Epithelial Neutrophil-Activating Protein 78 (CXCL5), amino acids 8-78, human recombinant (rHuENA78)

Human recombinant Epithelial Neutrophil-Activating Protein 78 produced in E.coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids (8-78) and having a molecular mass of 7.8kDa. Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils, and can be inhibited with the type II interferon IFN-?. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.