|Detection of Human MMP‑1 by Western Blot. Western blot shows lysates of HEK001 human epidermal keratinocyte cell line. PVDF membrane was probed with 5 µg/mL of Goat Anti-Human MMP‑1 Monoclonal Antibody (Catalog # MAB9011) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). 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.|
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, IGFBP-3, IGFBP-5, 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.
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