Recombinant Saccharomyces cerevisiae DNA repair protein RAD51(RAD51)

Code CSB-YP333076SVG
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Source Yeast
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Code CSB-EP333076SVG
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Source E.coli
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Code CSB-EP333076SVG-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP333076SVG
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Source Baculovirus
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Code CSB-MP333076SVG
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names RAD51
Uniprot No. P25454
Alternative Names RAD51; YER095W; DNA repair protein RAD51
Species Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Expression Region 1-400
Protein Length full length protein
Tag Info The following tags are available.
N-terminal His-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Background

(From Uniprot)
Required both for recombination and for the repair of DNA damage caused by X-rays. Its function may be modulated by interaction with other repair proteins. RAD52 interacts directly with RAD51, via its C-terminus. Forms a nucleoprotein filament with DNA as an early intermediate in recombination.
Gene References into Functions
  1. analysis of Rad51-dependent break-induced replication in which the invading double strand break end and its donor template share a 108-base-pair homology region and the donor carries different densities of single-base-pair mismatches PMID: 28405019
  2. Small Rad51 and Dmc1 complexes co-occupy both ends of a meiotic DNA double strand break. PMID: 26719980
  3. Using single-molecule imaging to visualize Rad51, study shows that Rad51 uses a length-based recognition mechanism while interrogating dsDNA, enabling robust kinetic selection of 8-nucleotide tracts of microhomology, which kinetically confines the search to sites with a high probability of being a homologous target. PMID: 25684365
  4. Shu complex utilizes homologous recombination machinery for error-free lesion bypass via physical interaction with a Rad51 paralogue PMID: 24339919
  5. Here we show that Rad51-mediated meiotic recombination is not subject to regulatory processes associated with high-fidelity chromosome segregation PMID: 24367271
  6. These results support the idea that down-regulation of Rad51 activity is important during meiosis to prevent Rad51 from competing with Dmc1 for repair of meiotic DSBs PMID: 24465215
  7. Rad51 protein overexpression induces resistance to DNA-damaging agents. PMID: 24741789
  8. Srs2's DNA-unwinding activity is greatly suppressed when Rad51 filaments form on duplex DNA. PMID: 23939144
  9. FBH1 restraining RAD51 DNA binding under unperturbed growth conditions to prevent unwanted or unscheduled DNA recombination. PMID: 24108124
  10. mechanism of Rad51 stabilization is inferred by our high-resolution crystal structure, which reveals Psy3-Csm2 to be a structural mimic of the Rad51-dimer, a fundamental unit of the Rad51-filament PMID: 23575680
  11. study provides biochemical evidence that Rad51 acts as an accessory factor with Mei5-Sae3 for Dmc1-mediated joint molecule formation during meios; Rad51 is a multifunctional protein that catalyzes recombination directly in mitosis and indirectly, via Dmc1, during meiosis PMID: 22955832
  12. Novel attributes of Hed1 affect dynamics and activity of the Rad51 presynaptic filament during meiotic recombination. PMID: 22115747
  13. Mutating Rad51 Ser 192 to Ala or Glu confers hypersensitivity to DNA damage and homologous-recombination defects. PMID: 21738226
  14. propose that the Shu complex shifts the balance of repair toward Rad51 filament stabilization by inhibiting the disassembly reaction of Srs2 PMID: 21372173
  15. determined Mei5-Sae3 interacts with the Rad51 recombinase through the N-terminal domain of Mei5 PMID: 21543267
  16. Rad51 inhibits translocation formation by non-conservative homologous recombination in Saccharomyces cerevisiae. PMID: 20686691
  17. RAD51-dependent BIR does not require special facilitating sequences that are required for a less efficient RAD51-independent process. PMID: 15657422
  18. Gly-103 in the N-terminal domain of Saccharomyces cerevisiae Rad51 protein is critical for DNA binding PMID: 15908697
  19. Yeast cells lacking the SGS1 DNA helicase and the MUS81 structure-specific endonuclease display a synthetic lethality that is suppressed by loss of the RAD51 recombinase. PMID: 16193328
  20. Dmc1p and Rad51p are loaded to the DNA repair site in an independent manner. PMID: 16341884
  21. The Rad51-lysine191arginine ATPase-defective mutant either forms an altered filament or is defective in turnover, resulting in a reduced pool of free protein available for DNA binding. PMID: 17030607
  22. The processing of double-strand breaks and binding of single-strand binding proteins RPA and Rad51 modulate the formation of ATR-kinase foci. PMID: 18003698
  23. Results indicate that Rad51 and Dmc1 filaments are essentially identical with respect to several structural parameters, including persistence length, helical pitch, filament diameter, DNA base pairs per helical turn and helical handedness. PMID: 18535008
  24. Rad51 presynaptic filaments are sufficient to locate a homologous sequence and form initial joints, even on the surface of a nucleosome. PMID: 18570881
  25. an additional role of Rad51 might be to protect eukaryotic genomes from instabilities by preventing chromosomal rearrangements PMID: 18755201
  26. Data show that during Rad51 polymerization, recombinase proteins moved all the nucleosomal arrays in front of the progressing filament; this had a powerful remodeling effect, as Rad51 destabilized the nucleosomes along considerable stretches of DNA. PMID: 18982066
  27. Findings suggest that loop 2 contributes to the primary DNA-binding site in Rad51, controlling filament formation and ATPase activity. PMID: 19033358
  28. Mph1, but not a helicase-defective variant, dissociates Rad51-made D-loops PMID: 19136626
  29. BIR defect observed for rad51 mutants is due to strand invasion failure, whereas the Pol delta complex mutants are proficient for strand invasion but unable to complete extensive tracts of recombination-initiated DNA synthesis. PMID: 19139272
  30. Rad51 spreads chromosome-wide bidirectionally from the DNA double-strand breaks but selectively only on the broken chromosome PMID: 19217407
  31. Data show that Rad51 readily dissociates from DNA in the presence of ADP or in the absence of nucleotide cofactor, but that free ATP in solution confers a fivefold increase in the stability of the nucleoprotein filaments. PMID: 19327367
  32. ssDNA annealing promoted by Rad52 is preceded by aggregation of multiple replication protein-A (RPA)-ssDNA complexes with Rad52, and Rad51 inhibits this aggregation. PMID: 19445949
  33. that a physical interaction between Rad51 and the C-terminal region of Srs2 triggers ATP hydrolysis within the Rad51 filament, causing Rad51 to dissociate from DNA. PMID: 19595720

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Subcellular Location Nucleus, Chromosome
Protein Families RecA family, RAD51 subfamily
Database Links

KEGG: sce:YER095W

STRING: 4932.YER095W


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