protein

MMP-2 Protein, Rat (P. pastoris, His)

HY-P700573

20 μg;50 μg;100 μg

180;325;480 USD

MMP-2 Protein, Rat (P. pastoris, His)

proteins

P. pastoris

20 μg;50 μg;100 μg

180;325;480 USD

MMP-2 is a multifunctional metalloproteinase that plays multiple roles in vasculature remodeling, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. In addition to degrading extracellular matrix proteins, MMP-2 also acts on non-matrix proteins to promote vasoconstriction. MMP-2 Protein, Rat (P. pastoris, His) is the recombinant rat-derived MMP-2 protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of MMP-2 Protein, Rat (P. pastoris, His) is 553 a.a., with molecular weight of 64.1 kDa.

Rat

MMP-2, a ubiquitinous metalloproteinase, plays a multifaceted role in diverse biological processes, encompassing vasculature remodeling, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. Beyond its conventional role in degrading extracellular matrix proteins, MMP-2 exhibits versatility by acting on non-matrix proteins like big endothelial 1 and beta-type CGRP, thereby promoting vasoconstriction. Additionally, it cleaves KISS at a Gly- -Leu bond and appears implicated in myocardial cell death pathways, contributing to myocardial oxidative stress through the regulation of GSK3beta activity, which it cleaves in vitro. Remarkably, the C-terminal non-catalytic fragment of MMP-2, known as PEX, possesses anti-angiogenic and anti-tumor properties, inhibiting cell migration and adhesion to FGF2 and vitronectin while serving as a ligand for integrin alpha-v/beta3 on the surface of blood vessels.

rHu72 kDa type IV collagenase/MMP-2, His ; 72 kDa Type IV Collagenase; 72 kDa Gelatinase; Gelatinase A; Matrix Metalloproteinase-2; MMP-2; TBE-1; MMP2; CLG4A

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of PBS, 6% Trehalose, pH 7.4.

Room temperature in continental US; may vary elsewhere.