SUMO Protease, Mass Spectrometry Grade

SUMO (Small Ubiquitin-Like Modifier) protease, derived from Saccharomyces cerevisiae, is a highly active cysteine protease. SUMO cleaves proteins in a highly specific manner, recognizing the tertiary structure of UBL proteins rather than their amino acid sequence. Therefore, this protease can cleave the SUMO tag of recombinant fusion proteins. Except for fusion proteins starting with proline, which cannot be cleaved, proteins starting with leucine, lysine, or valine show relatively low cleavage efficiency. The SUMO fusion tag at the C-terminus of any protein can be completely cleaved (recognizing the QIGG sequence). The target protein released after fusion protein cleavage by SUMO enzyme does not contain extra amino acids, resulting in an expressed product with a native sequence. Therefore, it is an ideal tool enzyme in genetically engineered protein expression.
This product is a high-purity, high-activity SUMO enzyme prepared using an E. coli expression system through multi-step chromatography. It is mainly used for the development of fusion protein cleavage processes.

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