Anti-Interleukin 8 (IL8)

Interleukin 8 (IL-8), a member of the neutrophil-specific CXC subfamily of chemokines, is a potent neutrophil chemotactic and activating factor. It is a primary inflammatory cytokine produced by many cells in response to proinflammatory stimuli such as IL-1, TNF, LPS and viruses. Its function is, in part, to attract neutrophils to the site of inflammation and to activate them. The IL-8 cDNA sequence predicts a protein of 99 amino acids. Removal of a 22-residue signal peptide generates a mature protein of 77 amino acids (ca. 8 kDa). Further proteolysis of the N-terminal end leads to a variant form with 72 amino acids, full activation of IL-8 may require cleavage to the 72 amino acid form. IL-8 can form non-covalent dimers in solution, especially at high concentrations, but dimerization is not necessary for biological activity.

Western blotting: 1:100-400, Immunocytochemistry in formalin fixed cells: 1:100-500, Immunohistochemistry in formalin fixed frozen section: 1:100-500, Immunohistochemistry in paraffin section: 1:50-417

3-10C, CXCL8, AMCF-I, GCP1, K60, LECT, LUCT, LYNAP, MDNCF, MONAP, NAF, NAP1, SCYB8, TSG1, B-ENAP, Chemokine C-X-C Motif Ligand 8

Guinea Pig