Description | Yeast SUMO protease (also known as Ulp), is a highly activie and robust cysteinyl protease encoded by the Ubl-specific protease 1 gene from Saccharomyces cerevisiae. There are as many as six SUMO proteases in human (SENP1–3, SENP5– 7). Both human and yeast SUMO proteases recognize the tertiary structure of the ubiquitin-like (UBL) protein, i.e., SUMO-1, SUMO-2 and SUMO-3, rather than a short stretch of amino acid sequence, consequently, these SUMO proteases will not cleave within the fused protein of interest. Turbo SUMO Protease is a mixture of core catalytic proteases of both human SENP2 and yeast Ulp1 SUMO proteins, thus SUMO-fusion proteins can be digested by the Turbo SUMO Protease at either ~15 °C overnight or at 30 °C for a few hours. After digestion, Turbo SUMO Protease can be easily removed from the cleavage reaction using Ni agarose beads |
Application | Removal of SUMO tag from fusion proteins |
Source | E. coli over-expressing the C-terminal SENP2 and Ulp1 catalytic protease domains from human and Saccharomyces cerevisiae, respectively. |
Purification | FPLC |
Purity | >95% by SDS-PAGE |
Components | 10 U/µl Turbo SUMO Protease in 50 mM Hepes, pH 7.5, 150 mM NaCl, 0.5 mM DTT, 50% glycerol |
Unit Definition | One unit of SUMO Protease is defined as the amount of enzyme needed to cleave 85% of 2 µg of substrate protein at 30 °C or 15 °C in one hour |
Recommended Reaction Condition | SUMO Protease: Add 1 unit to 2 µg of target SUMO fusion protein Buffer: 50 mM Tris-HCl, pH 8.0, 0.1% Igepal (NP-40), 150 mM NaCl, 1 mM DTT Temperature: 30 °C (1 ~3 hours), 15 °C (overnight) Optimal Salt Concentration: imidazole: <150 mM; NaCl: <300 mM |
Storage | -20°C, or at –80 °C for long-term storage |