His₆-Tagged HRV 3C Protease | High-Specificity for Tag Removal

A Reliable Tool for Structural Biology & Protein Engineering

Efficient removal of fusion tags is an essential step in producing high-quality recombinant proteins for structural and functional studies. MinneBio His₆-Tagged HRV 3C Protease provides highly specific cleavage of engineered protein constructs by recognizing the LEVLFQ↓GP sequence, enabling clean and controlled tag removal while preserving protein integrity.

Designed for precise recognition and cleavage of fusion protein substrates, MinneBio His₆-Tagged HRV 3C Protease provides researchers with a reliable tool for preparing native-like proteins for protein purification, structural biology, protein engineering, and biopharmaceutical development.

1. Upper Left Image: Purified MinneBio His₆-Tagged HRV 3C Protease

SDS-PAGE analysis demonstrates the high purity and consistent quality of recombinant MinneBio His₆-Tagged HRV 3C Protease, supporting reliable performance for precise protein processing applications.

2. Upper Right Image: Efficient Cleavage of a Fusion Protein by MinneBio His₆-Tagged HRV 3C Protease

Following incubation with MinneBio His₆-Tagged HRV 3C Protease for 16 hours at 4°C, the fusion protein was efficiently processed into two distinct fragments. This result demonstrates the enzyme’s high specificity and activity under mild cleavage conditions, enabling precise removal of fusion tags while preserving target protein integrity.

3. Lower Image: Specific Recognition and Cleavage Mechanism

MinneBio His₆-Tagged HRV 3C Protease specifically recognizes and cleaves the LEVLFQ↓GP sequence between glutamine (Q) and glycine (G), enabling efficient fusion tag removal and the generation of native-like recombinant proteins for structural and functional studies.