SUMO Protease

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SUMO Protease

SUMO protease is a recombinant cysteine protease, it is derived from yeast Ulp1 and expressed in E.coli system. SUMO protease can recognize and cleave the peptide bond downstream of the Gly-Gly motif at the C-terminal of SUMO (small ubiquitin-like modifier) fusion proteins. This protease is applied widely in removal of SUMO fusion tags from target proteins in affinity purification, facilitating structural and functional protein analysis. The post-cleavage SUMO protease with N-terminal histidine-tag can be removed effectively by affinity chromatography.

UBI-specific protease 1 can recognize proteins with complete SUMO (Small Ubiquitin-Like Modifier) and cleave the SUMO from the fusion protein. SUMO protease has high specificity because of its long recognition sequence, which can maintain high activity in a wide reaction environments. SUMO protease has a polymerized His label, which results in convenient removal of SUMO protease by purification of affinity chromatography.