The aim was to produce recombinant human bone morphogenetic protein 2 (BMP2) using baculovirus-insect cell protein expression system. The recombinant protein was purified by high affinity Ni-charged resin, then the bioactivity of recombinant protein was detected by alkaline phosphatase assay, and the result showed that the recombinant BMP2 stimulated alkaline phosphatase activity in MC3T3-E1 cells, which lay the foundation for further study and application of recombinant BMP2.
The aim was to produce recombinant human bone morphogenetic protein 2 (BMP2) using baculovirus-insect cell protein expression system. The recombinant protein was purified by high affinity Ni-charged resin, then the bioactivity of recombinant protein was detected by alkaline phosphatase assay, and the result showed that the recombinant BMP2 stimulated alkaline phosphatase activity in MC3T3-E1 cells, which lay the foundation for further study and application of recombinant BMP2.
