[Human interleukin-13 cDNA cloning and expression].
Zhiwei Sun, Jingyi Si, Shiwei Liu, Gwonhwa Song, Shuxuan Zheng
Abstract
Zhiwei Sun, Jingyi Si, Shiwei Liu, Gwonhwa Song, Shuxuan Zheng
Abstract
OBJECTIVE: To construct an efficient expression system for HIL-13 in prokaryotic cells. METHODS: After Amplified by RT-PCR, The cDNA fragment encoding HIL-13 was inserted into pGEX-2T plasmid and expressed under induced condition. RESULTS: HIL-13 cDNA was obtained. Recombinant plasmid pGEX-2T HIL-13 was constructed and sequenced, the inserted fragment of the recombinant plasmid was confirmed to be HIL-13 cDNA. HIL-13 was expressed as a fusion protein with glutathione-s-transferase (GST-HIL-13, MW = 39,000). CONCLUSIONS: (1) HIL-13 cDNA has been obtained from T lymphocytes. (2) The rate of expression of HIL-13 in prokaryotic cells is about 37%.
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OBJECTIVE: To construct an efficient expression system for HIL-13 in prokaryotic cells. METHODS: After Amplified by RT-PCR, The cDNA fragment encoding HIL-13 was inserted into pGEX-2T plasmid and expressed under induced condition. RESULTS: HIL-13 cDNA was obtained. Recombinant plasmid pGEX-2T HIL-13 was constructed and sequenced, the inserted fragment of the recombinant plasmid was confirmed to be HIL-13 cDNA. HIL-13 was expressed as a fusion protein with glutathione-s-transferase (GST-HIL-13, MW = 39,000). CONCLUSIONS: (1) HIL-13 cDNA has been obtained from T lymphocytes. (2) The rate of expression of HIL-13 in prokaryotic cells is about 37%.
Key concepts: Complementary DNA, Molecular biology, Recombinant DNA, Plasmid, Cloning (programming), Biology, Fusion protein, Molecular cloning