| 货号 | MAB903-SP |
| 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; MMP-2; MMP-II; MONA; neutrophil gelatinase; TBE-1matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IVcollagenase) | 全称 | Matrix Metalloproteinase 2 |
| 反应种属 | Human |
| 应用 | Western Blot(1 µg/mL) Intracellular Staining by Flow Cytometry(2.5 µg/106cells) |
| 目标/特异性 | Detects the pro and active forms of human MMP-2 in Western blots. In dot blots, no cross-reactivity with recombinant human MMP-1, -3, -7, -8, -9, -10, -12, or -13 is observed. |
| 使用方法 | Western Blot: 1 µg/mL Intracellular Staining by Flow Cytometry: 2.5 µg/106cells |
| 来源 | Reconstitute at 0.5 mg/mL in sterile PBS. |
| 产品组分 |
| 供应商 | R&D Systems |
| 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. Borrelia burgdorferi-induced monocyte chemoattractant protein-1 production in vivo and in vitro. | |
| 纯化方式 | Protein A or G purified from hybridoma culture supernatant |
| 免疫原 | Chinese hamster ovary cell line CHO-derived recombinant human MMP-2 |
| 生物活性 | Human |
| 标记 | Unconjugated |
| 溶解方法 | Reconstitute at 0.5 mg/mL in sterile PBS. |
| 背景 | 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‑2 (gelatinase A), a type IV collagenase, can degrade a broad range of substrates including type IV, V, VII and X collagens as well as elastin and fibronectin. 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‑2 has been shown to be associated with many connective tissue cells as well as neutrophils, macrophages and monocytes. Structurally, MMP‑2 may be divided into several distinct domains: a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin-like domain thought to play a role in substrate targeting; and a carboxyl terminal (hemopexin-like) domain containing 2 N-linked glycosylation sites. |
| 运输条件 | Blue Ice |
| 存放说明 | 4℃ |
| 参考文献 |
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