Human Interleukin-8 (72AA) Recombinant

IL-8 is produced by stimulated monocytes but not by tissue macrophages or T-lymphocytes. In many cell types the synthesis of IL-8 is strongly stimulated by IL-1 and TNF-alpha. In human skin fibroblasts, the expression of IL-8 is enhanced by Leukoregulin.The expression of IL-8 from resting and stimulated human blood monocytes is up-regulated by IL-7. In chondrocytes, the synthesis of IL-8 is stimulated by IL1-beta TNF-alpha and bacterial lipopolysaccharides. In human astrocytes, the synthesis and secretion of IL-8 is induced by IL-1 and TNF-alpha. The IL-8 receptor (CD128) is a dimeric glycoprotein consisting of a 59 kDa and a 67 kDa subunit. It is expressed in many different cell types including those not responding to IL-8. The biological activities of IL-8 resemble those of a related protein, NAP-2. IL-8 differs from all other cytokines in its ability to specifically activate neutrophil granulocytes. In neutrophils, IL-8 causes a transient increase in cytosolic calcium levels and the release of enzymes from granules. IL-8 also enhances the metabolism of reactive oxygen species and increases chemotaxis and the enhanced expression of adhesion molecules. Pre-activation by IL-3 is required to render basophils and neutrophils susceptible to further activation by IL-8. Native human IL-8, generated by the proteolytic removal of the signal peptide and propeptide, has a calculated molecular mass of approximately 8 kDa.

Reconstitute at 0.1-1.0 mg/ml in distilled water. This solution can then be diluted into other buffers. To maximize product collection from vial surface, vortex briefly and then spin down to recollect the liquid.

The lyophilized protein is stable for at least 2 years from date of receipt when stored at -20°C. Upon reconstitution, store in working aliquots at +4°C for up to one month, or at -20°C for up to six months, in the presence of a carrier protein. Avoid repeated freeze/thaw cycles.