Interleukin-8 is one of the first discovered chemokines and belongs to the CXCL family, in which the first two conserved cysteines are separated by one residue. 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. The receptors for IL-8 are the seven-helical G-protein coupled receptors CXCR1 and CXCR2, exclusively expressed on neutrophils. The functions of IL-8 are to induce rapid changes in cell morphology, activate integrins, and release the granule contents of neutrophils. Thus, IL-8 can enhance the antimicrobial actions of defense cells.
Recombinant human Interleukin-8 (IL-8, 77aa)/CXCL8 produced in E. coli is a single non-glycosylated polypeptide chain containing 77 amino acids. A fully biologically active molecule, rhIL-8(77aa)/CXCL8 has a molecular mass of 8.9 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.