Description

      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、Hige 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.

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

Example result

Storage

        This is stable at -20℃ for more than 2 years.

Usage

        This material is for laboratory purposes. NOT FOR HUMAN USE.