The fusion construction of HIV-1 Tat gene in pEGx-KG and efficient expression in Escherichia coli

Objective: To study the efficient expression of GST-Tat protein in Escherichia coli BZ21(DE3).Methods: HIV-1 Tat gene was amplified by PCR from cDNA library of HIV and was inserted into vector of pEGx-KG.The recombinant plasmid was transferred and expressed in E.coli BL21(DE3).The expressed products were identified by SDS-page and Western-blot.Results: HIV-1 Tat gene was amplified successfully by PCR.The recombinant plasmid was expressed efficiently in E.coli(BL21).SDS-page and Western-blot analyses showed the expressed Tat fusion protein with relative molecular weight was 38.9 kDa.Conclusion: HIV-1 Tat gene can be cloned and GST-Tat fusion protein can be expressed efficiently in E.coli,which may contribute to further research of anti-AIDS.