| 货号 | MMP300 |
| 描述 | The Quantikine Mouse MMP-3 Immunoassay is a 4.5 hour solid-phase ELISA designed to measure total mouse MMP-3 (pro-, active, and TIMP-complexed MMP-3) in cell culture supernates and mouse serum. It contains NS0-expressed recombinant mouse MMP-3 and antibodies raised against the recombinant factor. Both antibodies also recognize recombinant mouse active MMP-3. Natural mouse MMP-3 showed dose-response curves that were parallel to the standard curves obtained using the recombinant Quantikine kit standards. These results indicate that this kit can be used to determine relative levels of natural mouse MMP-3. |
| 别名 | CHDS6; EC 3.4.24; EC 3.4.24.17; matrix metallopeptidase 3 (stromelysin 1, progelatinase); matrix metalloproteinase 3 (stromelysin 1, progelatinase); Matrix metalloproteinase-3; MGC126102; MGC126103; MMP-3; proteoglycanase; SL-1; STMY; STMY1MGC126104; STR1; Stromelysin 1; stromelysin-1; transin-1; | 全称 | Matrix Metalloproteinase 3 |
| 反应种属 | Mouse |
| 目标/特异性 | Natural and recombinant mouse MMP-3 (pro-, active, and TIMP-complexed) |
| 供应商 | R&D Systems |
| 检测类型 | Solid Phase Sandwich ELISA |
| Entrez Gene IDs | 4314 (Human); 17392 (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. Aryl hydrocarbon receptor deficiency in T cells suppresses the development of collagen-induced arthritis. | |
| 生物活性 | < 0.5% cross-reactivity observed with available related molecules.< 50% cross-species reactivity observed with species tested. |
| 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℃ |
| 参考文献 |
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