Yeast SUMO protease variant corresponding to the active SUMO protease domain (amino acids Leu403-Lys621) expressed recombinantly in and purified from E. coli..
Highlights:
The SUMO domain can act to improve expression and stability of proteins made in E. coli. Hence, SUMO-fusion proteins hold great interest for those performing protein expression in E. coli. The SUMO protease is a highly specific and active protease that can be used to cleave the bond between the SUMO tag and the protein of interest. Further purification, for example by Nickel-affinity columns, can capture the SUMO tag and SUMO protease, yielding a highly pure protein of interest.
From the laboratory of Arnon Lavie, PhD, University of Illinois at Chicago.
Catalog Number | Product | DataSheet | Size | AVAILABILITY | Price | Qty |
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Product Type: | Protein |
Name: | Yeast SUMO protease (Ulp1p; protease domain; M1_K402del) |
Accession ID: | E7KUV8, protease domain |
Source: | Recombinant expression in E. coli |
Molecular Weight: | 28,168 Da |
Amino Acid Sequence: | MGSSHHHHHHSSGGTENLYFQGHMLVPELNEKDDDQVQKALASRENTQLMNRDNIEITVRDFKTLAPRRWLNDTIIEFFMKYIEKSTPNTVAFNSFFYTNLSERGYQGVRRWMKRKKTQIDKLDKIFTPINLNQSHWALGIIDLKKKTIGYVDSLSNGPNAMSFAILTDLQKYVMEESKHTIGEDFDLIHLDCPQQPNGYDCGIYVCMNTLYGSADAPLDFDYKDAIRMRRFIAHLILTDALK |
Fusion Tag(s): | N-terminal polyhistidine tag |
Purity: | >95% |
Buffer: | 12.5 mM Tris (pH 7.5), 250 mM NaCl, 125 mM Imidazole, 1 mM DTT, 50 % glycerol |
Concentration: | 3.7mg/mL |
Activity: | Cutting will be dependent on spacing between the SUMO tag and the rest of the protein. Hence, it is hard to define activity. In most cases, 1 hour incubation at a ratio 1:200 at room temperature will result in >99% cleavage of the SUMO tag. |
Suggested Amount per Experiment: | 10-1000ug, To remove the SUMO tag, incubate the SUMO-X fusion protein with SUMO protease at a ratio of 200:1 (w:w) |
Shipped: | Dry Ice |
SDS-PAGE Analysis
(Left) Purity of protein preperation. (Right) Protein X was expressed as a SUMO fusion protein. To remove the SUMO tag, the SUMO-X fusion protein was incubated with SUMO protease at a ratio of 200:1 (w:w); after 10 minutes, >99% of the protein was cleaved.
1. Kim L, Kwon DH, Heo J, Park MR, Song HK. Use of the LC3B-fusion technique for biochemical and structural studies of proteins involved in the N-degron pathway. J Biol Chem. 2020;295(9):2590-2600. View article
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