

| 货号 | ARO-A11980 |
|---|---|
| 品牌 | ProteoGenix |
| 描述 |
Anti-Human NDOR1 Polyclonal Antibody (ARO-A11980) is a rabbit polyclonal antibody detecting NR1, NDOR1, NADPH-dependent diflavin oxidoreductase 1, NADPH-dependent FMN and FAD-containing oxidoreductase, Novel reductase 1 in ELISA, IHC, WB. Suitable for Human.
Highlights
|
| 种属反应性 | Human |
| 应用 | ELISA, IHC, WB |
| 宿主 | Rabbit |
| 克隆类型 | Polyclonal |
| 同种型 | IgG |
| 免疫原 | E. coli - derived recombinant Human NDOR1 (Met1-Leu154). |
| 靶标 | NR1, NDOR1, NADPH-dependent diflavin oxidoreductase 1, NADPH-dependent FMN and FAD-containing oxidoreductase, Novel reductase 1 |
| 纯化方式 | Purified by antigen affinity column. |
| Accession号 | Q9UHB4 |
| 状态 | Liquid |
| 保存溶液 | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| 稳定性和存储 | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| 背景 | NADPH-dependent diflavin oxidoreductase 1 (NDOR1) is a ~66 kDa protein. NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of CIAPIN1, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. It can also reduce the [2Fe-2S] cluster of CISD1 and activate this protein implicated in Fe/S cluster repair. In vitro can fully activate methionine synthase/MTR in the presence of soluble cytochrome b5/CYB5A. 1. Paine, MJ. et al. (2000) The Journal of biological chemistry 275, 1471-8. PMID: 10625700 2. Finn, RD. et al. (2005) Pharmacogenetics and genomics 15, 381-6. PMID: 15900210 3. Netz, DJ. et al. (2010) Nature chemical biology 6, 758-65. PMID: 20802492 4. Banci, L. et al. (2013) Proceedings of the National Academy of Sciences of the United States of America 110, 7136-41. PMID: 23596212 5. Camponeschi, F. et al. (2017) Journal of the American Chemical Society 139, 9479-9482. PMID: 28648056 |
| Note | For research use only. |

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