Human MMP‑12 Antibody

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.