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RP-77534 is a purified recombinant MMP-15 (catalytic domain) protein purified from E. coli periplasm. MT2-MMP catalytic domain is produced by activation of a recombinant soluble proform of MT2-MMP. This domain represents more than 95% of the protein. The catalytic domain is inhibited by tissue inhibitors of matrix metalloproteinases 2 and 3 (TIMP-2 and TIMP-3) and by chelators of divalent cations like EDTA or o-phenanthroline. This product can be used to study the activation of TIMP-2 and the degradation of proteins of the extracellular matrix. The enzyme allows screening of TIMP inhibitors and characterization of inhibitor action.
MMPs are a group of enzymes involved in matrix degradation. Of the sixteen members of matrix metalloproteinase family ten exist in soluble form whereas MT-MMPs exist as integral membrane proteins. MT1-MMP, MT2-MMP, MT3-MMP also known as MMP14, MMP15, MMP16 respectively contain a C-terminal transmembrane domain anchoring them to the cell surface. They have an 8 amino acid insert in their catalytic domain. MT1-MMP cleaves progelatinase A (MMP-2) and progelatinase B to their active forms. MT2-MMP plays a minor role in activation of pro-MMP-2 to its active form in breast carcinomas. Coexpression of MT1-MMP and MT2-MMp in advanced stages of breast carcinomas is indicative of possible involvement of MT2-MMP in its metastasis.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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