IL-8/CXCL8 Protein, Human

IL-8/CXCL8 protein, a vital chemotactic factor, orchestrates inflammatory responses by attracting neutrophils, basophils, and T-cells to clear pathogens. It activates neutrophils and binds to CXCR1/CXCR2 receptors, initiating downstream signaling pathways. IL-8/CXCL8 homodimerizes, disrupted by tick evasin-3, and interacts with TNFAIP6, potentially regulating chemokine activity in the inflammatory microenvironment. IL-8/CXCL8 Protein, Human is the recombinant human-derived IL-8/CXCL8 protein, expressed by E. coli , with tag free. The total length of IL-8/CXCL8 Protein, Human is 77 a.a., with molecular weight of ~11.0 kDa.

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.

Human

E. coli

Tag Free

P10145 (A23-S99)

3576  [NCBI]

AVLPRSAKELRCQCIKTYSKPFHPKFIKELRVIESGPHCANTEIIVKLSDGRELCLDPKENWVQRVVEKFLKRAENS

Approximately 11.0 kDa

• 
  Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.