货号 | SMMP200 |
简介 | For human, mouse, rat, porcine, and canine samples |
描述 | The Quantikine Total MMP-2 Immunoassay is a 4.5 hour solid-phase ELISA designed to measure MMP-2 in cell culture supernates, serum, and plasma. It contains NS0-expressed recombinant mouse/rat pro-MMP-2 and has been shown to accurately quantitate the recombinant factor. Results obtained using natural MMP-2 showed linear curves that were parallel to the standard curves obtained using the Quantikine kit standards. These results indicate that this kit can be used to determine relative mass values for naturally occurring MMP-2. |
别名 | 72 kDa gelatinase; CLG4; CLG4A72 kDa type IV collagenase; collagenase type IV-A; EC 3.4.24; EC 3.4.24.24; Gelatinase A; matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IVcollagenase); matrix metalloproteinase 2 (gelatinase A, 72kD gelatinase, 72kD type IVcollagenase); Matrix metalloproteinase-2; matrix metalloproteinase-II; MMP2; MMP-2; MMP-II; MONA; neutrophil gelatinase; TBE-1matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IVcollagenase); | 全称 | Matrix Metalloproteinase 2 |
目标/特异性 | Recombinant MMP-2 and natural human, mouse, rat, porcine, and canine active, pro-, and TIMP complexed MMP-2. |
供应商 | R&D Systems |
检测类型 | Solid Phase Sandwich ELISA |
Entrez Gene IDs | 4313 (Human); 17390 (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. Aurora Kinase A is a Biomarker for Bladder Cancer Detection and Contributes to its Aggressive Behavior | |
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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