Soluble expression and purification of synthetic human bone morphogenetic protein-2 in Escherichia coli

A 345-bp gene that encodes human bone morphogenetic pro-tein-2 (hBMP-2) has been synthesized. The codon usage of the resulting gene was modified to include those triplets that are utilized in highly expressed Escherichia coli genes. The hBMP-2 gene was efficiently expressed in E. coli as a soluble and active protein. Since the recombinant hBMP-2 was readily solublized, no further solublization steps were required throughout purifi-cation. No additional tagging residues were introduced into the synthetic hBMP-2 gene product. The developed synthetic gene is a promising approach for scaling-up the soluble ex-pression of hBMP-2. [BMB reports 2008; 41(5): 404-407