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Matrix Metalloproteinase-7 (MMP-7)

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.1 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.2 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.3 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.



1 results found in Immunoassays
1 results found in Planar Arrays.


Product: Size:

Matrix Metalloproteinase-7 (MMP-7) Human ELISA

Type: Sandwich ELISA, Biotin-labelled antibody

RD193438200CS 96 wells (1 kit)

Product: Size:

Q-Plex™ Human MMP 7

RQS467949HU 96 wells (1 kit)
Find more on Matrix Metalloproteinase-7 (MMP-7) on pubmed


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