Human rhinovirus 3C protease (HRV3C Protease) is a cysteine protease that recognizes the cleavage site of Leu-Glu-Val-Leu-Phe-Gln/- Gly-Pro, commonly referred to as the 'PreScission' site. It cleaves between Gln and Gly. The recombinant form of the HRV3C protease is a restriction grade protease that has robust activity at 4 °C with high specific activity and great stability. It does not require any special buffer for its activity and can be used in a buffer most suitable for the target protein. This HRV3C Protease is a 47 kDa protein with both GST- and His-tags, so it can be removed by either Ni-chelating or Glutathione (GSH) resin.
Features
Highly specific, e.g. more specific than thrombin protease
Cost effective compared to GE’s 'PreScission' Protease
Easy removal of HRV3C using His- or GST-tags
No buffer restrictions; use the suitable buffer for your target protein
Freeze resistant and functional even after multiple freeze-thaws
Unit Definition
Unit Definition One unit of HRV3C Protease cleaves >95% of 100 μg of control target protein at 4 °C for 16 hours. No non-specific activity has been observed under the same condition with HRV3C Protease to control target protein ratio of 1:10. Prolonged incubation (several days) under the same condition does not show any non-specific cleavage.
Reference
Cordingley et al. (1989) Cleavage of small peptides in vitro by human rhinovirus 14 3C protease expressed in Escherichia coli. J Virol. 63(12), 5037-45.
