SUMO Protease is a recombinant protein obtained by expressing the ULP1 (Ubl-specific protease 1) from Saccharomyces cerevisiae in E. coli. SUMO protease specifically recognizes the three-dimensional structure rather than the linear amino acid sequence of SUMO (Small Ubiquitin-like Modifier), and cleaves the peptide bond after Gly-Gly within the x-Gly-Gly-x motif at the C-terminus of SUMO. Based on this property, SUMO protease offers two major advantages over proteases such as TEV protease and thrombin:After cleavage, the target protein retains its native N-terminus without any extra amino acids, which is the greatest advantage over TEV protease and thrombin.It recognizes a long sequence, giving it very high specificity. 
       SUMO protease is active over a wide ranges temperature (4~30℃), ionic strength (0~300 mM NaCl), imidazole concentration (0~150 mM), reducing-agent (0~8 mM DTT/TCEP), and pH (pH6.0~9.5). In addition, this product carries a polyhistidine (His) tag, which facilitates removal of SUMO protease by affinity chromatography to purify the target protein.
 

Store at -85℃ to -65℃ for 2 years. Aliquot storage is recommended to avoid repeated freezing and thawing.