SUMO Protease
SUMO protease (Ulp) is a recombinant cysteine protease derived from yeast Ulp1 (Ubl-specific protease 1), typically expressed in E. coli systems. It precisely recognizes and cleaves the peptide bond immediately downstream of the Gly-Gly motif at the C-terminal of SUMO (small ubiquitin-like modifier) fusion proteins. This protease is widely employed in removing SUMO fusion tags from target proteins during affinity purification, facilitating structural and functional protein analysis. The enzymatic reaction optimally occurs at temperatures around 30 ºC and pH near 8.0, yet remains active at broader ranges (2–30 ºC, pH 6.0–10.0, NaCl concentrations up to 400mM). Inclusion of 0.5–2 mM DTT in reaction significantly enhances proteolytic activity. Protease reactions performed overnight at 4 ºC are suitable for preserving unstable or temperature-sensitive targets. Post-cleavage SUMO protease with N-terminal histidine-tag can be efficiently removed via affinity chromatography.
| 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 | ||||