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- W2369367617 abstract "Objective To construct His-tagged FemA fusion protein expression vectors,and express it in E.coli and establish foundation for further studies.Methods PCR primers were designed using Primer Premier 5.0 software according to the sequence of femA gene in GenBank.Two restriction endonuclease recognition sites BamHI and SalI were added to the 5′ end of the primer.Genomic DNA from S.aureus was used as the templete for PCR amplification of femA gene.The obtained femA gene and plasmid pQE30 were double-enzyme digested respectively,ligated and transferred into DH5α.The positive clones were selected and the recombinant plasmid pQE30-femA was identified by PCR,restriction endonuclease analysis and DNA sequencing.Then the identified pQE30-femA was transformed into E.coli JM109 and the target protein expression was induced by IPTG.The expressed product was identified by SDS-PAGE and Western blot.Results Verified by PCR,double-enzyme digested assessment and sequencing,recombinant plamid pQE30-femA was successfully constructed.SDS-PAGE and Western blot analysis revealed that the recombinant plasmid pQE30-femA expressed a 53 kD target protein in E.coli JM109.Bandscan software analysis showed that the expressed target protein at 4 h accounted for about 27.5% of the total bacterial protein.Conclusion The His-tagged femA fusion protein expression vectors(pQE30-femA) was successfully constructed and high-effectively expressed in E.coli." @default.
- W2369367617 created "2016-06-24" @default.
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- W2369367617 date "2012-01-01" @default.
- W2369367617 modified "2023-09-23" @default.
- W2369367617 title "Construction of His-FemA fusion protein expression vectors and the expressions in prokaryotic cells" @default.
- W2369367617 hasPublicationYear "2012" @default.
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