SUMO Protease
SUMO protease, Ulp, is a highly active cysteine protease originating from a recombinant gene fragment of yeast Ulp1 (Ubl-specific protease 1). SUMO protease recognizes and cleaves the peptide bond immediately following the Gly-Gly residues at the carboxyl terminus (C-terminal) of the ubiquitin-like (UBL) protein SUMO with high specificity.
The optimal cleavage temperature is 30 ºC and the optimal pH is 8.0. The protease maintains relatively high enzymatic activity over a broad range of pH 6.0-10.0, temperature (2~30ºC), and ionic strength conditions (0-400 mM NaCl). Adding DTT (0.5~2 mM)to the enzyme reaction buffer may improve cleavage efficiency, such as o/n digestion at 4ºC. After cleavage, SUMO protease can be removed from the sample by affinity chromatography utilizing the histidine-tag on its N-terminus.
| Components | Ingredients | Specification | ||
| 200 U | 1000 U | 5000 U | ||
| SUMO Protease (10 U/µL) | 25 mM Tris-HCl, pH 8.0 0.1% Igepal (NP-40) 250 mM NaCl 500 μM DTT 50% (v/v) glycerol |
20 µL | 100 µL | 500 µL |
| 10X SUMO Protease Buffer + Salt | 500 mM Tris acetate, pH 8.0 2% Igepal (NP-40) 1.5 M NaCl 10 mM DTT |
400 µL | 2 x 1 mL | 10 x 1 mL |
| 10X SUMO Protease Buffer - Salt | 500 mM Tris acetate, pH 8.0 2% Igepal (NP-40) 10 mM DTT |
400 µL | 2 x 1 mL | 10 x 1 mL |
Long-term storage: -80°C | ||||