Interleukin-8 (IL-8), also known as CXCL8, is a proinflammatory chemokine that plays a crucial role in the immune response by attracting neutrophils to sites of infection or inflammation. In canines, recombinant IL-8 is produced to study its functions and potential therapeutic applications.
Recombinant canine IL-8 is typically produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain containing 79 amino acids, with a molecular mass of approximately 9.1 kDa . The protein is purified using proprietary chromatographic techniques to ensure high purity and activity.
IL-8 is a potent neutrophil chemoattractant, meaning it recruits neutrophils to sites of inflammation. It also activates neutrophil functions, such as degranulation and the respiratory burst, which are essential for the destruction of pathogens . Additionally, IL-8 promotes angiogenesis, the formation of new blood vessels, through mechanisms that are not yet fully understood .
The biological activities of IL-8 are mediated by two types of G protein-coupled chemokine receptors, CXCR1 and CXCR2 . These receptors are expressed on the surface of neutrophils and other immune cells, allowing IL-8 to exert its effects by binding to these receptors and activating intracellular signaling pathways.
Recombinant canine IL-8 is used in various research applications to study its role in the immune response and its potential therapeutic uses. For example, it is used to investigate the mechanisms of neutrophil recruitment and activation, as well as its role in inflammatory diseases and cancer . Additionally, recombinant IL-8 can be used as a standard in ELISA assays to measure IL-8 levels in biological samples .