2010•Laboratory Medicine and ClinicRequires access

Construction and expression of HBV core antigen in E. coli

Ye Li

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Abstract

Objective To obtain the gene fragment encoding HBcAg,construct recombinant plasmid and express the recombinant HBcAg protein in E.coli using genetic engineering methods.Methods The HBcAg gene fragment was amplified by PCR and the cloning and expression plasmids including HBcAg gene were constructed.Then the recombinant plasmid was transformed into E.coli BL21(DE3)host cell.The HBcAg fusion protein was expressed under the induction of IPTG and identified by Western blot.Results Recombinant HBcAg was expressed in E.coli.The special band of recombinant protein was showed at expectant position by Western blot.Conclusion A prokaryotic expression system for HBcAg gene is successfully constructed and the recombinant HBcAg protein is obtained.It lays a foundation of further study on the function of the recombinant protein.

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What this paper is about

Objective To obtain the gene fragment encoding HBcAg,construct recombinant plasmid and express the recombinant HBcAg protein in E.coli using genetic engineering methods.Methods The HBcAg gene fragment was amplified by PCR and the cloning and expression plasmids including HBcAg gene were constructed.Then the recombinant plasmid was transformed into E.coli BL21(DE3)host cell.The HBcAg fusion protein was expressed under the induction of IPTG and identified by Western blot.Results Recombinant HBcAg was expressed in E.coli.The special band of recombinant protein was showed at expectant position by Western blot.Conclusion A prokaryotic expression system for HBcAg gene is successfully constructed and the recombinant HBcAg protein is obtained.It lays a foundation of further study on the function of the recombinant protein.

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Available abstract

Objective To obtain the gene fragment encoding HBcAg,construct recombinant plasmid and express the recombinant HBcAg protein in E.coli using genetic engineering methods.Methods The HBcAg gene fragment was amplified by PCR and the cloning and expression plasmids including HBcAg gene were constructed.Then the recombinant plasmid was transformed into E.coli BL21(DE3)host cell.The HBcAg fusion protein was expressed under the induction of IPTG and identified by Western blot.Results Recombinant HBcAg was expressed in E.coli.The special band of recombinant protein was showed at expectant position by Western blot.Conclusion A prokaryotic expression system for HBcAg gene is successfully constructed and the recombinant HBcAg protein is obtained.It lays a foundation of further study on the function of the recombinant protein.

Key concepts: HBcAg, Recombinant DNA, Molecular biology, Plasmid, Western blot, Gene, Biology, Virology

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Construction and expression of HBV core antigen in E. coli — Research Paper | ScholarLens