Purity >95% SDS-PAGE. Function May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly- -Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide. Background Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 maybe be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin-binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline-rich linker region, and a carboxyl terminal hemopexin-like domain. In addition to the human enzyme, the recombinant mouse MMP-9 is also available.
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Recombinant Human MMP9 Protein
CAS number：unknown molecular formula：
overview
compound introduction
Specs
| Chinese alias | 重组人MMP9蛋白 | 重组人MMP9蛋白 | ||
| English alias | 92 kDa gelatinase | 92 kDa type IV collagenase | CLG4B | EC 3.4.24 | EC 3.4.24.35 | Gelatinase B | GELB | macrophage gelatinase | MANDP2 | matrix metallopeptidase 9 | matrix metalloproteinase 9 | matrix metalloproteinase-9 | MMP9 | MMP-9 | type V collagen | ||
| CAS number | unknown | molecular formula | |
| molecular weight | - | Exact mass | 无动物源 |
| PSA | - | logp | - |
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