Catalog Products » Recombinant Proteins » Enzymes and Inhibitors » Tobacco Etch Virus Protease (TEV Protease)

TEV Protease

*This product has been discontinued!*
Recombinant TEV Protease is a site-specific protease purified from E. coli by the affinity tag, GST tag. The protease can be used for the removal of affinity tags from fusion proteins. The seven-amino-acid recognition site for TEV protease is Glu-Asn-Leu-Tyr-Phe-Gln-Gly with cleavage occurring between Gln and Gly. The optimal temperature for cleavage is 30°C; however, the enzyme can be used at temperatures as low as 4°C. Following digestion, TEV protease can be removed from the reaction via the GST tag sequence by affinity chromatography.
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Description

Recombinant TEV Protease is a site-specific protease purified from E. coli by the affinity tag, GST tag.The seven-amino-acid recognition site for TEV protease is Glu-Asn-Leu-Tyr-Phe-Gln-(Gly/Ser) [ENLYFQ(G/S)] with cleavage occurring between Gln and Gly. The optimal temperature for cleavage is 30°C; however, the enzyme can be used at temperatures as low as 4°C. Following digestion, TEV protease can be removed from the reaction via the GST tag sequence by affinity chromatography (GenScript Glutathione Resin L00206).

Synonyms

Tobacco Etch Virus Protease (TEV Protease)

Overview
Source E. coli

Properties
Reaction Buffer 10xTEV buffer:
0.50 M Tris-HCl (pH 8.0), 10 mM DTT, 5 mM EDTA.
Purity > 90 % by SDS-PAGE analysis.
Physical Appearance Clear colorless liquid.
Biological Activity One unit is defined as the amount of enzyme needed to cleave 3 μg of fusion protein in 1 hour to 85 % completion at 30°C in a buffer containing 50 mM Tris-HCl, pH 8.0, 0.5 mM EDTA, and 1 mM DTT.
Usage This material is for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE.
Formulation A 0.2 µm filtered solution in 25 mM Tris-HCl, pH 8.0, 75 mM NaCl, 5 mM EDTA, 10 mM GSH, with 50 % Glycerol.
Storage & Stability Store recombinant TEV protease at -70°C for long term or at -20°C for < 6 months.

Applications
A number of variables can be changed to optimize the cleavage of any specific protein. The amount of TEV protease, the temperature of the incubation, and the time needed for cleavage may be examined. If the protein of interest is heat-labile, then 4°C incubations are recommended. Reactions at 4°C will require longerincubation times and/or more TEV protease.

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