Interleukin-8, or IL-8, the prototypic member of the C-X-C, or alpha, family of chemokines, is a chemoattractant cytokine involved in the chemotaxis and activation of neutrophils. IL-8 expression has been correlated to a large number of chronic inflammatory diseases, including inflammatory bowel disease (IBD) and atherosclerosis. IL-8 is cleaved from a 99 amino acid precursor to a 72 amino acid, nonglycosylated, and biologically active protein. Whether IL-8 functions in vivo as a monomer or a hydrogen-bonded dimer has not yet been resolved. Two IL-8 receptors, designated IL-8RA and IL-8RB, have been described and share 77% sequence identity. Both are seven-transmembrane domain proteins (7TMD), similar to the G protein-coupled receptors, and, in addition to IL-8, serve as receptors for other members of the alpha and beta chemokine families.

The antibody is stable for at least 1 year from the date of receipt when stored at -20°C to -70°C. Reconstituted antibody can also be aliquotted and stored at 4°C for 1 month or at -20°C to -70°C in a manual defrost freezer for many months without detectable loss activity. Please avoid freeze-thaw cycles.

This antibody was selected for its ability to detect human IL-8 in Sandwich ELISA and Array. In ELISA, this antibody shows approximately 5% cross-reactivity with human IL-1b, and no crossreactivity with murine IL-8 and other tested proteins.