Objective     To amplify EBV-LMP1 carboxy region and express it in recombinant prokaryotic plasmid pET-32a-LMP1c.      Methods     EBV-LMP1 exon c gene was amplified from the B95-8 cell genomic DNA by nest PCR and cloned into plasmid pET-32a. The recombinant plasmid was then transformed into E. coli. BL21. The EBV-LMP1 C was expressed as a recombinant fusion protein and detected by Western blotting．     Results     The size of amplified LMP1exon c DNA was 801 bp

which was the same as the published EBV-LMP1 carboxy region sequence. The recombinant prokaryotic expression plasmid pET-32a-LMP1c was constructed and 48×10

3

fusion protein was expressed in E. coli. BL21. The expresse

d protein was detected with the anti-LMP1 monoclonal antibody by Western blotting．     Conclusion     Recombinant prokaryotic expression plasmid was constructed successfully. The expressed recombinant fusion protein provided the basic material to produce our own anti-LMP1 monoclonal antibody and study the oncogenic role of LMP1.