RAD52, Recombinant, Saccharomyces Cerevisiae, aa60-282, His-SUMO-Tag (DNA Repair and Recombination Protein RAD52)

Cat# 374986-100ug

Size : 100ug

Brand : US Biological

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374986 RAD52, Recombinant, Saccharomyces Cerevisiae, aa60-282, His-SUMO-Tag (DNA Repair and Recombination Protein RAD52)

Clone Type
Polyclonal
Swiss Prot
P06778
Grade
Purified
Shipping Temp
Blue Ice
Storage Temp
-20°C

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.||Source:|Recombinant protein corresponding to aa60-282 from saccharomyces cerevisiae RAD52, fused to His-SUMO-Tag at N-terminal, expressed in E. coli.||Molecular Weight: |~41.1kD||Amino Acid Sequence:|IFGYNGWSTEVKSVVIDFLDERQGKFSIGCTAIVRVTLTSGTYREDIGYGTVENERRKPAAFERAKKSAVTDALKRSLRGFGNALGNCLYDKDFLAKIDKVKFDPPDFDENNLFRPTDEISESSRTNTLHENQEQQQYPNKRRQLTKVTNTNPDSTKNLVKIENTVSRGTPMMAAPAEANSKNSSNKDTDLKSLDASKQDQDDLLDDSLMFSDDFQDDDLINM||Storage and Stability:|Lyophilized and reconstituted products are stable for 6 months after receipt at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Applications
Source: Recombinant, E. coli|Purity: ≥90% (SDS-PAGE)|Form: Supplied as a lyophilized powder from 20mM Tris-HCl, 0.5M sodium chloride, pH 8.0, 6% trehalose. Reconstitute with sterile ddH2O to a concentration of 0.1-1mg/ml.||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Form
Supplied as a lyophilized powder from 20mM Tris-HCl, 0.5M sodium chloride, pH 8.0, 6% trehalose. Reconstitute with sterile ddH2O to a concentration of 0.1-1mg/ml.
Purity
≥90% (SDS-PAGE)
References
1. 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).