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Cat. No.: TEV-1k (for 1,000U)

Cat. No.: TEV-5k (for 5,000U)

Description

TEV Protease (Tobacco etch virus protease) is a recombinant protease derived from tobacco etch virus (TEV) Nla, which is used to excise affinity tags of purified fusion proteins. TEV Protease has strong site-specificity and can recognize the seven amino acid sequence (Glu-Asn-Leu-Tyr-Phe-Gln-Gly) of EXXYXQ (G/S), most commonly ENLYFQG, whose cleavage site is between glutamine and glycine or serine. The enzyme is active in a wide range of pH 5.5-8.5 and 4-30 °C so that the reaction conditions can be modified according to the target proteins. TEV Protease is expressed and purified from E. coli. TEV Protease has a polyhistidine tag and can be removed by affinity chromatography after the enzyme digestion reaction.

Unite definition

In 1×TEV Buffer (50 mM Tris-HCl, pH 8.0, 0.5 mM EDTA, 1 mM DTT), the amount of enzyme required to cleave >85% of the 3 µg control substrate at 30 °C for 1 h is defined as an active unit.

Storage

TEV Protease can be stored for 2 years at -80 °C for a long time or for 6 months at -20 °C after sub-packaged to avoid repeated freezing and thawing. 10 x TEV Buffer can be stored at -20 °C.

Protocol

If the protein is thermally unstable, incubate at 4 °C for a longer time or increase the amount of enzyme used.

1. Set up the following reaction system in EP tube:
2. After mixing the system, incubate at 30 °C. Take 30 μl solution at 1, 2, 4, and 6 h respectively, and place it in a separate EP tube.
3. Add 20 μl 2 x SDS Loading Buffer to the above EP tube and place it at -20 °C.
4. Take 30 μl sample for SDA-PAGE analysis.

Note

To achieve the best digestion result, please ensure that the recombinant protein is partially or completely purified. 

Related: Enhanced TEV Protease

Only for research and not intended for treatment of humans or animals

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