

| Catalog No. | HP735014 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Species reactivity | Human | ||||||||
| Applications | ELISA, IHC, WB | ||||||||
| Host species | Rabbit | ||||||||
| Clonality | Polyclonal | ||||||||
| Isotype | IgG | ||||||||
| Immunogen | E. coli - derived recombinant Human NDOR1 (Met1-Leu154). | ||||||||
| Target | NR1, NDOR1, NADPH-dependent diflavin oxidoreductase 1, NADPH-dependent FMN and FAD-containing oxidoreductase, Novel reductase 1 | ||||||||
| Purification | Purified by antigen affinity column. | ||||||||
| Accession | Q9UHB4 | ||||||||
| Form | Liquid | ||||||||
| Storage buffer | 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. |
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| Product Usage Information |
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| Stability and Storage | 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. | ||||||||
| Background | 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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