Matrix metalloproteinase-7(MMP-7) previously called putative metalloproteinase I(PUMP1) or matrilysin. The PUMP1 gene has been identified through studies of collagenase-related connective-tissue-degrading metalloproteinases produced by human tumors. The PUMP I protein has 267 amino acids and is significantly shorter than stromelysin or collagenase(477 and 469 amino acids, respectively). Matrix metalloproteinases play a crucial role in tumor invasion and metastasis. Matrilysin, a member of the matrix metalloproteinase family, is structurally different from the other matrix metalloproteinases by virtue of the absence of a conserved COOH-terminal protein domain. In addition, matrilysin mRNA is regulated in a specific and distinct manner in normal and malignant tissues. Matrilysin has been shown to correlate with nodal or distant metastasis in colorectal carcinomas; however, its implication in early invasive colorectal carcinomas has not been determined.1 Matrilysin is also a mediator of pulmonary fibrosis and a potential therapeutic target. The standard product used in this kit is recombinant human MMP-7, consisting of 250 amino acids with the molecular mass of 28KDa. The detected MMP-7 includes zymogen and active enzyme.
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