IL 8 Human (1-77), His

Interleukin-8 (IL-8), also known as CXCL8, is a pro-inflammatory chemokine that plays a crucial role in the immune response by attracting neutrophils to sites of infection or inflammation. The recombinant form of IL-8, specifically the 1-77 amino acid sequence with a His tag, is widely used in research to study its biological functions and potential therapeutic applications.

IL-8 is a member of the CXC chemokine family and is characterized by the presence of a conserved ELR motif (Glu-Leu-Arg) near its N-terminus, which is essential for its angiogenic properties . The recombinant IL-8 (1-77 a.a) is an 8.9 kDa protein containing 77 amino acid residues . The His tag facilitates purification and detection of the protein in various experimental setups.

IL-8 functions primarily as a chemoattractant for neutrophils, guiding them to sites of infection or injury. It binds to the CXCR1 and CXCR2 receptors on the surface of neutrophils, triggering a cascade of intracellular signaling events that result in chemotaxis . Additionally, IL-8 has been shown to promote angiogenesis, the formation of new blood vessels, which is critical in wound healing and tumor growth .

Recombinant IL-8 (1-77 a.a) is typically produced using an E. coli expression system. The gene encoding IL-8 is cloned into an expression vector that includes a sequence for the His tag. The vector is then introduced into E. coli cells, which express the recombinant protein. Following expression, the protein is purified using affinity chromatography, leveraging the His tag for selective binding to a nickel or cobalt resin .

Recombinant IL-8 is used extensively in immunological research to study its role in inflammation, immune response, and cancer biology. It is also employed in functional assays to investigate neutrophil chemotaxis and angiogenesis . Furthermore, IL-8 serves as a valuable tool in drug development, particularly in the search for anti-inflammatory and anti-cancer therapies.