HRV-3C protease fuses with GST 

HRV-3C protease fuses with GST is a recombinant protease fused with HRV-3C protease and GST, which recognizes the LEVLFQGP polypeptide sequence. HRV-3C protease fuses with GST precisely cleaves between glutamine and glycine-proline residues to remove fusion tags from target proteins. HRV-3C protease fuses with GST exhibits cleavage activity both in vitro in silkworm fat body lysates and in vivo in silkworm larval fat bodies, and achieves functional expression in E. coli and silkworm-baculovirus expression systems. HRV-3C protease fuses with GST can be applied to recombinant protein-related research^[1][2].

GST-HRV-3C protease fuses with GST (1:1-1:2 (v/v) ratio; 4 h) expressed in Escherichia coli Rosetta-gami B cells potently cleaves its target substrate GST-3Csite-VP15^[1].
GST-HRV-3C protease fuses with GST (1:1-1:3 (v/v) ratio; 4 h) expressed in silkworm (Bombyx mori) larvae fat bodies cleaves its target substrate GST-3Csite-VP15-FLAG, with more complete cleavage observed at higher protease lysate ratios^[1].
GST-HRV 3C protease (1:50 (w/w) ratio; 6 mM DTT; 0.5 mM EDTA; 1-16 h; 4 °C, 25 °C) actively cleaves the GST-Cyclin A fusion protein, and maintains efficient proteolytic activity across PBS, Tris-HCl (pH 7.5, 8), and HEPES (pH 7.5, 8) buffer systems^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

2178107-79-2

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[HRV-3C protease fuses with GST]

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• [1]. Xu J, et al. In vivo enzymatic digestion of HRV 3C protease cleavage sites-containing proteins produced in a silkworm-baculovirus expression system. Biosci Rep. 2022 Jun 30;42(6):BSR20220739.

  [2]. Antoniou G, et al. Optimization of Soluble Expression and Purification of Recombinant Human Rhinovirus Type-14 3C Protease Using Statistically Designed Experiments: Isolation and Characterization of the Enzyme. Mol Biotechnol. 2017;59(9-10):407-424.