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Amino Acid Sequence: SAKELRCQCIKTYSKPFHPKFIKELRVIESGPHCANTEIIVKLSDGRELCLDPKENWVQRVVEKFLKRAENS
Background: 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.
Biological Activity: Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.
Description: Recombinant human Interleukin-8 is a disulfide-linked monomer protein consisting of 73 amino acid residues, migrates as an approximately 8 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Interleukin-8 mature chain was expressed in E. coli.
Endotoxin Level: <0.1 ng/µg (1 EU/µg), using the LAL gel clot method.
Format: lyophilized protein
Formulation: Lyophilized from a 0.2 µm filtered PBS solution, pH 7.5
Genbank: P10145
Purity: ≥95% by SDS-PAGE and HPLC
Reconstitution: 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.
Storage Stability: 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.
Uniprot: P10145
Warnings: Avoid freeze/thaw cycles.
Biosafety Level: Not applicable (BSL-1)
References: Orjalo, A., et al. 2009. Proc. Natl. Acad. Sci. 106:17030-5.
2. Stillie, R.M., et al. J. Leukoc. Biol., Sep 2009, 86: 529 - 543.
3. Bautista, M.V., et al. J. Immunol., Aug 2009, 183: 2159 - 2166.
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