Intracellular Staining by Flow Cytometry
|Detection of MMP‑3 in MG‑63 Human Cell Line by Flow Cytometry. MG‑63 human osteosarcoma cell line was stained with Mouse Anti-Human MMP‑3 PE‑conjugated Monoclonal Antibody (Catalog # IC513P, filled histogram) or isotype control antibody (Catalog # IC002P, open histogram). To facilitate intracellular staining, cells were fixed with Flow Cytometry Fixation Buffer (Catalog # FC004) and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I (Catalog # FC005). View our protocol for Staining Intracellular Molecules.|
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.