Recombinant Saccharomyces cerevisiae DNA repair and recombination protein RAD52(RAD52),partial CSB-EP361943SVG
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
RAD52; YML032C; DNA repair and recombination protein RAD52
Species: (Organism)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Gene Names:
RAD52
Tag info:
N-terminal 6xHis-SUMO-tagged
Target Protein AA Sequence:
IFGYNGWSTEVKSVVIDFLDERQGKFSIGCTAIVRVTLTSGTYREDIGYGTVENERRKPAAFERAKKSAVTDALKRSLRGFGNALGNCLYDKDFLAKIDKVKFDPPDFDENNLFRPTDEISESSRTNTLHENQEQQQYPNKRRQLTKVTNTNPDSTKNLVKIENTVSRGTPMMAAPAEANSKNSSNKDTDLKSLDASKQDQDDLLDDSLMFSDDFQDDDLINM
Expression Region:
60-282aa
Subcellular Location:
Nucleus
Tissue Specificity:
Protein Length:
Partial
Pathway:
Mol. Weight:
41.1 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Others
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.
Involvement in disease:
Relevance:
Involved in DNA double-strand break (DSB) repair and recombination. Promotes the annealing of complentary single-stranded DNA and by stimulation of the RAD51 recombinase.
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.
Protein Families:
RAD52 family
Reference:
A multidimensional chromatography technology for in-depth phosphoproteome analysis.Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.Mol. Cell. Proteomics 7:1389-1396(2008)
