Recombinant Yeast SUMO Protease/Ulp1 is expressed in E. coli. SUMO protease Ulp1 recognises the folded SUMO tag and cleaves it precisely from fusion proteins, leaving a native N-terminus. Supplied as a solution in 50% glycerol with purity of >98% by SDS-PAGE and endotoxin below 0.005 EU/U by LAL assay. Suitable for bioprocessing. For research use only.
This product (SKU: GKRP0051) is expressed in E. coli and is supplied unconjugated. It has a calculated molecular weight of 28 kDa (monomer) and an observed molecular weight of 28 kDa (reducing) on SDS-PAGE. Purity is >98% by SDS-PAGE and endotoxin is <0.005 EU/U by the LAL method.
Leu403-Lys621, with an N-terminal His-tag and a TEV cleavage site
Biological Activity:
SUMO protease Ulp1p is highly specific for cleaving SUMO protein fusions. It exhibits both high activity and specificity, making it a preferred choice for cleaving SUMO tags independently of the target protein’s structure, leaving no additional amino acids at the N-terminus of the target protein. Specific activity is >1×105 Units/mg. One unit of SUMO Protease Ulp1p is the amount of enzyme required to cleave >90% of 20 µg of SUMO-tag fused protein at 30°C in one hour.
Specific Activity:
>1 × 105 Units/mg
Endotoxin:
<0.005 EU/U of protein, as determined by the LAL method.
Purity:
>98% by SDS-PAGE and quantitative densitometry by Coomassie Blue staining.
Formulation:
In 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 1 mM DTT, 50% Glycerol.
Reconstitution:
Not required (liquid).
Storage:
12 months from date of receipt at -20°C. Avoid repeated freeze-thaw cycles.
SUMO protease Ulp1p is highly specific for cleaving SUMO protein fusions. It exhibits both high activity and specificity, making it a preferred choice for cleaving SUMO tags independently of the target protein’s structure, leaving no additional amino acids at the N-terminus of the target protein.
Recombinant SUMO Protease Ulp1p (2 µg/lane) on SDS-PAGE under reducing (R) conditions. The gel was stained using Coomassie Blue showing a band at 28 kDa and purity greater than 98%.
SDS-PAGE analysis of Ulp1p cleavage reaction with 20 µg of substrate at 30°C for 60 min with varying enzyme units. Greater than 90% cleavage observed with 1U.
SDS-PAGE analysis of 1U Ulp1p cleavage reaction with 20 µg of substrate at 30°C with varying incubation time. Greater than 90% cleavage observed at 60 min.
