To investigate a feasible way to reconstruct Bone Morphogenetic Protein-2(BMP2) with Bioengineering technology and express the protein in a E.coli system.,we reconstruct and filtrate the gene of BMP-2 in E.coli system.Analysis via a SDS-PAGE electrophoresis shows that the exogenous protein cingulum lies around the comparative molecular weight marker 12kD site.After a purification with ion-exchange chromatogram and molecular screen,the purified BMP-2 protein is renatured and the bioactivity is measured by the induction of alkaline phosphatase activity(ALP) in C2C12 cells.