HRV 3C Protease for fusion tag cleavage from recombinant proteins
HRV 3C Protease is a highly purified recombinant protein derived from human Rhinovirus type 14 and expressed in E. coli. HRV 3C Protease cleaves a specific amino acid sequence (LeuGluValLeuPheGln ↓ GlyPro) and can be used to cleave fusion tag sequences from recombinant proteins that contain an HRV 3C protease cleavage site.
This 3C protease also contains an N-terminal 6xHN tag (modified his-tag), and thus can be easily eliminated from the protease reaction solution through immobilized metal affinity chromatography (IMAC) using TALON Metal Affinity Resin or His60 Ni Superflow Resin. In addition, because the enzyme is active at 4°C, protein cleavage reactions can be performed under conditions that do not affect activity or stability of the target protein.
This product also includes a Cleavage Control Fusion Protein for use as a positive control. The Control Protein has an N-terminal 6xHN tag, and digestion of the protein with HRV 3C Protease results in a 52-kDa TF peptide and a 24-kDa GST peptide that can be visualized by SDS-PAGE.
Overview
Active at 4°C, allowing the cleavage reaction to proceed under conditions that do not affect the activity or stability of the recombinant target protein
6xHN tag allows removal of the 3C protease from the reaction using IMAC
1 unit (U) is defined as the amount of enzyme that cleaves at least 95% of the Cleavage Control Fusion Protein (100 µg in 1X HRV 3C Cleavage Buffer) in 16 hours at 4°C.
HRV 3C Protease for fusion tag cleavage from recombinant proteins
HRV 3C Protease is a highly purified recombinant protein derived from human Rhinovirus type 14 and expressed in E. coli. HRV 3C Protease cleaves a specific amino acid sequence (LeuGluValLeuPheGln ↓ GlyPro) and can be used to cleave fusion tag sequences from recombinant proteins that contain an HRV 3C protease cleavage site.
This 3C protease also contains an N-terminal 6xHN tag (modified his-tag), and thus can be easily eliminated from the protease reaction solution through immobilized metal affinity chromatography (IMAC) using TALON Metal Affinity Resin or His60 Ni Superflow Resin. In addition, because the enzyme is active at 4°C, protein cleavage reactions can be performed under conditions that do not affect activity or stability of the target protein.
This product also includes a Cleavage Control Fusion Protein for use as a positive control. The Control Protein has an N-terminal 6xHN tag, and digestion of the protein with HRV 3C Protease results in a 52-kDa TF peptide and a 24-kDa GST peptide that can be visualized by SDS-PAGE.
Overview
Active at 4°C, allowing the cleavage reaction to proceed under conditions that do not affect the activity or stability of the recombinant target protein
6xHN tag allows removal of the 3C protease from the reaction using IMAC
1 unit (U) is defined as the amount of enzyme that cleaves at least 95% of the Cleavage Control Fusion Protein (100 µg in 1X HRV 3C Cleavage Buffer) in 16 hours at 4°C.
