MMP-9 ELISA Assay Kit
The MMP-9 ELISA Assay Kit is For Research Use Only
Size: 1×96 wells
Sensitivity: 31 pg/ml
Dynamic Range: 62.5 – 2000 pg/ml
Incubation Time: 3.5 hours
Sample Type: Serum, Plasma, Cell Culture
Sample Size: 100 µl
Alternative Names: Matrix metalloproteinase 9, Gelatinase B
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade extracellular matrix proteins. They are secreted as zymogens (Pro-MMPs) that are activated by a variety of proteinases or by reaction with organic mercurials. They are inhibited by specific tissue inhibitors of metalloproteinases (TIMPs) and by 2-macroglobulin. The regulation of MMP activity is important in tissue remodeling, inflammation, tumor growth and metastasis.
Human MMP-9 (also known as gelatinase B) is secreted as a 92 kDa zymogen (2, 3). Cleavage of Pro-MMP-9 at or near residue 87 results in the active enzyme with a mass of approximately 82 kDa. MMP-9 has three fibronectin type II domains, a hemopexin-like domain and a proline-rich type V collagen-homologous domain. Pro-MMP-9 can be activated by MMP-3 or by certain bacterial proteinases (10). MMP-9 is inhibited by α2-macroglobulin or by TIMP-1, which binds to Pro-MMP-9 as well as to active MMP-9. In vitro treatment of Pro-MMP-9 with 4-aminophenylmercuric acid (APMA) produces not only the 82 kDa active enzyme but also a C-terminal truncated form of approximately 65 kDa with the activity comparable to that of the 82 kDa form.
Pro-MMP-9 is secreted by monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts, chondrocytes, skeletal muscle satellite cells, endothelial cells, and various tumor cells. Pro-MMP-9 expression is upregulated by TGF-β1, IL-1β, TGF-α, PDGF-AB, TNF-α, and IL-1α. Substrates for MMP-9 include denatured collagen type I (gelatin), native collagens type IV, V, VII, X and XI, fibrinogen, vitronectin, IL-1β, and entactin, a molecule that bridges laminin and type IV collagen.