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- W2382161528 abstract "Objective To construct prokaryotic expression vector of human ubiquitin-conjugating enzymes E2Cs(UBE2C/UbcH10) gene,and induce the expression of UbcH10 in E.coli,and to purify and identify the obtained recombinant protein.Methods UbcH10 gene was amplified by PCR,and then was subcloned into prokaryotic expression vector pET32a(+) to construct the recombinant vector pET32a(+)/UbcH10.After being identified by enzyme digestion and DNA sequencing,the pET32a(+)/UbcH10 was transformed into E.coli BL21,and the expression was induced with 1mmol/L IPTG for 4 hours.The expressed product was then analyzed by SDS-PAGE and Western blotting.The UbcH10 protein obtained was purified by Ni-Sepharose affinity column and SephadexG-50 molecular sieve chromatography.Results Prokaryotic expression vector pET32a(+)/UbcH10 was successfully constructed.A large amount of recombinant protein about 29kD was obtained in E.coli BL21 after IPTG induation,and it was soluble and accounted for about 40% of total bacterial protein.Western blotting showed that the molecular weight of recombinant protein was consistent with the theoretical value.The concentration of purified protein was about 8.82mg/ml,and the purity coefficient was up to 90%.Conclusions The successful expression and purification of recombinant protein UbcH10 will be valuable for the further study on the structure,function and its important role in tumorigenesis and tumor progression." @default.
- W2382161528 created "2016-06-24" @default.
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- W2382161528 date "2009-01-01" @default.
- W2382161528 modified "2023-09-23" @default.
- W2382161528 title "Expression and identification of human ubiquitin-conjugating enzyme UBE2C/UbcH10 in E.coli" @default.
- W2382161528 hasPublicationYear "2009" @default.
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