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RP-77536 is a purified recombinant MMP-24 (catalytic domain) protein purified from E. coli periplasm. MT5-MMP catalytic domain is produced by activation of a recombinant soluble proform of MT5-MMP. Activation generates two molecular species. One species begins at the N-terminus with Tyr156 of full-length MT5-MMP, while the other species is two amino acid residues shorter and starts with Leu158. Both species extend to Ser351 of MT5-MMP.
All cells within tissues are surrounded by an extracellular matrix (ECM) giving the tissues shape and structure. The ECM is constantly being remodeled and constant communication is maintained between cells through this matrix. Secreted proteins, termed matrix metalloproteinases (MMPs), are involved in the modulation of cell-matrix interactions. MMPs are Zn (2+)-binding endopeptidases that degrade various components of the ECM. MMPs are enzymes implicated in normal and pathologic tissue remodeling processes, wound healing, angiogenesis, and tumor invasion. These enzymes are very potent when active, and are associated with extracellular space inhibitors called TIMPs (tissue inhibitors of matrix metalloproteinases). TIMPs have been shown to block tumor cell invasion suggesting that they act as metastasis suppressor genes.
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