|MMP‑16/MT3‑MMP in Human Breast. MMP‑16/MT3‑MMP was detected in immersion fixed paraffin-embedded sections of human breast using Goat Anti-Human MMP‑16/MT3‑MMP Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1785) at 15 µg/mL overnight at 4 °C. 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 cytoplasm of epithelial 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 (ECM). MMP-16 (MT3-MMP) is found in brain, lung, placenta, smooth muscle cells, and malignant tumor tissues including oral melanoma and renal carcinoma (1). MMP-16 has been shown to activate proMMP-2 and degrade various ECM components including native collagens (2, 3). MMP-16 has been proposed to possess the potential to directly enhance the growth and invasiveness of cells in vivo, two critical processes for development and carcinogenesis (4). Structurally, MMP-16 consists of the following domains: a pro domain containing the furin cleavage site, a catalytic domain containing the zinc-binding site, a hinge region, a hemopexin-like domain, a transmembrane domain, and a cytoplamasic tail (1). The structure of the catalytic domain in complex with a hydroxamate inhibitor has been solved (5). The rhMMP-16PC consists of the pro and catalytic domains, which can be activated by treatment with furin.
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