

| Catalog No. | HT142014 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Species reactivity | Human | ||||||||
| Applications | ELISA, IHC, WB | ||||||||
| Host species | Rabbit | ||||||||
| Isotype | IgG | ||||||||
| Clonality | Polyclonal | ||||||||
| Immunogen | E. coli - derived recombinant Human NR5A2 (Ser300-Ala541). | ||||||||
| Target | Liver receptor homolog 1, hB1F, NR5A2, Alpha-1-fetoprotein transcription factor, CYP7A promoter-binding factor, B1-binding factor, FTF, Nuclear receptor subfamily 5 group A member 2, LRH-1, B1F, CPF, Hepatocytic transcription factor | ||||||||
| Purification | Purified by antigen affinity column. | ||||||||
| Accession | O00482 | ||||||||
| 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 | Nuclear receptor subfamily 5 group A member 2 (NR5A2) is a ~61 kDa protein. Orphan nuclear receptor that binds DNA as a monomer to the 5'-TCAAGGCCA-3' sequence and controls expression of target genes: regulates key biological processes, such as early embryonic development, cholesterol and bile acid synthesis pathways, as well as liver and pancreas morphogenesis. Ligand-binding causes conformational change which causes recruitment of coactivators, promoting target gene activation. The specific ligand is unknown, but specific phospholipids, such as phosphatidylethanolamine, phosphatidylserine, dilauroyl phosphatidylcholine and diundecanoyl phosphatidylcholine can act as ligand in vitro. Acts as a pioneer transcription factor, which unwraps target DNA from histones and elicits local opening of closed chromatin. Plays a central role during preimplantation stages of embryonic development. 1. Solomon, IH. et al. (2005) Journal of molecular biology 354, 1091-102. PMID: 16289203 2. Burendahl, S. et al. (2008) Biochemistry 47, 5205-15. PMID: 18410128 3. Lee, JM. et al. (2011) Nature 474, 506-10. PMID: 21614002 4. Seacrist, CD. et al. (2020) Structure (London, England : 1993) 28, 830-846.e9. PMID: 32433991 5. Kobayashi, W. et al. (2024) Nature structural & molecular biology 31, 757-766. PMID: 38409506 6. Li, M. et al. (1998) The Journal of biological chemistry 273, 29022-31. PMID: 9786908 7. Krylova, IN. et al. (2005) Cell 120, 343-55. PMID: 15707893 8. Ortlund, EA. et al. (2005) Nature structural & molecular biology 12, 357-63. PMID: 15723037 9. Wang, W. et al. (2005) Proceedings of the National Academy of Sciences of the United States of America 102, 7505-10. PMID: 15897460 10. Musille, PM. et al. (2012) Nature structural & molecular biology 19, 532-S2. PMID: 22504882 | ||||||||
| Note | For research use only. |
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