Dihydroflavonol 4-reductase(DFR) is a key enzyme in the biosynthesis of anthocyanins in tartary buckwheat.The DFR coding gene was amplified from the seed-filling period cDNA of tartary buckwheat by RT-PCR and ligated to the expression vector pET47b.The E.coli BL21(DE3) carrying the DFR coding gene was obtained and induced by IPTG.The expression products were analyzed by SDS-PAGE,purified by affinity chromatograph and the high titer polyclonal antiserum raised against rabbit was obtained.The open reading frame of DFR coding gene was obtained by RT-PCR.As analyzed by PCR and DNA sequencing.The recombinant prokaryotic expression vector was constructed successfully.As analyzed by SDS-PAGE,the DFR had been high-efficiency expressed in E.coli in the form of soluble protein and inclusion bodies.Pure fusion protein was obtained by affinity chromatography.Western blotting analysis showed the raised antibody could specifically react with the antigen and native DFR existed in total protein of seed filling period of buckwheat.These results will be valuable for the further study on the biological function of DFR.