|Detection of Mouse MMP‑12 by Western Blot. Western blot shows lysates of mouse small intestine tissue. PVDF membrane was probed with 0.25 µg/mL of Goat Anti-Mouse MMP‑12 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3467) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for MMP‑12 at approximately 50 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
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-12 (macrophage elastase) is found in macrophages and its expression in monocytes can be induced by cytokines such as GM-CSF and CD40 signaling. In addition to elastin, MMP-12 can degrade a broad spectrum of substrates, including type IV collagen, fibronectin, laminin, vitronectin, proteoglycans, chondroitin sulfate, myelin basic protein, alpha 1-antitrypsin, and plasminogen. It can also activate MMP-2 and MMP-3. MMP-12 is required for macrophage-mediated proteolysis and matrix invasion in mice. MMP-12 is proposed to have a direct role in the pathogenesis of aortic aneurysms and in the development of pulmonary emphysema that results from chronic inhalation of cigarette smoke. Structurally, the pro-MMP-12 consists of following domains: a pro domain, a catalytic domain containing the zinc-binding site, and a C-terminal hemopexin-like domain. The recombinant mouse MMP-12 corresponds to the pro form that can be activated.
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Western Blot: Mouse MMP-12 Antibody [AF3467]
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