivity to non-acetylated alpha-Tubulin at Lysine 40. This antibody may also react to mouse or rat Acetyl- alpha-Tubulin at Lysine 40, as predicted by immunogen homology.  

RM318  

Protein A purified.  

BLUE ICE  

-20°C  

Stable for at least 1 year after receipt when stored at -20°C.  

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Description

 

Recombinant Antibody. This antibody reacts to alpha-Tubulin acetylated at Lysine 40. No cross reactivity to non-acetylated alpha-Tubulin at Lysine 40. This antibody may also react to mouse or rat Acetyl- alpha-Tubulin at Lysine 40, as predicted by immunogen homology. Applications: WB, ICC. Source: Rabbit. Liquid. 50% Glycerol/PBS with 1% BSA and 0.09% sodium azide. Microtubules are key elements of the eukaryotic cytoskeleton that dynamically assemble from heterodimers of α- and β-tubulin. Two different mechanisms can generate microtubule diversity: the expression of different α- and β-tubulin genes, referred to as tubulin isotypes, and the generation of posttranslational modifications (PTMs) on α- and β-tubulin. Tubulin PTMs include the well-known acetylation or phosphorylation, and others that have so far mostly been found on tubulin, detyrosination/tyrosination, polyglutamylation and polyglycylation. These PTMs might have evolved to specifically regulate tubulin and microtubule functions. Tubulin acetylation was discovered on K40 of flagellar α-tubulin in Chlamydomonas reinhardtii and is generally enriched on stable microtubules in cells. It is located on the microtubule lumenal surface. As a result of its localization at the inner face of microtubules, K40 acetylation might rather affect the binding of microtubule inner proteins, a poorly characterized family of proteins. Functional experiments in cells have further suggested that K40 acetylation regulates intracellular transport by regulating the traffic of kinesin motors probably by indirect mechanisms. Acetyltransferase α-Tat1 (or Mec-17) specifically acetylate α-tubulin K40. Acetylation of tubulin by α-Tat1 accumulates selectively in stable, long-lived microtubules thus explaining the link between this posttranslational modication and stable microtubules in cells. However, the direct cellular function of K40 acetylation on microtubules is still unclear.

 

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