The expression plasmid pMS32C/BMP1 was constructed successfully by using recombinant DNA techniques. The validity of the reconstructed plasmid was confirmed by restriction map of PMS32C/BMP1 plasmid. Then the 66KD BMP1 fusion protein was highly expressed in E. coli, which accounting for 20% of total bacterial proteins. The expressed protein was purified by means of SDS-PAGE. The antiserum of BMP1 fusion protein was prepared by immunization of mice. The antisera immunoprecipitated with fusion protein and specifically bound to BMPs purified from human bone with high titer in immuno-dot assay. It is indicated that the BMP1 fusion protein contains human BMP moiety.