

| Catalog No. | HP402014 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Species reactivity | Human | ||||||||
| Applications | ELISA, IHC, WB | ||||||||
| Host species | Rabbit | ||||||||
| Isotype | IgG | ||||||||
| Clonality | Polyclonal | ||||||||
| Immunogen | E. coli - derived recombinant Human RAD51AP1 (Arg70-Asn116). | ||||||||
| Target | PIR51, RAD51-interacting protein, RAD51-associated protein 1, RAD51AP1, HsRAD51AP1 | ||||||||
| Purification | Purified by antigen affinity column. | ||||||||
| Accession | Q96B01 | ||||||||
| 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 | RAD51-associated protein 1 (RAD51AP1) is a ~38 kDa protein. Structure-specific DNA-binding protein involved in DNA repair by promoting RAD51-mediated homologous recombination. Acts by stimulating D-Loop formation by RAD51: specifically enhances joint molecule formation through its structure-specific DNA interaction and its interaction with RAD51. Binds single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures: has a strong preference for branched-DNA structures that are obligatory intermediates during joint molecule formation. Cooperates with WDR48/UAF1 to stimulate RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during homologous recombination and DNA repair. WDR48/UAF1 and RAD51AP1 also have a coordinated role in DNA-binding to promote USP1-mediated deubiquitination of FANCD2. 1. Modesti, M. et al. (2007) Molecular cell 28, 468-81. PMID: 17996710 2. Wiese, C. et al. (2007) Molecular cell 28, 482-90. PMID: 17996711 3. Dray, E. et al. (2010) Nature structural & molecular biology 17, 1255-9. PMID: 20871616 4. Parplys, AC. et al. (2014) DNA repair 24, 87-97. PMID: 25288561 5. Parplys, AC. et al. (2015) Nucleic acids research 43, 9817-34. PMID: 26323318 6. Dunlop, MH. et al. (2012) The Journal of biological chemistry 287, 12343-7. PMID: 22375013 | ||||||||
| Note | For research use only. |
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