MinneBio SUMO Protease is a highly specific recombinant Ulp1 (Ubiquitin-like-specific protease 1) derived from Saccharomyces cerevisiae. The enzyme efficiently removes SUMO fusion tags from recombinant proteins by recognizing the native three-dimensional structure of the SUMO domain rather than a short linear peptide sequence. This unique recognition mechanism enables precise cleavage while preserving the authentic N-terminus of the target protein, making it an ideal tool for structural biology, protein engineering, and functional characterization studies.
The recombinant enzyme contains a His₆ tag, enabling convenient removal of the protease after digestion through immobilized metal affinity chromatography (IMAC).
SDS-PAGE analysis demonstrates the high purity and consistent quality of recombinant MinneBio His₆-Tagged SUMO Protease, supporting reliable performance in precise protein processing applications.
Following incubation with MinneBio His₆-Tagged SUMO Protease for 16 hours at 4°C, the SUMO-GFP fusion protein was efficiently processed into two distinct fragments. This result demonstrates the enzyme’s high specificity and robust activity under mild cleavage conditions, enabling effective fusion tag removal while maintaining target protein integrity.
MinneBio His₆-Tagged SUMO Protease specifically recognizes the three-dimensional structure of the SUMO domain and cleaves precisely after the SUMO sequence at the C-ter (-GG) sequence. This highly specific cleavage mechanism enables efficient removal of SUMO fusion tags and generation of native-like recombinant proteins for downstream structural and functional studies.
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