An improved strategy for high-level production of TEV protease in Escherichia coli and its purification and characterization.

@article{Fang2007AnIS,
  title={An improved strategy for high-level production of TEV protease in Escherichia coli and its purification and characterization.},
  author={Lei Fang and Kun-Zhi Jia and Y Tang and D. Ma and Mei Yu and Zi-Chun Hua},
  journal={Protein expression and purification},
  year={2007},
  volume={51 1},
  pages={102-9}
}
Because of its stringent sequence specificity, tobacco etch virus (TEV) protease emerges as a useful reagent with wide application in the cleavage of recombinant fusion proteins. However, the solubility of TEV protease expressed in Escherichia coli is extremely low. In the present study, we introduced a more efficient system to improve and facilitate the soluble production of TEV protease in E. coli. Optimal expression of soluble His6-TEV was achieved by examining the contribution of chaperone… CONTINUE READING

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