Sumo Protease - 25.5 Kda, 3 Year Shelf Life | High Purity > 95%, Easy Removal Via Affinity Chromatography, Specific Tertiary Structure Recognition

SUMO Protease is a recombinant fragment of Ulp1 (Ubl-specific protease 1) expressed in E.coli. SUMO Protease cleaves in a highly specific manner, recognizing the tertiary structure of the SUMO (small ubiquitin-related modifier) rather than an amino acid sequence. The protease can be used to cleave SUMO from recombinant fusion proteins. The optimal temperature for cleavage is 30, however, the enzyme is active over wide ranges of temperature and pH (pH 7.0-9.0). Following digestion, SUMO Protease is easily removed from the cleavage reaction by affinity chromatography using the polyhistidine tag at the N-terminus of the protease. After cleavage, the released protein has native N-terminal amino acid sequence without additional amino acid.

Product features
1. High purity more than 95% by SDS-PAGE assay;
2. High specificity recognition the SUMO tertiary structure rather than aa sequence with native N-terminal sequence released;
3.Easily removal the protease can be removed by one step optimized chromatography.

Specifications
MW.Approximately 25.5 kDa.
Purity> 95 % by SDS-PAGE analysis.
Unit: One unit of SUMO Protease cleaves AY85% 2g fusion protein in 1 h at 30.
Formulation: 50% glycerol solution containing PBS buffer, DTT. pH 8.0.
Endotoxin: Less than 1 EU/A A g of SUMO protease as determined by LAL method.
Recommended Conditions for Cleavage of a Fusion Protein
fusion protein 2mg/ml): 1mg
SUMO protease: 10U
10 x PBS: 0.1ml
Add ddH20 to: 1ml
Temp): 30
Time (hour): 1~2
Usage: This material is for laboratory purposes. NOT FOR HUMAN USE.