Abstract
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.
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Chu, W., Luo, S., Xu, L., Long, M., Diao, A. (2014). Expression of Recombinant Human Bone Morphogenetic Protein 2 in Insect Cells, Purification and Activity Analysis. In: Zhang, TC., Ouyang, P., Kaplan, S., Skarnes, B. (eds) Proceedings of the 2012 International Conference on Applied Biotechnology (ICAB 2012). Lecture Notes in Electrical Engineering, vol 251. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-37925-3_140
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DOI: https://doi.org/10.1007/978-3-642-37925-3_140
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