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The Anti-IL-8 Protein A Scaffold molecule was selected against human recombinant IL-8. Cross reactivity with other species has not been tested. The Anti-IL-8 Protein A Scaffold molecule is an ideal affinity ligand as capture reagent in ELISA. The Anti-IL-8 Protein A Scaffold molecule is modified with a unique C-terminal cysteine for directed single-point chemical modification, facilitating labeling with fluorescent dyes, biotin or coupling to matrices.
Anti-IL-8 Protein A scaffold molecule binds to human IL-8. Cross reactivity with other species has not been tested.
At +4°C is recommended for lyophilized protein. For reconstituted protein in physiological buffer, short-term storage at +4°C is recommended. For long-term storage, the protein solution should first be aliquoted and stored frozen at -20°C. There is no dec
Interleukin 8 (IL-8) or CXCL8 is a non-glycosylated protein of 8 kDa belonging to the CXC family of chemokines. IL-8 is produced as a precursor protein of 99 amino acids and processing of the precursor results in variants of IL-8 that have various biological effects. It is produced by a number of cell types in response to inflammatory stimuli such as LPS, TNF and viruses. The IL-8 receptor belongs to the G-protein coupled receptor family and is expressed on many cell types including neutrophilic granulocytes. The role of IL-8 is primarily to attract neutrophilic granulocytes to the site of inflammation upon binding to the receptor. IL-8 causes a transient increase in cytosolic calcium levels, the release of enzymes from granules as well as enhanced expression of adhesion molecules in neutrophils.
chemokine activity; interleukin-8 receptor binding; protein binding.