Tobacco etch virus protease retains its activity in various buffers and in the presence of diverse additives.

@article{Sun2012TobaccoEV,
  title={Tobacco etch virus protease retains its activity in various buffers and in the presence of diverse additives.},
  author={Changsheng Sun and Jiongqiu Liang and Rui Shi and Xuna Gao and Ruijuan Zhang and Fulin Hong and Qihang Yuan and Shengbin Wang},
  journal={Protein expression and purification},
  year={2012},
  volume={82 1},
  pages={226-31}
}
Tobacco etch virus (TEV) protease is widely used to remove tags from recombinant fusion proteins because of its stringent sequence specificity. It is generally accepted that the high concentrations of salts or other special agents in most protein affinity chromatography buffers can affect enzyme activity, including that of TEV protease. Consequently, tedious desalination or the substitution of standard TEV reaction buffer for elution buffer are often needed to ensure TEV protease activity when… CONTINUE READING
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An overview of enzymatic reagents for the removal of affinity tags

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