Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor. Human recombinant Interleukin-8 produced in yeast is a single, glycosylated polypeptide chain containing 79 amino acids and having a molecular mass of 9 kDa.
Human IL8 expressed in Pichia Pastoris
CAT# CSC-CTK0238-25 (25 μg); CAT# CSC-CTK0238-125 (125 μg)
Greater than 98% as determined by SDS-PAGE and RP-HPLC analysis.
Specific activity of IL-8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 25 ng/ml.
Sterile-filtered, white, lyophilized (freeze-dried) powder. Lyophilized from a protein solution containing 20 mM phosphate buffer (pH 8).
Please centrifuge product briefly before opening vial. The lyophilized protein should be reconstituted in sterile, ultra-pure water to a concentration of 0.1-1.0 mg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted protein should be used immediately or stored long-term in undiluted working aliquots at -20°C. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
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