Recombinant Saccharomyces Cerevisiae Dna Repair And Recombination Protein Rad52 (RAD52) Protein (His-SUMO)

Name: Recombinant Saccharomyces Cerevisiae Dna Repair And Recombination Protein Rad52 (RAD52) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04435P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Saccharomyces Cerevisiae Dna Repair And Recombination Protein Rad52 (RAD52) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P06778
Target Symbol	RAD52
Synonyms	RAD52; YML032C; DNA repair and recombination protein RAD52
Species	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	IFGYNGWSTEVKSVVIDFLDERQGKFSIGCTAIVRVTLTSGTYREDIGYGTVENERRKPAAFERAKKSAVTDALKRSLRGFGNALGNCLYDKDFLAKIDKVKFDPPDFDENNLFRPTDEISESSRTNTLHENQEQQQYPNKRRQLTKVTNTNPDSTKNLVKIENTVSRGTPMMAAPAEANSKNSSNKDTDLKSLDASKQDQDDLLDDSLMFSDDFQDDDLINM
Expression Range	60-282aa
Protein Length	Partial
Mol. Weight	41.1kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Involved in DNA double-strand break (DSB) repair and recombination. Promotes the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.
Subcellular Location	Nucleus.
Protein Families	RAD52 family
Database References	KEGG: sce:YML032C STRING: 4932.YML032C

Gene Functions References

Global chromosome mobility is regulated by the Rad51 recombinase and its mediator, Rad52. PMID: 30181361
Rad52 inverse strand exchange plays an important role in RNA-templated double strand break repair in vivo. PMID: 28602639
The C-terminal region of yRad52, but not of hRAD52, is involved in ssDNA annealing. This suggests that the second DNA binding site is required for the efficient ssDNA annealing by yRad52. We propose an updated model of Rad52-mediated ssDNA annealing. PMID: 27362509
Rad52 is needed to repair telomere attrition-induced replication stress PMID: 27428329
investigated the contribution of the nuclear double-strand break repair (DSBR) proteins Rad51p, Rad52p and Rad59p in mtDNA repair PMID: 26540255
the homeologous pairing between the terminal TG1-3 repeats at VII-L and internal repeats on other chromosome ends was largely independent of Rad51, but instead it was facilitated by Rad59 that stimulates Rad52 strand annealing activity PMID: 25375789
It was found that, despite the absence of self-homology on the T-DNA, the homologous repair proteins Rad52 and Rad51 are involved in T-DNA circle formation. PMID: 24460832
The study suggested that phenylalanine-349 and tyrosine-409 are key residues in the C-terminal half of Rad52 and probably play an important role in the recombination mediator activity. PMID: 24163251
This conclusion is strengthened by the finding that Rad52 is often associated with complete Rad51 filaments in vitro PMID: 24130504
The Shu complex plays a central role in Rad52 rDNA localization as long as Rad52 can be sumoylated. PMID: 23790361
New scenario for homologous recombination where Rad52 and Rad51 are recruited to the fork to promote DNA damage tolerance by distinct and cell cycle-regulated replicative and repair functions. PMID: 23563117
Our results describe 8 new genes involved in SCR, including functions such as histone acetylation/deacetylation, SUMO-Ubiquitin metabolism, and stress response, as well as an allele of RAD52 PMID: 23357952
Ty1 sequence-specific gross chromosomal rearrangements are RAD52-dependent. PMID: 21637792
Rad52 within the complex associates with double-stranded DNA to assist Rad51-mediated homologous pairing. PMID: 21454474
results highlight the importance of Rad52 SUMOylation as part of a 'quality control' mechanism regulating the efficiency of recombination and DNA repair. PMID: 20371517
result suggests that spontaneous DNA lesions that require recombinational repair occur at the same frequency in wild-type and rad52-Y66A cells, but that the recombination process is slow in rad52-Y66A cells. PMID: 19892607
Results from chromatin immunoprecipitation experiments find that rad52-R70A associates with DNA double-strand breaks and promotes recruitment of Rad51 as efficiently as wild-type Rad52. PMID: 19812039
Increases in transposition activity in sir4 mutant strains at high temperature is dependent on the RAD52 gene. PMID: 15454529
These results imply that telomeres can use looped-out telomeric rings to promote telomere-telomere recombination through Rad52-, Rad50-, and polymerase delta in telomerase-deficient Saccharomyces cerevisiae. PMID: 15701795
examined the ssDNA annealing activity of Rad52 and Rad59 proteins and found significant differences in their biochemical properties PMID: 16565518
Multiple Rad52 protein species are due to promiscuous choice of start codons as well as post-translational modification. PMID: 16707661
The rearrangement frequency was found to increase with array size, and partial complementation of the rad27Delta mutation by hFEN1 demonstrated that the production of novel CEB1 alleles is Rad52 and Rad51 dependent. PMID: 16914748
S. cerevisiae Rad52 protein and its eukaryotic counterparts function by binding to single-stranded DNA formed as intermediates of recombination rather than by binding to the unprocessed DNA double-strand break. PMID: 17040915
Error-free RAD52 pathwaydetermines spontaneous mutagenesis in Saccharomyces cerevisiae PMID: 17396018
The contributions of the RAD51, RAD52, and RAD54 genes and of the RAD50 and XRS2 genes to the postreplicational repair of ultraviolet rays-damaged DNA, is examined. PMID: 17785441
These results provide a mechanistic framework for rationalizing the multi-faceted role of Rad52 in recombination and DNA repair. PMID: 18310075
Results show that Rad52 functions in temporally and biochemically distinct reactions and suggest a general annealing mechanism for reuniting DSB ends during recombination. PMID: 18313389
regulation of Rad52-mediated annealing suggests a control function for Rad51 in deciding the recombination path taken for a processed DNA break; the ssDNA can be directed to either Rad51-mediated DNA strand invasion or to Rad52-mediated DNA annealing PMID: 18337252
These findings indicate that nuclear localization of Rad52 is pre-requisite for its sumoylation. PMID: 18482582
support a role for Rad52-promoted annealing in the formation of Holliday junctions in double-stranded break repair PMID: 19204284
Rad52 interaction with replication protein-A (RPA) requires multiple molecules of RPA to be associated with ssDNA, suggesting that multiple contacts between the Rad52 ring and RPA-ssDNA filament are needed for stable binding. PMID: 19445949
condensin and Rad52 have opposing roles in the control of rDNA stability under nutrient starvation conditions PMID: 19520859
The structure and functions of Rad52 are briefly reviewed. The DNA annealing & mediator functions of Rad52 play a central role in homologous recombination-based DNA double-strand-break repair. Review. PMID: 19706272

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.