Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization.

@article{Bao2006HighlyEE,
  title={Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization.},
  author={Wen-Jing Bao and Yong-guang Gao and Yong-Gang Chang and Tie-ying Zhang and Xiao-jing Lin and Xian-zhong Yan and Hong-yu Hu},
  journal={Protein expression and purification},
  year={2006},
  volume={47 2},
  pages={599-606}
}
It is often essential to focus the study on the small-size domains of large proteins in eukaryotic cells in the post-genomic era, but the low expression level, insolubility, and instability of the domains have been continuing to hinder the massive purification of domain peptides for structural and biological investigation. In this work, a highly efficient expression and purification system based on a small-size fusion partner GB1 and histidine tag was utilized to solve these problems. Two… CONTINUE READING

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