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. MMP-9 consists of a prodomain, catalytic domain, hinge region, and a hemopexin domain, and is secreted as an inactive zymogen that becomes activated extracellularly. The most relevant natural activators of proMMP-9 are unknown. MMP-9 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. MMP-9 is capable of processing cytokines and chemokines. For example, it is reported to release the biologically active form of vascular endothelial growth factor (VEGF), indicating that MMP-9 may play a crucial role in the formation of new blood vessels. MMP-9 participates in the migration of immune cells as demonstrated by MMP-9 knockout mice after antigen challenge. Increased MMP-9 expression and activity has been observed 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 ECM and basement membrane.
Size
25 μg
Concentration
n/a
Applications
BA
Other Names
Gelatinase B, Type IV collagenase, 92kDa gelatinase, Type V collagenase, MMP9