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- W2389862376 abstract "Objective To prepare full-length RAP and N-terminal fusion protein through the PCR and molecular cloning technology,and examine the expression of RAP1083 and RAP258 fusion protein in E.coli BL21.Methods Renal cortex total RNA was extracted from SD rats with Trizol,and the full-length RAP cDNA obtained by RT-PCR method.The connection of cDNA and pGEM-T cloning vector was carried out to clone and transform.The positive clones were picked and sequenced,then the primers were designed according to the cDNA sequences in GenBank for the RAP.By running PCR,the target DNA obtained which was aiming directly at N-terminal and the full length of RAP.The purified DNA and pGEX-4T-1 containing GST were reorganized in vitro and subcloned into competent BL21 cells.The positive clones were chose and expanded the cultured.The fusion proteins were prepared by IPTG and purified.Results The sequencing results showed that the original expression vector pGEX-4T-1-RAP1083/258 were successfully constructed in the inducted E.coli BL21.The recombinant fusion proteins of the RAP total length of 70kD and N-terminal 36kD were expressed and purified.Conclusion The prokaryotic expression vector pGEX-4T-1-RAP1083/258 is constructed successfully,and the purified fusion protein of GST-RAP1083/258 is expressed stable in E.coli BL21,which will provide the basis for further study on the molecular pathogenesis of Heymann nephritis." @default.
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- W2389862376 date "2009-01-01" @default.
- W2389862376 modified "2023-09-23" @default.
- W2389862376 title "The fusion expression of full-length and N-terminal of receptor associated protein in Heymann nephritis and its significance" @default.
- W2389862376 hasPublicationYear "2009" @default.
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