Detection of Human Pro‑MMP‑12 by Western Blot. Western blot shows lysates of human heart tissue. PVDF membrane was probed with 2 µg/mL of Goat Anti-Human MMP‑12 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF917) followed by|
HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for Pro‑MMP‑12 at approximately 54 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.
|MMP‑12 in Human Squamous Cell Carcinoma. MMP‑12 was detected in immersion fixed paraffin-embedded sections of human squamous cell carcinoma using Goat Anti-Human MMP‑12 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF917) at 10 µg/mL overnight at 4 °C. Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # CTS013). Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to cancer cells. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
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 (1). 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 rhMMP-12 corresponds to the pro form that can be activated by autocatalysis under the conditions described above.