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Recombinant Rat MMP2 protein (His Tag) (PDMR100093)

All Size Price Qty
500μg $ 1440.00
100μg $ 488.00
20μg $ 158.00
1mg $ 2340.00
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For research use only.

Synonyms 72 kDa gelatinase, 72 kDa type IV collagenase, EC 3.4.24.24, Gelatinase A, MMP-2, Matrix metalloproteinase-2
Species Rat
Expression Host HEK293 Cells
Sequence Met1-Cys662
Accession P33436
Calculated Molecular Weight 72.7 kDa
Observed Molecular Weight 72 kDa
Tag C-His
Bio-activity Not validated for activity
Purity > 95% as determined by reducing SDS-PAGE.
Endotoxin < 1.0 EU/mg of the protein as determined by the LAL method
Storage Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping This product is provided as lyophilized powder which is shipped with ice packs.
Formulation Lyophilized from a 0.2 μm filtered solution in PBS with 5% Trehalose and 5% Mannitol.
Reconstitution It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis.
Background Ubiquitinous metalloproteinase that is 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. Involved in the formation of the fibrovascular tissues. 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. Ligand for integrin alpha-v/beta3 on the surface of blood vessels.
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