IL 8 Canine
Description
Detection and Quantification Methods
IL-8 Canine is quantified using specialized immunoassays. Below is a comparison of commercially available kits:
Biological Roles in Canine Pathophysiology
IL-8 Canine drives inflammatory and angiogenic processes, with implications in both health and disease:
Neutrophil Activation
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Chemotaxis: Recombinant human IL-8 induces dose-dependent migration of canine neutrophils at concentrations ≥10⁻⁸ M, peaking at 10⁻⁶ M (Table 1) .
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Shape Change: Rapid activation occurs at 10⁻⁹–10⁻⁷ M IL-8, enhancing neutrophil adhesion to endothelial cells .
Table 1: Neutrophil Migration in Response to IL-8
| IL-8 Concentration | PMN/HPF (Mean ± SEM) | Significance |
|---|---|---|
| Buffer control | 6.66 ± 1.35 | — |
| 10⁻⁹ M | 6.88 ± 0.40 | ns |
| 10⁻⁸ M | 11.50 ± 1.74 | p < 0.01 |
| 10⁻⁶ M | 55.67 ± 7.76 | p < 0.001 |
Data from . HPF = High-power field; ns = not significant.
Angiogenesis and Tumor Progression
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Hemangiosarcoma (HSA): IL-8 is upregulated in canine HSA, promoting tumor growth and vascularization .
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Mammary Carcinoma: Elevated serum IL-8 correlates with metastasis, recurrence, and poor prognosis. IL-8 levels > 20,000 pg/mL are linked to advanced clinical stages .
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Osteosarcoma (OS): IL-8 enhances OS cell migration and VEGF expression, supporting a pro-metastatic microenvironment .
Clinical Relevance in Canine Diseases
IL-8 serves as a diagnostic and prognostic biomarker across multiple conditions:
Research Applications and Neutralization
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Antibody Neutralization: Mouse Anti-Canine IL-8/CXCL8 Antibody (MAB1608) blocks chemotaxis at 0.3–1.2 µg/mL, confirming IL-8’s role in neutrophil recruitment .
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Tumor Microenvironment: In OS, IL-8 upregulates VEGF expression, supporting angiogenesis. Blocking CXCR1/CXCR2 with Reparixin reduces migration but not proliferation .
Product Specs
Product Science Overview
Interleukin-8 (IL-8), also known as CXCL8, is a proinflammatory chemokine that plays a crucial role in the immune response by attracting neutrophils to sites of infection or inflammation. In canines, recombinant IL-8 is produced to study its functions and potential therapeutic applications.
Recombinant canine IL-8 is typically produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain containing 79 amino acids, with a molecular mass of approximately 9.1 kDa . The protein is purified using proprietary chromatographic techniques to ensure high purity and activity.
IL-8 is a potent neutrophil chemoattractant, meaning it recruits neutrophils to sites of inflammation. It also activates neutrophil functions, such as degranulation and the respiratory burst, which are essential for the destruction of pathogens . Additionally, IL-8 promotes angiogenesis, the formation of new blood vessels, through mechanisms that are not yet fully understood .
The biological activities of IL-8 are mediated by two types of G protein-coupled chemokine receptors, CXCR1 and CXCR2 . These receptors are expressed on the surface of neutrophils and other immune cells, allowing IL-8 to exert its effects by binding to these receptors and activating intracellular signaling pathways.
Recombinant canine IL-8 is used in various research applications to study its role in the immune response and its potential therapeutic uses. For example, it is used to investigate the mechanisms of neutrophil recruitment and activation, as well as its role in inflammatory diseases and cancer . Additionally, recombinant IL-8 can be used as a standard in ELISA assays to measure IL-8 levels in biological samples .
