Anti-MMP7 Antibody Picoband® Fluoro488 Conjugated

Matrix metalloproteinase-7 (MMP-7) previously called putative metalloproteinase I (PUMP1) or matrilysin. The MMP-7 gene has been identified through studies of collagenase-related connective-tissue-degrading metalloproteinases produced by human tumors. The MMP-7 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. MMP-7, 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, MMP-7 mRNA is regulated in a specific and distinct manner in normal and malignant tissues. MMP-7 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. MMP-7 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.

E.coli-derived human MMP7 recombinant protein (Position: M1-K267) . Human MMP7 shares 71% amino acid (aa) sequence identity with both mouse and rat MMP7.

Angiogenesis, Cancer, Cardiovascular, Cell Biology, Cytoskeleton/ECM, ECM Enzymes, Extracellular Matrix, Invasion/Microenvironment, Metalloprotease, Proteolysis/Ubiquitin, Proteolytic Enzymes, Signal Transduction, Tumor Biomarkers

1. Masaki, T.; Matsuoka, H.; Sugiyama, M.; Abe, N.; Goto, A.; Sakamoto, A.; Atomi, Y. Matrilysin (MMP-7) as a significant determinant of malignant potential of early invasive colorectal carcinomas. Brit. J. Cancer 84: 1317-1321, 2001. 2. Gaire, M.; Magbanua, Z.; McDonnell, S.; McNeil, L.; Lovett, D. H.; Matrisian, L. M. Structure and expression of the human gene for the matrix metalloproteinase matrilysin. J. Biol. Chem. 269: 2032-2040, 1994. 3. Zuo, F.; Kaminski, N.; Eugui, E.; Allard, J.; Yakhini, Z.; Ben-Dor, A.; Lollini, L.; Morris, D.; Kim, Y.; DeLustro, B.; Sheppard, D.; Pardo, A.; Selman, M.; Heller, R. A. Gene expression analysis reveals matrilysin as a key regulator of pulmonary fibrosis in mice and humans. Proc. Nat. Acad. Sci. 99: 6292-6297, 2002.