Anti-MMP2, clone MMP2/1501

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced) and 0.05% sodium azide. It recognizes a protein of 72 kDa, which is identified as MMP2. The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, Fibronectin, Laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP2 (also designated type IV collagenase) cleaves collagen types IV,V, VII and X and gelatin type I. Activation of MMP2 secretion requires the Ras signaling pathway. Protein function: 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 in association with MMP14. [The UniProt Consortium]