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Expression of the Recombinant Human Interleukin-11 in Pichia pastoris.

Wang Ty, Wang Cm, Guoqing Wei, JW Qiu, Huang Ys

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Abstract

Full length cDNA of human IL-11 was synthesized by DNA synthesizer. An expression plasmid, pGENYk, containing the recombinant DNA fragment, was linearized and transformed into Pichia pastoris. This recombinant gene was highly expressed in this yeast, and the expression product was purified by a three-step chromatography method. Analysis of the purified recombination protein with SDS-PAGE, Western blot and biological activities showed that the activity of the protein was the same as the Neumega expressed in E.coli.

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What this paper is about

Full length cDNA of human IL-11 was synthesized by DNA synthesizer. An expression plasmid, pGENYk, containing the recombinant DNA fragment, was linearized and transformed into Pichia pastoris. This recombinant gene was highly expressed in this yeast, and the expression product was purified by a three-step chromatography method. Analysis of the purified recombination protein with SDS-PAGE, Western blot and biological activities showed that the activity of the protein was the same as the Neumega expressed in E.coli.

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Available abstract

Full length cDNA of human IL-11 was synthesized by DNA synthesizer. An expression plasmid, pGENYk, containing the recombinant DNA fragment, was linearized and transformed into Pichia pastoris. This recombinant gene was highly expressed in this yeast, and the expression product was purified by a three-step chromatography method. Analysis of the purified recombination protein with SDS-PAGE, Western blot and biological activities showed that the activity of the protein was the same as the Neumega expressed in E.coli.

Key concepts: Pichia pastoris, Recombinant DNA, Molecular biology, Complementary DNA, Pichia, Myc-tag, Plasmid, Biology

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