MMP2 Antibody

Background

Matrix metalloproteases (matrix metalloproteinase, MMPs), also called matrixins, are zinc-dependent endopeptidases and the major proteases in ECM degradation. MMPs can degrade several extracellular molecules and several bioactive molecules. MMP2 is a gelatinase A, type IV collagenase, that contains three fibronectin type II repeats in its catalytic site that allow binding of denatured type IV and V collagen and elastin. Unlike most MMP family members, activation of this protein can occur on the cell membrane. This enzyme can be activated extracellularly by proteases, or, intracellularly by its S-glutathiolation with no requirement for proteolytical removal of the pro-domain. This protein is thought to be involved in multiple pathways including roles in the nervous system, endometrial menstrual breakdown, regulation of vascularization, metastasis, tissue repair, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, it can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. MMP2 also cleaves KISS at a Gly- -Leu bond. It appears to have a role in myocardial cell death pathways and contributes to myocardial oxidative stress by regulating the activity of GSK3beta. It cleaves GSK3beta in vitro and is involved in the formation of the fibrovascular tissues in association with MMP14. PEX, the C-terminal non-catalytic fragment of MMP2, possesses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. MMP2 is a ligand for integrin/beta3 on the surface of blood vessels. Anti-MMP2 antibody is useful for researchers interested in osteolysis, nodulosis, arthropathy, Apoptosis Research, and Cytokines & Growth Factor Antibodies.