- 入驻时间: 2012-04-17
- 联系人:客户经理
- 电话:400-968-7988
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- Email:fuwu@bioleaf.com
Catalogue number
ENZ-769
Synonyms
kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.
Introduction
Matrix metalloproteinase-2 (MMP-2) 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 ; 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).
Description
Source
Physical Appearance
Formulation
Stability
Avoid multiple freeze-thaw cycles.
Purity
References
Publication: Journal of Biological Chemistry 285.53 (2010): 41270-41279.
Link:http://www.jbc.org/content/285/53/41270.full
Amino acid sequence
Safety Data Sheet
SDS