Isolation of Human Interleukin 22 Gene and Its Expression in E.coli
Cai Xin
Abstract
Cai Xin
Abstract
A cDNA fragment encoding mature hIL-22 protein was amplified by RT-PCR from mRNA extracted from anti-CD3 and ConA activated peripheral blood white cells. The gene was sequenced and consistent with that reported. hIL-22 gene was cloned into the plasmid pBV220 and expressed in E.coli JM109 in the form of inclusion bodies. The recombinant protein amounts to 40% of total bacterial protein in bacterial cells. The results suggested that a confirmed hIL-22 clone was obtained and highly expressed in E.coli. It provides a reliable foundation to investigate the biological function of IL-22.
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A cDNA fragment encoding mature hIL-22 protein was amplified by RT-PCR from mRNA extracted from anti-CD3 and ConA activated peripheral blood white cells. The gene was sequenced and consistent with that reported. hIL-22 gene was cloned into the plasmid pBV220 and expressed in E.coli JM109 in the form of inclusion bodies. The recombinant protein amounts to 40% of total bacterial protein in bacterial cells. The results suggested that a confirmed hIL-22 clone was obtained and highly expressed in E.coli. It provides a reliable foundation to investigate the biological function of IL-22.
Key concepts: Molecular biology, Recombinant DNA, Plasmid, Gene, Biology, Complementary DNA, clone (Java method), Gene expression