This Antibody was verified by Neutralization to ensure that the antibody binds to the antigen stated. View Details
In direct ELISAs, approximately 40% cross-reactivity with recombinant canine IL-8 is observed and 15% cross-reactivity with recombinant porcine IL-8 and recombinant human IL-8 is observed.\r
Reconstitute at 0.2 mg/mL in sterile PBS.\r
Endoxin level is <0.10 EU per 1 µg of the antibody by the LAL method.
Interleukin 8 (IL-8, CXCL8) is a 72 amino acid pro-inflammatory factor which belongs to the CXC subfamily of chemokines, and are bound by the cell surface receptors IL-8RA and IL-8RB. IL-8 functions as a chemoattractant and potent angiogenic factor. The expression and secretion of IL-8 can be induced by diverse inflammatory stimuli in many cells, including macrophages and endothelial cells. In endothelial cells, IL-8 is present in storage vesicles called Weibel-Palade bodies. IL-8, first isolated from osteosarcoma cells, contains the ELR-motif (N-terminal Glu-Leu-Arg amino acid sequence) and signals through the CXCR1 and CXCR2 receptors. Previous nomenclature for IL-8 includes neutrophil activating protein 1 (NAP-1), granulocyte chemotactic protein 1 (GCP-1), monocyte-derived neutrophil-activating peptide (MONAP) and protein 3-10C. IL-8 and ten other members of the CXC chemokine gene family form a chemokine gene cluster in a region mapped to chromosome 4q. Cancer studies have demonstrated a role for IL-8 in the angiogenesis and growth of tumours, and IL-8 is believed to play a role in the pathogenesis of bronchiolitis, a common respiratory tract disease caused by viral infection.