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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Soluble expression and purification of synthetic human bone morphogenetic protein-2 in Escherichia coli

  • Ihm, Hyo-Jin (Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine) ;
  • Yang, Seung-Ju (Department of Biomedical Laboratory Science, Konyang University) ;
  • Huh, Jae-Wan (Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine) ;
  • Choi, Soo-Young (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Cho, Sung-Woo (Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine)
  • Published : 2008.05.31
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Abstract

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.

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References

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