Sino Biological offers quality reagents for matrix metalloproteinase related study, including recombinant proteins, antibodies, ELISA kits, and ORF cDNA clones.
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Matrix metalloproteinases (MMPs), a subfamily of metalloproteinases, are zinc-dependent endopeptidases. They share a common domain structure. The three common domains are the pro-peptide, the catalytic domain and the haemopexin-like C-terminal domain which is linked to the catalytic domain by a flexible hinge region. Matrix metalloproteinases are characterized by their ability of degrading extracellular matrix proteins, but they can also process a number of bioactive molecules. Matrix metalloproteinases are involved in the cleavage of cell surface receptors, the release of apoptotic ligands (such as the FAS ligand), as well as chemokines and cytokines. Matrix metalloproteinases are also thought to play a major role in a variety of biological processes, such as cell differentiation and proliferation, cell migration/adhesion, apoptosis, angiogenesis, and host defense (innate immunity). Loss of the exquisite control of the MMP system leads to extensive and often destructive degradation of the extracellular matrix as seen in arthritis, cancer, congestive heart failure, and osteoarthritis. On the basis of their massive up-regulation in malignant tissues and their unique ability to degrade all components of the extracellular matrix, matrix metalloproteinases have been heralded as promising targets for cancer therapy. Matrix metalloproteinases are inhibited by specific endogenous tissue inhibitor of metalloproteinases (TIMPs), which comprise a family of four protease inhibitors: TIMP-1, TIMP-2, TIMP-3 and TIMP-4. Other natural inhibitors of MMPs include Î±2-macroglobulin (Î±2M) and endostatin.