Anti-MMP7 Antibody Picoband® fluoro594 Vervoeging

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.

Matrilysin;3.4.24.23; Matrin; Matrix metalloproteinase-7; MMP-7; Pump-1 protease; Uterine metalloproteinase; MMP7; MPSL1, PUMP1

MMP7

4316

P09237

Human

No cross-reactivity with other proteins

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.

Widely distributed in various tissues.

Flow Cytometry

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

Immunogen affinity purified.

Liquid

Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase. .

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.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

29677 MW

No cross reactivity with other proteins.

6

Matrilysin

Secreted, extracellular space, extracellular matrix .

Belongs to the peptidase M10A family.

Matrilysin

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.