protein_function: Ubiquitinous metalloproteinase that is involved indiverse functions such as remodeling of the vasculature,angiogenesis, tissue repair, tumor invasion, inflammation, andatherosclerotic plaque rupture. As well as degrading extracellularmatrix proteins, can also act on several nonmatrix proteins suchas big endothelial 1 and beta-type CGRP promotingvasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appearsto have a role in myocardial cell death pathways. Contributes tomyocardial oxidative stress by regulating the activity ofGSK3beta. Cleaves GSK3beta in vitro. Involved in the formation ofthe fibrovascular tissues in association with MMP14.
Type IV collagenase, 72-kD, is officially designated matrix metalloproteinase-2(MMP2). It is also known as gelatinase, 72-kD. MMP-2 plays an essential role in angiogenesis and arteriogenesis, two processes critical to restoration of tissue perfusion after ischemia. MMP-2 expression is increased in tissue ischemia, but the responsible mechanisms remain unknown. Matrix metalloproteinases(MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide(cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability. The gene is localized to 16q21 using somatic cell hybrids and in situ hybridization. The standard product used in this kit is recombinant human MMP-2, consisting of 631 amino acids with the molecular mass of 71KDa. The detected MMP-2 includes zymogen and active enzyme.