Canine IL-8/CXCL8 Antibody Summary
Ala23-Pro101
Accession # P41324
Applications
Canine IL-8/CXCL8 Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Chemotaxis Induced by CXCL8/IL‑8 and Neutralization by Canine CXCL8/IL‑8 Antibody. Recombinant Canine CXCL8/IL-8 (Catalog # 1608-CL) chemoattracts the BaF3 mouse pro-B cell line transfected with human CXCR2 in a dose-dependent manner (orange line). The amount of cells that migrated through to the lower chemotaxis chamber was measured by Resazurin (Catalog # AR002). Chemotaxis elicited by Recombinant Canine CXCL8/IL-8 (10 ng/mL) is neutralized (green line) by increasing concentrations of Canine CXCL8/IL-8 Monoclonal Antibody (Catalog # MAB16081). The ND50 is typically 3-12 µg/mL.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: IL-8/CXCL8
Interleukin 8 (IL-8), also named monocyte-derived neutrophil chemotactic factor (MDNCF), neutrophil-activating protein 1 (NAP-1), neutrophil-activating factor (NAF) and granulocyte chemotactic peptide (GCP), belongs to the Glu-Leu-Arg motif containing (ELR+) CXC chemokine family and has been designated CXCL8. IL-8 is a potent neutrophil chemoattractant that recruits neutrophils to sites of inflammation. IL-8 also activates neutrophil functions and through a poorly understood mechanism, promotes angiogenesis. The biological activites of IL-8 is mediated by two types of G protein-coupled chemokine receptors, CXCR1 and CXCR2. In normal tissues, IL-8 expression and secretion is barely detectable. Upon stimulation by a wide range of pro-inflammatory signals including exposure to IL-1, TNF, bacterial or viral products, IL-8 production is rapidly induced in many different cell types. Secreted IL-8 is not glycosylated but has N-terminal sequence heterogenecity due to proteolytic processing. In human, two major forms, the 72 amino acid (aa) monocyte-derived IL-8 and the 77 aa endothelial IL-8 have been identified. Whereas the 72 aa isoform is a more potent chemoattractant, only the 77 aa isoform can induce apoptosis in leukemic cells. The N-terminal pentapeptide in the 77 aa isoform has been identified as the active site for the IL-8 apoptotic activity. Canine IL-8 encodes a 101 aa precursor protein with a putative 22 aa signal peptide. It shares 77% and 87% aa sequence identity with human and porcine IL-8, respectively. Similar to human IL-8, recombinant canine IL-8 also undergoes
N‑terminal processing. Two major peptides (the 79 aa and 74 aa variants that differ by an analogous N-terminal pentapeptide) are present in the recombinant canine IL-8 preparations.
- Van Damme, J. et al. (1998) in The Cytokine Handbook, A.W. Thomson, ed., Academic Press, New York., p. 271.
- Terui, Y. et al. (1998) Blood, 92:2672.
- Terui, Y. et al. (1999) Cancer Research 59:5651.
Product Datasheets
Citation for Canine IL-8/CXCL8 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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Lentivirus-mediated overexpression of suppressor of cytokine signaling-3 reduces neutrophilic airway inflammation by suppressing T-helper 17 responses in mice with chronic Pseudomonas�aeruginosa lung infections
Authors: Feng‑Ming Ding, Xing‑Yi Zhang, Yu‑Qing Chen, Ruo‑Min Liao, Guo‑Gang Xie, Peng‑Yu Zhang et al.
International Journal of Molecular Medicine
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