Innovative Tools for Molecular and Cell Biology

Innovative Tools for Molecular and Cell Biology


HRV3C Protease

Highly Active Protease for the ‘PreScission’ Site

Cleavage site of HRV3C Protease

Schematic view of cleavage site


  • 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


  • 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.

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.


  • For shipping and storage information please click on Order#.
Order# Description Amount Price Data Sheet
PR-ETA20010-01 HRV3C Protease, recombinant, GST- & His-Tag 1000 U 320,00 PDF
  • All prices are in EURO excl. VAT and shipping. For further pricing and order information please ask your local distributor.


  • 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.