Anti-MMP7

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Matrix metalloproteinase-7, previously called putative metalloproteinase I (PUMP1) or Matrilysin has been identified through studies of collagenase-related connective-tissue-degrading metalloproteinases produced by human tumors. The MMP7 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. MMP7, 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, MMP7 mRNA is regulated in a specific and distinct manner in normal and malignant tissues. MMP7 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. MMP7 is also a mediator of pulmonary fibrosis and a potential therapeutic target.