EXPRESSION AND PURIFICATION OF RECOMBINANT HUMAN BONE MORPHOGENETIC PROTEIN-7 IN Escherichia coli

Bone morphogenetic protein-7 (BMP-7) is a multifunctional cytokine of the transforming growth factor superfamily, which induces bone formation and plays an important role during bone tissue repair and embryonic development. In this study, human BMP-7 (hBMP-7) cDNA was cloned and expressed in Escherichia coli, and its yield was approximately 30% of the total bacterial protein. After the bacteria were lysed by ultrasonication and repeated washing, inclusion bodies were extracted and dissolved using a high-strength denaturant. The monomer of rhBMP-7 was purified by ion-exchange chromatography, and the purity coefficient was approximately 96%. The protein was renatured with refolding buffers at different pH values. The renatured rhBMP-7 dimer protein in this study increased the alkaline phosphatase activity of NIH3T3 cells. This study may be helpful for the in vitro production and biomedical application of rhBMP-7 protein expressed in an E. coli expression system.