Rat MMP-8 Antibody Summary
Leu21-Pro466
Accession # O88766
Applications
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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Detection of Rat MMP‑8 by Western Blot. Western blot shows lysates of rat lung tissue and rat spleen tissue. PVDF membrane was probed with 1 µg/mL of Mouse Anti-Rat MMP-8 Monoclonal Antibody (Catalog # MAB3245) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). A specific band was detected for MMP-8 at approximately 53 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
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: MMP-8
Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-8 (neutrophil collagenase, collagenase 2) is expressed in neutrophils, where it is stored in specific granules. MMP-8 release from the neutrophils is stimulated by various factors such as interleukins 1 and 8, TNF-alpha and GM-CSF. MMP-8 is capable of cleaving types I, II, and III triple-helical collagen, gelatin peptides, fibronectin, proteoglycans, aggrecan, serpins, beta -casein, and peptides such as angiotensin and substance P. In addition to its function in phagocytosis, MMP-8 has a high capacity for infiltrating connective tissue and is implicated in the breakdown of the extracellular matrix in diseases such as rheumatoid arthritis. Structurally, MMP-8 consists of several domains: a pro-domain that is cleaved upon activation, a catalytic domain containing the zinc-binding site, a short hinge region, and a hemopexin-like domain (1). The amino acid sequence of rat MMP-8 shares 91%, 75% and 73% identity with that of mouse, dog and human, respectively.
- Tschesche, T. et al. (2004) Handbook of Proteolytic Enzymes (eds. A.J. Barrett et al.) p.480, Academic Press, San Diego.
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