|Detection of Mouse Pro‑MMP‑7 by Western Blot. Western blot shows lysates of NS0 mouse myeloma cell line transfected with with mouse MMP-7. PVDF Membrane was probed with 2 µg/mL of Mouse Pro‑MMP‑7 Monoclonal Antibody (Catalog # MAB29671) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). For additional reference, active rmMMP-7 was derived from the proteolytic activation of Recombinant Mouse MMP-7 (Catalog # 2967-MP) (20 ng/lane) and probed with 1 µg/mL of Mouse MMP‑7 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2967). Specific bands were detected for Pro‑MMP‑7 at approximately 35 kDa and active MMP‑7 at approximately 23 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‑7 (matrilysin) is expressed in epithelial cells of normal and diseased tissues and is capable of digesting a large series of proteins of the extracellular matrix including collagen IV and X, gelatin, casein, laminin, aggrecan, entactin, elastin, and versican (1). MMP-7 is implicated in the activation of other proteinases such as plasminogen, MMP-1, MMP-2, and MMP-9. In addition to its roles in connective tissue remodeling and cancer, MMP-7 also regulates intestinal alpha ‑defensin activation in innate host defense, releases tumor necrosis factor-alpha in a model of herniated disc resorption and cleaves FasL to generate a soluble form in a model of prostate involution. Structurally, MMP-7 is the smallest of the MMPs and consists of two domains: a pro-domain that is cleaved upon activation and a catalytic domain containing the zinc-binding site.
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