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KMID : 0624620080410050404
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BMB Reports
2008 Volume.41 No. 5 p.404 ~ p.407
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Soluble expression and purification of synthetic human bone morphogenetic protein-2 in Escherichia coli
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Ihm Hyo-Jin
Yang Seung-Ju
Huh Jae-Wan
Choi Soo-Young
Cho Sung-Woo
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Abstract
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A 345-bp gene that encodes human bone morphogenetic protein-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 purification. 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 expression of hBMP-2. [BMB reports 2008; 41(5): 404-407]
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KEYWORD
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Bone morphogenetic protein-2, Protein purification, Synthetic gene, Over-expression
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