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Published on: October 29, 2013
[Expression and purification of GST-HPV16E7 fusion protein]
Jian Zhang1, Tao Wang, Ming-Rong Xi
1Department of Obstetrics and Gynecology, West China Second Hospital, Sichuan University, Chengdu 610041, China.
Objective:
To construct a recombinant prokaryotic expression vector efficiently expressing HPV16E7 and purify GST-HPV16E7 fusion protein.
Methods:
The HPV16E7 gene obtained from a local cervical cancer patient was cloned into vector pGEX-4T-1, to generate the recombinant named as pGEX-4T-1-HPV16E7. The recombinant plasmid was transformed into E. coli BL21. After inducing with IPTG the HPV16E7 fusion protein was analyzed by SDS-PAGE and Western blot. B-PER GST Fusion Protein Purification Kit was appkied to purify GST-HPV16E7 fusion protein.
Results:
The recombinant plasmid pGEX-4T-1-HPV16E7 was successfully constructed. Highly expressed and purified GST-HPV16E7 fusion protein was obtained. The specificity of fusion protein was verified by SDS-PAGE and Western blot.
Conclusion:
GST-HPV16E7 fusion protein was successfully expressed and purified.
