IL-8/CXCL8 Protein, Canine
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. IL-8/CXCL8 Protein, Canine is produced in E.coil, and consists of 79 amino acids (A23-P101).
- Species: Canine
- Source: E. coli
-
Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
-
Biological Activity
-
Technical Parameters
-
Product Properties
- Documentation
- References
- Help & FAQs
Biological Activity
Description
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, Canine is produced in E.coil, and consists of 79 amino acids (A23-P101).
Background
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].
In Vitro
Recombinant Canine IL-8 (5 μg; for 12 weeks; transplantation of biphasic scaffolds) induces massive bone regeneration in beagles[7].
In Vivo
Recombinant Canine IL-8 (1-1 nM; 15-45 min) markedly increases adhesion of neutrophils to isolated canine cardiac myocytes[6].
Technical Parameters
-
Species Canine
-
Source E. coli
-
Tag Tag Free
-
Accession
P41324 (A23-P101)
-
Molecular Construction
-
N-term
-
IL-8 (A23-P101)
Accession # P41324 -
C-term
-
-
Protein Length
Full Length of Mature Protein
-
Synonyms
CXCL8; Lung Giant Cell Carcinoma-Derived Chemotactic Protein; Prev. IL8; Alveolar Macrophage Chemotactic Factor I; MDNCF; Tumor Necrosis Factor-Induced Gene 1; NAP-1; Neutrophil-Activating Peptide 1; MONAP; T-Cell Chemotactic Factor; GCP-1; Interleukin 8;
-
AA Sequence
AVLSRVSSELRCQCIKTHSTPFHPKYIKELRVIDSGPHCENSEIIVKLFNGNEVCLDPKEKWVQKVVQIFLKKAEKQDP
-
Predicted Molecular Mass
9.2 kDa
-
Molecular Weight
Approximately 9 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.
-
Purity
≥ 95%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
References
[1]. M Baggiolini, et al. Neutrophil-activating peptide-1/interleukin 8, a novel cytokine that activates neutrophils. J Clin Invest. 1989 Oct;84(4):1045-9. [Content Brief]
[2]. M Wolf, et al. Granulocyte chemotactic protein 2 acts via both IL-8 receptors, CXCR1 and CXCR2. Eur J Immunol. 1998 Jan;28(1):164-70. [Content Brief]
[3]. Qian Liu, et al. The CXCL8-CXCR1/2 pathways in cancer. Cytokine Growth Factor Rev. 2016 Oct;31:61-71. [Content Brief]
[4]. Jian-Feng Liu, et al. IL-8 Is Upregulated in the Tissue-Derived EVs of Odontogenic Keratocysts. Biomed Res Int. 2022 Jul 30;2022:9453270. [Content Brief]
[5]. Remo C Russo, et al. The CXCL8/IL-8 chemokine family and its receptors in inflammatory diseases. Expert Rev Clin Immunol. 2014 May;10(5):593-619. [Content Brief]
[6]. G L Kukielka, et al. Interleukin-8 gene induction in the myocardium after ischemia and reperfusion in vivo. J Clin Invest. 1995 Jan;95(1):89-103. [Content Brief]
[7]. Dong Suk Yoon, et al. Synergistic Action of IL-8 and Bone Marrow Concentrate on Cartilage Regeneration Through Upregulation of Chondrogenic Transcription Factors. Tissue Eng Part A. 2016 Feb;22(3-4):363-74. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
Powered by Bioz
