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  • 产品名称：MatrixMetalloproteinase2(MMP2)(AA30-660)(Active)protein(Histag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
MatrixMetalloproteinase2(MMP2)(AA30-660)(Active)protein(Histag)
详情介绍：
Characteristics rh MMP2 is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 71.8 kDa. The predicted N-terminus is Ala 30. The reducing (R) protein migrates as 66-71 kDa in SDS-PAGE .
Purity >92 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
ProductDetails: Biological Activity Comment Biological Activity: Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2. The specific activity is >1,000 pmol/min/μg.
Background Matrix metalloproteinase-2 (MMP-2) is also known as 72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A and CLG4A, which belongs to the peptidase M10A family. MMP-2 / CLG4A contains 3 fibronectin type-II domains and 4 hemopexin-like domains. MMP-2 is produced by normal skin fibroblasts. MMP-2 cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln. MMP2 involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin.
Molecular Weight 71.8 kDa
UniProt P08253
Research Area Extracellular Matrix
Pathways Activation of Innate immune Response
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 50 mM Tris, 150 mM NaCl, pH 8.0
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 6 months (4 °C), After reconstitution under sterile conditions for 1 month (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for Matrix Metalloproteinase 2 (MMP2) (AA 30-660) (Active) protein (His tag) (ABIN2181511) Human MMP-2, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained ov...
Background publications al-Rakaf, Bello, Turkustani, Adenubi: "Intra-nasal midazolam in conscious sedation of young paediatric dental patients." in: International journal of paediatric dentistry / the British Paedodontic Society [and] the International Association of Dentistry for Children, Vol. 11, Issue 1, pp. 33-40, 2001 (PubMed).

Bello, Lucini, Carrabba, Giussani, Machluf, Pluderi, Nikas, Zhang, Tomei, Villani, Carroll, Bikfalvi, Black: "Simultaneous inhibition of glioma angiogenesis, cell proliferation, and invasion by a naturally occurring fragment of human metalloproteinase-2." in: Cancer research, Vol. 61, Issue 24, pp. 8730-6, 2001 (PubMed).

Fernandez-Patron, Stewart, Zhang, Koivunen, Radomski, Davidge: "Vascular matrix metalloproteinase-2-dependent cleavage of calcitonin gene-related peptide promotes vasoconstriction." in: Circulation research, Vol. 87, Issue 8, pp. 670-6, 2000 (PubMed).

Fernandez-Patron, Radomski, Davidge: "Vascular matrix metalloproteinase-2 cleaves big endothelin-1 yielding a novel vasoconstrictor." in: Circulation research, Vol. 85, Issue 10, pp. 906-11, 1999 (PubMed).

Brooks, Silletti, von Schalscha, Friedlander, Cheresh: "Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity." in: Cell, Vol. 92, Issue 3, pp. 391-400, 1998 (PubMed).