Reactivity | CaSpecies Glossary |
Applications | B/N, ELISA(Cap) |
Clone | 258901 |
Clonality | Monoclonal |
Host | Mouse |
Conjugate | Unconjugated |
Concentration | LYOPH |
Immunogen | E. coli-derived recombinant canine IL-8/CXCL8 Ala23-Pro101 Accession # P41324 |
Specificity | Detects canine IL-8/CXCL8 in ELISAs. In ELISAs, no cross-reactivity with recombinant feline IL-8/CXCL8, recombinant human CXCL8/IL-8, recombinant porcine CXCL8/IL-8, recombinant canine (rca) IL‑1 beta /IL‑1F2, or rcaCXCL6/IL‑6 is observed. |
Source | N/A |
Isotype | IgG1 |
Clonality | Monoclonal |
Host | Mouse |
Gene | IL8 |
Purity Statement | Protein A or G purified from hybridoma culture supernatant |
Endotoxin Note | <0.10 EU per 1 μg of the antibody by the LAL method. |
Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
Dilutions |
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Application Notes | ELISA Capture: Canine CXCL8/IL-8 Antibody (Catalog # MAB16081) ELISA Detection: Canine CXCL8/IL-8 Biotinylated Antibody (Catalog # BAM16082) Standard: Recombinant Canine CXCL8/IL-8 (Catalog # 1608-CL) |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
Preservative | No Preservative |
Concentration | LYOPH |
Reconstitution Instructions | Reconstitute at 0.5 mg/mL in sterile PBS. |
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.
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