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SP4020: SUMO Protease 2

LifeSensors SP4020 is a SUMO Protease 2 enzyme used for precise removal of SUMO tags from fusion proteins in research, enabling efficient protein purification and analysis.

$393.00$5,687.00

Digestion and removal of SUMOpro tags from recombinant fusion proteins made with our SUMOpro Expression systems (Cat.#s: 1010A, 1016, 1010K, 1011, 2150, 2151)

Benefits

  • SUMO Protease 1 cleaves consistently over a broad range of temperature (30°C is optimal), pH [5.5-9.5], and ionic strength. SUMO Protease 1 contains a polyhistidine tag at the N-terminus, making it easy to remove from the cleavage reaction by affinity chromatography.
For removal of SUMOpro3 tags from fusion proteins expressed from the following SUMOpro3 expression systems: (Cat.#s: 1010A, 1016, 1010K, 1011, 2151). SUMO Protease 2, a highly active and robust recombinant protease, cleaves hSUMO3 from recombinant fusion proteins. Unlike thrombin, EK, or TEV protease, which recognize short, linear sequences, SUMO Protease 2 recognizes the tertiary structure of huSUMO3. As a result, SUMO Protease 2 will not cleave within the fused protein of interest. By purchasing this product, the purchaser agrees to comply with the terms of our Limited Use Label License. Need bulk quantities? We would be happy to work out a custom price that fits your budget. Please click here to request a quote.

Info

Species Human
Source E. coli
Tag His
Molecular Weight 28 kDa
Quantity 250, 500, 1000, 5000 units
Concentration Variable
Formulation 50 mM Hepes pH 7.5, 150 mM NaCl, 10% glycerol
Storage -80°C, avoid freeze/thaw cycles

Digestion and removal of SUMOpro tags from recombinant fusion proteins made with our SUMOpro Expression systems (Cat.#s: 1010A, 1016, 1010K, 1011, 2150, 2151)

Benefits

  • SUMO Protease 1 cleaves consistently over a broad range of temperature (30°C is optimal), pH [5.5-9.5], and ionic strength. SUMO Protease 1 contains a polyhistidine tag at the N-terminus, making it easy to remove from the cleavage reaction by affinity chromatography.

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