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Cloning and expression of endostatin in escherichia coli

WU Cheng-jun, Lijian Ye, Xiaozhong Peng, Zhigang Ma, Jimei Liu, Ningzhu Hu, Bo Yan, Xingqi Huang

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Abstract

The total RNA was extracted from the fetal liver and the endostatin gene was amplifieated by RT-PCR. After identified by DNA sequencing, it was cloned into the expression vector pGEX-KG and then transformed into the host cells E. coli DH5alpha and BL21. Subsequently the recombinant GST-fusion protein was expressed and purified.

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What this paper is about

The total RNA was extracted from the fetal liver and the endostatin gene was amplifieated by RT-PCR. After identified by DNA sequencing, it was cloned into the expression vector pGEX-KG and then transformed into the host cells E. coli DH5alpha and BL21. Subsequently the recombinant GST-fusion protein was expressed and purified.

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Available abstract

The total RNA was extracted from the fetal liver and the endostatin gene was amplifieated by RT-PCR. After identified by DNA sequencing, it was cloned into the expression vector pGEX-KG and then transformed into the host cells E. coli DH5alpha and BL21. Subsequently the recombinant GST-fusion protein was expressed and purified.

Key concepts: Cloning (programming), Escherichia coli, Endostatin, Recombinant DNA, Molecular biology, Biology, Gene, Fusion protein

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Cloning and expression of endostatin in escherichia coli — Research Paper | ScholarLens