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RP-77531 is a purified recombinant MMP-14 (catalytic domain) protein, expressed in E.coli. MT1-MMP catalytic domain is produced by activation of a recombinant soluble proform of MT1-MMP purified from E. coli periplasm. 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.
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 protein, and this activity may be involved in tumor invasion.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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