FAQ: Is the rate of TEV Protease cleavage affected by urea, guanidine hydrochloride and/or SDS?

The activity of TEV Protease on an MBP-fusion protein in the presence of these denaturants has been reported by C. Sun et al. as follows: Urea: In up to 2 M urea near complete cleavage is detected. There is some inhibition of TEV Protease cleavage in urea concentrations of 4 M. Guanidine HCl: 1 M guanidine HCl yields slight inhibition of TEV Protease cleavage; however, some TEV Protease activity is still observed in the presence of 3 M guanidine HCL. SDS: TEV Protease is unaffected by concentrations of SDS below 0.5%. In the presence of 1% SDS, TEV Protease retains most, but not all, of its activity.

Sun, C. et al. (2012) Protein Expression and Purification 82, 226–231.