Human MMP-3 Alexa Fluor® 405-conjugated Antibody Summary
Accession # P08254
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of MMP-3 in Human MG-63 Cell Line byFlow Cytometry. MG-63 Human osteosarcoma cell line was stainedwith Mouse Anti-HumanMMP-3 Alexa Fluor® 405-conjugated Monoclonal Antibody (Catalog #IC513V, filled histogram) or isotype control antibody (Catalog # IC002V,open histogram). To facilitate intracellular staining, cells were fixed withFlow Cytometry Fixation Buffer (Catalog # FC004)and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I(Catalog # FC005).View our protocol for Staining Intracellular Molecules.
Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
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-3 (stromelysin-1), can degrade a broad range of substrates including collagen alpha chains, aggrecan, laminin, fibronectin, elastin, casein, alpha -1 antitrypsin, myelin basic protein, IL-1 beta, IGFBP-3, pro MMP-1, pro MMP-7, pro MMP-8, pro MMP-9 and pro MMP-13. MMP-3 does not cleave the triple helical region of interstitial collagens, a characteristic which distinguishes the stromelysins from the collagenases. The MMP-3 substrate repertoire extends beyond extracellular matrix proteins and implicates MMP-3 in roles other than direct tissue remodelling, for instance, enzyme cascades and cytokine regulation. MMP-3 is expressed by fibroblasts, chrondrocytes, osteoblasts, endothelial cells, smooth muscle cells and macrophages. Structurally, MMP-3 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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