|MMP‑9 in MMP‑9 transfected NS0 Mouse Cell Line. MMP‑9 was detected in immersion fixed MMP-9 transfected NS0 mouse myeloma cell line using Goat Anti-Human MMP‑9 Polyclonal Antibody (Catalog # AB911) at 5 µg/mL for 3 hours at room temperature. Cells were stained (red) and counterstained (green). Specific labeling was localized to the cytoplasm. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.|
|MMP‑9 in Human Liver Cancer Tissue. MMP‑9 was detected in immersion fixed paraffin-embedded sections of human liver cancer tissue using Goat Anti-Human MMP‑9 Polyclonal Antibody (Catalog # AB911) at 10 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 in cancer cells. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
The matrix metalloproteinases (MMPs) consist of 24 known human zinc proteases with essential roles in breaking down components of the extracellular matrix (ECM). Additional MMP substrates include cytokines, chemokines, growth factors and binding proteins, cell/cell adhesion molecules, and other proteinases. With a few exceptions, MMPs share common structural motifs including a pro-peptide domain, a catalytic domain, a hinge region, and a hemopexin-like domain. Synthesized as pro-enzymes, most MMPs are secreted before conversion to their active form. MMP activities are modulated on several levels including transcription, pro-enzyme activation, or by their endogenous inhibitors, tissue inhibitors of metalloproteinases (TIMPs). A subset of MMPs are associated with membranes and designated as membrane-type metalloproteinases (MT-MMP).
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