IL-8/CXCL8 Protein, Human (Biotinylated, HEK293, His-Avi)

IL-8/CXCL8 protein serves as a pivotal chemotactic factor, playing a central role in mediating inflammatory responses by attracting neutrophils, basophils, and T-cells to effectively clear pathogens and protect the host from infections. It also contributes significantly to neutrophil activation. Released in response to inflammatory stimuli, IL-8/CXCL8 exerts its effects by binding to G-protein-coupled receptors CXCR1 and CXCR2, primarily found in neutrophils, monocytes, and endothelial cells. The G-protein heterotrimer (alpha, beta, gamma subunits) constitutively binds to CXCR1/CXCR2 receptors, and activation by IL-8 leads to the release of beta and gamma subunits from Galpha (GNAI2 in neutrophils) and subsequent activation of downstream signaling pathways, including PI3K and MAPK pathways. IL-8/CXCL8 forms homodimers, and this dimerization is disrupted by tick evasin-3. Furthermore, IL-8/CXCL8 interacts with TNFAIP6 via its Link domain, and this interaction interferes with chemokine binding to glycosaminoglycans, suggesting a regulatory role in modulating chemokine activity within the inflammatory microenvironment.