Abstract: To obtain the purified protein kinase BvM14-STPK, E. coli transformed with BvM14-STPK was induced under the condition of low temperature 16℃ and 0.5 mmol/L IPTG in this study. And the supernatant of the bacterium solution was purified by Ni2+ affinity chromatography. Furthermore, SDS-PAGE was applied to detect the purified protein. The result showed that BvM14-STPK protein existed in the form of inclusion bodies after inducing with 0.5 mmol/L IPTG at 37℃ which could not be further purified and analyzed. With better induction conditions, we made sure that a large amount of soluable BvM14-STPK in the supernatant can be obtained after being induced by 0.5 mmol/L IPTG at 16℃ overnight. After the detection with SDS-PAGE to the purification of supernatant, BvM14-STPK protein was detected. During the purification of the target protein, it was found that the imidazole at 150 mmol/L worked the best. The target protein BvM14-STPK was obtained successfully in this study.