|Detection of Human MMP‑1 by Western Blot. Western blot shows lysates of IMR‑90 human lung fibroblast cell line and PC‑3 human prostate cancer cell line. PVDF membrane was probed with 2 µg/mL of Recombinant Mouse Anti-Human MMP‑1 Monoclonal Antibody (Catalog # MAB901R) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). A specific band was detected for MMP‑1 at approximately 50 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|MMP‑1 in Human Liver. MMP‑1 was detected in immersion fixed paraffin-embedded sections of human liver using Recombinant Mouse Anti-Human MMP‑1 Monoclonal Antibody (Catalog # MAB901R) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Mouse HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS002) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm in hepatocytes. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
|Western Blot Shows Human MMP‑1 Specificity by Using Knockout Cell Line. Western blot shows lysates of PC‑3 human prostate cancer parental cell line and MMP-1 knockout PC‑3 cell line (KO). PVDF membrane was probed with 2 µg/mL of Mouse Anti-Human MMP‑1 Monoclonal Antibody (Catalog # MAB901R) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). A specific band was detected for MMP‑1 at approximately 50 kDa (as indicated) in the parental PC‑3 cell line, but is not detectable in knockout PC‑3 cell line. GAPDH (Catalog # AF5718) is shown as a loading control. This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-1 (interstitial collagenase), can degrade a broad range of substrates including types I, II, III, VII, VIII, and X collagens as well as casein, gelatin, alpha ‑1 antitrypsin, myelin basic protein, L-Selectin, pro-TNF, IL-1 beta, IGF-BP3, IGF-BP5, pro MMP-2 and pro MMP-9. A significant role of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling, characterized by the cleavage of the interstitial collagen triple helix into ¾, ¼ fragments. However, as the list of substrates above illustrates, the role of MMP-1 is more diverse than originally envisaged, and may involve enzyme cascades, cytokine regulation and cell surface molecule modulation. MMP-1 is expressed by fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. Structurally, MMP-1 may be divided into several distinct domains; a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexin-like) domain.