Description:
HRV 3C Protease is fused to GST, so that the protease is easily removed from cleavage reactions using immobilized glutathione (GSH). HRV 3C Protease is highly active at 4^oC, and also active in a variety of commonly used buffers, providing more flexibility in experimental design to keep the activity and intact structure of the target proteins.

Application:
HRV 3C Protease is a recombinant cysteine protease used to remove fusion tag from proteins with the HRV 3C cleavage sequence. HRV 3C Protease is highly specific for the PreScission Site, Leu-Glu-Val-Leu-Phe-Gln-↓-Gly-Pro, and cleaves between the Gln and Gly residues.

 

Figure. SDS-PAGE Analysis of Cleavage of Control Protein by HRV 3C Protease
A 66 kD GST-fusion protein (1) at 1 mg/ml is reacted with HRV 3C Protease at a ratio of 1: 100 (w/w) in cleavage buffer at 4°C for 4 hours (2) and 3 days (3). The cleaved products are 40 kD and 26 kD.

Source:  E. coli

Supplied With:
HRV 3C Substrate, 100 µl
10x Cleavage buffer

HRV3C Protease 10x Cleavage buffer:
500 mM Tris-HCl (pH 7.0)
1.5 M NaCl
10 mM EDTA
10 mM DTT

Supplied In:
50 mM Tris-HCl (pH 8.0)
150 mM NaCl
10 mM EDTA
1 mM DTT
50% glycerol

Unit definition:
1 unit will cleave >95% of 100 µg His Tag fusion control protein in 50 mM Tris-HCl, 150 mM NaCl, pH 7.5 at 4°C for 16 h.

Recommended Storage Condition: -20°C