Objective To screen the new gene p7TP2 transregulated by HCV p7 protein through gene chip technique and investigate its biological functions. Methods The p7TP2 cDNA was ampli? ed by PCR and prokaryotic expression vector pET-32a (+)-p7TP2 was constructed by gene recombination techniques, which were transformed into E. coli Rosetta-gami B, for IPTG induced expression. The p7TP2 fusion protein was expressed in the form of inclusion body. A band with 35 kD appeared on SDS-PAGE gel. The protein expressed by carboxyl terminal coding sequence had a high purity after denaturation, refolding and purification. New Zealand rabbits were immunized with p7TP2 fusion protein to prepare polyclonal antibody against p7TP2. The p7TP2 antiserun was obtained and characterized by ELISA, Western blot, immunohistochemistry. Results Results showed that the polyclonal antibody had high titer, affinity and speci? city. Conclusions The study provide a favorable tool for further functional study of HCV p7TP2 and the pathogenesis of hepatitis C.
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