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Description
Biotin anti-human MMP-9. MMP9, or MMP-9, is a member of the matrix metalloprotease family of proteins (MMPs). Members of this family are structurally related, zinc-containing enzymes that degrade the extracellular matrix (ECM) and connective tissue proteins. Proteolytic activities of MMPs play an important role in vascular remodeling, cellular migration, and the processing of ECM proteins and adhesion molecules. MMP9 consists of a prodomain, catalytic domain, hinge region, and a hemopexin domain. It is secreted as an inactive zymogen that becomes activated extracellularly. The most relevant natural activators of proMMP9 are unknown. MMP9 activation may be mediated by removal of the prodomain by serine proteases or other MMPs, or it may be a direct response to oxidative stress that disrupts the cysteine switch. MMP9 is capable of processing cytokines and chemokines. For example, it is reported to release the biologically active form of vascular endothelial growth factor (VEGF), which indicates that MMP9 may play a crucial role in the formation of new blood vessels. Increased MMP9 expression and activity has been shown to be related to various cancers, as it may contribute to the release of metastatic cells from the bulk tumor as well as their entrance at the site of metastasis by degrading proteins in the ECM and basement membrane.
Immunogen
Recombinant Human MMP-9
Other Names
Gelatinase B, Type IV collagenase, 92 kD gelatinase, Type V collagenase, GELB, CLG4B, MMP-9, MANDP2