IL-8 (77 a.a.), human recombinant

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Background

Interleukin-8 (IL-8) is a proinflammatory CXC chemokine produced by macrophages, epithelial cells. IL-8 is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. In vivo, IL-8 exists in two forms: a 77 a.a. protein produced by endothelial cells, and the more active 72 a.a. protein produced by monocytes. IL-8 (72 a.a.) has a 5-10 fold higher activity on neutrophil activation compared to IL-8 (77 a.a.). The receptors for IL-8 are the seven-helical G-protein coupled receptors CXCR1 and CXCR2, exclusively expressed on neutrophils. IL-8 serves as a chemical signal that attracts neutrophils at the site of inflammation and thus enhances the antimicrobial actions of defense cells.The human IL-8 cDNA encodes a 99 aa protein with a 20 aa signal sequence. Recombinant human IL-8 (endothelial-derived) is a 8.9 kDa protein containing 77 amino acid residues.