IL-8 (human):Fc (human) (rec.) (non-lytic)

  CHI-HF-22008-C010 10 µg

Data Sheet:    

---

Human  

CHO cells  

>98% (SDS-PAGE)  

BLUE ICE  

+4°C  

-20°C  

Stable for at least 1 year after receipt when stored at -20°C. Working aliquots are stable for up to 3 months when stored at -20°C.  

---

Description

 

Protein. The extracellular domain of human IL-8 (aa 23-99) is fused to the N-terminus of the Fc region of a mutant human IgG1. Source: CHO cells. Endotoxin content: <0.06EU/µg protein (LAL test; Lonza). Lyophilized from 0.2µm-filtered solution in PBS. Purity: >98% (SDS-PAGE). Interleukin-8 (IL-8) was originally discovered as a neutrophil chemotactic and activating factor and is a member of the alpha (CXC) subfamily of chemokines (including also platelet factor 4, GRO, IP-10, etc.). Many cell types, including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, keratinocytes, hepatocytes, chondrocytes and various tumor cell lines, produce IL-8 in response to a wide variety of proinflammatory stimuli such as exposure to IL-1, TNF, LPS and viruses. IL-8 has a wide range of other proinflammatory effects. It is a potent chemoattractant for neutrophils and causes degranulation of neutrophil specific granules and azurophilic granules. IL-8 induces expression of the cell adhesion molecules CD11/CD18 and enhances the adherence of neutrophils to endothelial cells and subendothelial matrix proteins. Besides neutrophils, IL-8 is also chemotactic for basophils, T cells and eosinophils. IL-8 has been reported to be a co-mitogen for keratinocytes and was also shown to be an autocrine growth factor for melanoma cells. IL-8 was also reported to be angiogenic both in vivo and in vitro.

 

---