The SUMO protease releases target proteins from TriAltus’s Im7 resin. This protease recognizes SUMO tertiary structure – not a specific amino acid sequence – to cleave and release the target protein from the Im7-bound CL7 tag.
PURITY | ~100% (SDS gel analysis)
ENZYME SOURCE | Yeast protein overexpressed in E. coli with histidine (His) tag
CLEAVAGE SITE | SUMOP cleaves after the C-terminal glycine at the end of the SUMO sequence. If the target protein is fused downstream of the SUMO C-terminus, SUMOP cleavage renders the native protein sequence without any additional amino acids.
CLEAVAGE EFFICIENCY | 1 ug protease will digest 2 mg protein with 99% efficiency at 4°C in 40 minutes.
STORAGE/SHIPPING CONCENTRATION | ~7.5 mg/mL
SHIPPING CONDITIONS | We ship SUMO protease on dry ice in buffer (15 mM Tris (pH 8.0), 0.2 M NaCl, 50% glycerol).
RECOMMENDED STORAGE CONDITIONS | -80°C long term or -20°C for 2-3 months in shipping buffer
Additional processing information: SUMOP releases CL7-tagged proteins from the Im7 resin-bound CL7 tag. The final protease concentration in the eluted sample comprises ~1.5-3% of total impurities. If needed, SUMOP can be purified from the sample with a His-trap column or via size exclusion chromatography.