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- W959889750 abstract "Objective. To investigate the expression of telomemse genc hTRT mRNA in HeLa cells and to obtain hTRT pro-tein for luther study. Methods. The genc for encoding hTRT catalytic domain was cloned based on RT-PCR amplification from HeLa cells and sequenced. The cloned hTRTcDNA was in-frame inserted into His-tag fusion expression vector pEK318. The His-tag hTRT fusion proteins were purified by Ni-NTA chromatography and stained by western blotting. Results. An approximately 620bp fragment was generated and cloned into pBluescfipt SK + between Sall and BamHI sites. DNA sequencing showed the isolated fragment was consistent to those reported. SDS-PAGE present that a 17kDa protein was expressed stably in E.coli JM109 harboring pEKTRT344 containing 6 × His-tag and hTRT 150aa, and the expression level of the protein was about 26% of the total bacterial proteins, while the expression of pEKTRT containing 6 × His-tag and hTRT 243aa was only detectable as 27 kDa hand in western blotting. Both of fu-sion proteins were purified by Ni-NTA chromatography and showed single band( > 95% pufifity) in Coomassie Bril-liant staining. Western-blotting confmned that two proteins could be recognized by the Ni-NTA AP conjugate. Conclusions. The hTRT catalytic domain was highly conserved. The expressed hTRT protein contained recogniz-able His-tag, telomerase-specific and strong antigenic epitops, which may be convenient for ftrrther investigation." @default.
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- W959889750 date "2000-01-01" @default.
- W959889750 modified "2023-09-27" @default.
- W959889750 title "MOLECULAR CLONING OF hTRT CATALYTIC DOMAIN FROM HeLa CELLS AND ITS EXPRESSION IN E. Coli AND PURIFICATION" @default.
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