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Introduction | Matrix metalloproteinase-2 (MMP-2) is a type IV collagenase, which is involved in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. MMP-2 contains a number of distinct domains: a prodomain that is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin like domain believed to have a role in substrate targeting; and a carboxyl terminal (hemopexin like) domain containing 2 N-linked glycosylation. The MMP-2 can degrade an extensive array of substrates including type IV, V, VII and X collagens as well as gelatin type I. In addition, MMP-2 interacts with THBS2, TIMP2, Thrombospondin 1, CCL7 and TIMP4. MMP-2 autocatalytic cleavage in the C-terminal generates the anti-angiogenic peptide, PEX. This process seems to be made possible by binding integrinv/beta3. Defects in the MMP-2 are the cause of Torg-Winchester syndrome (TWS), aka multicentric osteolysis nodulosis and arthropathy (MONA). |
Synonyms | 72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II. |
Source | HEK293 cells. |
Physical Appearance | The MMP-2 is supplied as a sterile Filtered colorless solution. |
Formulation | The MMP-2 is supplied as a 0.2 |
Stability | Store MMP-2 at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time.Avoid multiple freeze-thaw cycles. |
Purity | Greater than 95% as determined by SDS-PAGE. |
Biological Activity | The activity was measured by its ability to cleave the colorimetric peptide substrate, Mca-PLGL-DpaAR-NH2, The specific activity is > 1,000 pmoles/min/ |
Usage | NeoScientific's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drµgs, agricultural or pesticidal products, food additives or household chemicals. |
References | Title:MMP-2 regulates human platelet activation by interacting withintegrin aIIbb 3.Publication:To cite this article: Choi W-S, Jeon O-H, Kim H-H, Kim D-S. MMP-2 regulates human platelet activation by interacting with integrin aIIbb3.J Thromb Haemost 2008; 6: 517–23.Link:http://onlinelibrary.wiley.com/doi/10.1111/j.1538-7836.2007.02871.x/pdf |
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