SUMO Protease (Ulp1p, M1_K402del)

Yeast SUMO protease variant corresponding to the active SUMO protease domain (amino acids Leu403-Lys621) expressed recombinantly in and purified from E. coli..

Highlights:

  • Highly specific and active protease for efficient cleavage of SUMO tags from proteins of interest
  • Contains N-terminal polyhistidine tag; Useful for further downstream purification steps

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 Size AVAILABILITY Price Qty
EB1008
SUMO Protease (Ulp1p, M1_K402del), 100ug
100ug In stock
Price: $199.00
EB1009
SUMO Protease (Ulp1p, M1_K402del), 1mg
1mg In stock
Price: $1,499.00

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Specifications
Name: Yeast SUMO protease (Ulp1p; protease domain; M1_K402del)
Accession ID: E7KUV8, protease domain
Molecular Weight: 28,168 Da
Fusion Tag(s): N-terminal polyhistidine tag
Amino Acid Sequence: MGSSHHHHHHSSGGTENLYFQGHMLVPELNEKDDDQVQKALASRENTQLMNRDNIEITVRDFKTLAPRRWLNDTIIEFFMKYIEKSTPNTVAFNSFFYTNLSERGYQGVRRWMKRKKTQIDKLDKIFTPINLNQSHWALGIIDLKKKTIGYVDSLSNGPNAMSFAILTDLQKYVMEESKHTIGEDFDLIHLDCPQQPNGYDCGIYVCMNTLYGSADAPLDFDYKDAIRMRRFIAHLILTDALK
Buffer: 12.5 mM Tris (pH 7.5), 250 mM NaCl, 125 mM Imidazole, 1 mM DTT, 50 % glycerol
Source: Recombinant expression in E. coli
Purity: >95%
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
Data

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.

Provider
From the laboratory of Arnon Lavie, PhD, University of Illinois at Chicago
References

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