protein

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

HY-P70569

2 μg;10 μg;50 μg

70;180;540 USD

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

proteins

HEK293

2 μg;10 μg;50 μg

70;180;540 USD

Interleukin-8 (IL-8), also known as CXCL8 or NAP-1, is a pro-inflammatory CXC chemokine. IL-8 acts on human neutrophils via two receptors, CXCR1 and CXCR2. IL-8 has a conserved Glu-Leu-Arg (ELR) N-terminal motif, and is an agonist for CXCR1/CXCR2. IL-8 is produced by various cells including leukocytes, endothelial cells, and epithelial cells [1] [2] [3] . IL-8/CXCL8 Protein, Human (HEK293, His) is produced in HEK293 cells with six C-Terminal His-tags. It consists of 79 amino acids (E21-S99).

Human

IL-8 (CXCL8) belongs to the ELR + CXC chemokines family. IL-8 is initially produced as a protein of 99 amino acids that undergoes cleavage to form active IL-8 isoforms, a 77 amino acid peptide in non-immune cells or a 72 amino acid peptide in monocytes and macrophages. The gene encoding IL-8 is located on chromosome 4q13-q21. Dimerisation of IL-8 forms the structural basis for receptor binding. IL-8 is expressed by various cells including monocytes, macrophages, leukocytes, endothelial cells, and epithelial cells [1] [2] [3] . Mature human IL-8/CXCL8 shares 75% amino acid sequence identity with canine IL-8/CXCL8. While, human IL-8 shares 94.95% aa sequence identity with Rhesus Macaque IL-8 protein. IL-8 is responsible for the recruitment and activation of neutrophils and granulocytes to the site of inflammation. IL-8 is almost undetectable in physiological states, but is rapidly induced by pro-inflammatory cytokines such as TNFα and IL-1β. The function of IL-8 mainly relies on its interaction with specific cell surface GPCR, CXCR1 and CXCR2. In addition, IL-8 is reported to promote integrin β3 upregulation and the invasion of hepatocellular carcinoma cells through activation of the PI3K/Akt pathway. In odontogenic lesions, IL-8 has been proven to be highly expressed in ameloblastoma epithelial cells and irreversible pulpitis. In rheumatoid arthritis and other inflammatory joint diseases IL-8 could bring about the accumulation of neutrophils, which are considered a major source of cartilage-degrading enzymes. IL-8 stimulates the MAPK and tyrosine phosphorylation of cellular proteins. Tumour cells and fibroblasts communicate with each other, including autocrine and paracrine factors, including IL-8, resulting in the upregulation of MMP2 and MMP9 degradable extracellular matrix (ECM) components that trigger tumour invasion [1] [2] [3] [4] .   IL-8 is typically known to promote angiogenesis, but it also activates matrix metalloproteinase (MMP) that is involved in metastasisrelated tissue remodelling. IL-8 is induced in lipopolysaccharide (LPS)-stimulated monocytes and shown to induce neutrophil migration. IL-8 exerts multiple effects on biological activities of tumour cells including proliferation, invasion and migration. IL-8 also increases the expression of Akt in androgen-independent prostate cancer (AIPC) cell lines. IL-8 activates MAPK signalling via PI3K in neutrophils, and via transactivation of EGFR resulting in Ras-GTPase activation in ovarian and lung cancer cell lines. There is substantial amount of experimental data suggesting that IL-8 and receptors contribute to elimination of pathogens, but may also contribute significantly to disease-associated processes, including tissue injury, fibrosis, angiogenesis and tumorigenesis [3] [5] .

Interleukin-8; IL-8; C-X-C Motif Chemokine 8; CXCL8; Emoctakin; Granulocyte Chemotactic Protein 1; GCP-1; Monocyte-Derived Neutrophil Chemotactic Factor; MDNCF; Monocyte-Derived Neutrophil-Activating Peptide; MONAP; Neutrophil-Activating Protein 1; NAP-1

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4.

Room temperature in continental US; may vary elsewhere.