SUMO protease, also known as Ulp, is a highly active cysteine protease derived from a recombinant gene fragment of Ubl-specific protease 1 in Saccharomyces cerevisiae. SUMO proteases recognize and cleave peptide bonds after the SUMO carboxyl (C-terminal) of the Ubiquitin-like (UBL) protein in a highly specific manner. SUMO is an Ubiquitin-like protein that is commonly found in post-translation modification (PTM), which plays an important role in the stability of proteins and the regulation of biological functions.

The optimal lysis temperature for SUMO proteases is 30 ºC and the optimal pH is 8.0, but it is in the wide pH range (6.0-10.0) and temperature range (2 to 30 ºC). The ion strength range (0-400mM NaCl) maintains high enzyme activity. In special scenario use, the sample can be digested overnight at 4ºC to maintain the structure and biological activity of the protein of interest. SUMO Protease has higher digestion activity in the presence of the reducing agent DTT (0.5~2mM), and the addition of DTT at the appropriate concentration to the digestion system can significantly improve the digestion efficiency, especially during long-term digestion, such as Enzymes are cut overnight at 4 ºC. The lysed SUMO protease can be removed using histidine tags at its N-terminus for affinity chromatography.