| 货号 | DY907 |
| 别名 | EC 3.4.24; EC 3.4.24.23; Matrilysin; matrin; matrix metallopeptidase 7 (matrilysin, uterine); matrix metalloproteinase 7 (matrilysin, uterine); Matrix metalloproteinase-7; MMP7; MMP-7; MPSL1; Pump-1 protease; PUMP1; PUMP-1; uterine matrilysin; Uterine metalloproteinase | 全称 | Matrix Metalloproteinase 7 |
| 反应种属 | Human |
| 目标/特异性 | Please see the product datasheet |
| 供应商 | R&D Systems |
| 检测类型 | Solid Phase Sandwich ELISA |
| Entrez Gene IDs | 4316 (Human); 17393 (Mouse); |
| 应用文献 | |
| R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions. Association of Matrix Metalloproteinases -7, -8 and -9 and TIMP -1 with Disease Severity in Acute Pancreatitis. A Cohort Study | |
| 背景 | The matrix metalloproteinases (MMPs) consist of 24 known human zinc proteases with essential roles in breaking down components of the extracellular matrix (ECM). Additional MMP substrates include cytokines, chemokines, growth factors and binding proteins, cell/cell adhesion molecules, and other proteinases. With a few exceptions, MMPs share common structural motifs including a pro-peptide domain, a catalytic domain, a hinge region, and a hemopexin-like domain. Synthesized as pro-enzymes, most MMPs are secreted before conversion to their active form. MMP activities are modulated on several levels including transcription, pro-enzyme activation, or by their endogenous inhibitors, tissue inhibitors of metalloproteinases (TIMPs). A subset of MMPs are associated with membranes and designated as membrane-type metalloproteinases (MT-MMP). |
| 运输条件 | Blue Ice |
| 存放说明 | 4℃ |