2009•PubMedRequires access
[Expression and purification of GST-HPV16E7 fusion protein].
Jian Zhang, Tao Wang, Mingrong Xi, Min Han, Yue Chen
Open publisher page 1 citations
Abstract
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.