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Published on: September 1, 2018
[Cloning of PD-1 gene and its prokaryotic expression in Escherichia coli]
Si-yong Chen1, Kun-ping Guan, Min-zhuo Guo
1Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 100052, China.
Objective:
To clone human PD-1 gene, construct a prokaryotic expression plasmid and express in E. coli.
Methods:
The human PD-1 cDNA was cloned by RT-PCR from the total RNA, which was extracted from peripheral blood lymphocyte cell of the patient with chronic hepatitis B. Recombinant PD-1 protein was been expressed and purified after the prokaryotic expression plasmid had been constructed. It was identified by SDS-PAGE, DNA sequencing and amino acid sequencing.
Results:
The PD-1 gene was cloned and confirmed by DNA sequencing. The recombinant protein was expressed in E. coli. The purified protein was obtained, then been confirmed by amino acid sequencing.
Conclusion:
The human PD-1 gene was successfully cloned and expressed in E. coli, which lays the foundation for further study on the function and application of PD-1.
