Human recombinant TEV protease (from E. coli)

Supplier: BioVision
BIOV7847-100EA 108 EUR
BIOV7847-100 BIOV7847-1000
Human recombinant TEV protease (from E. coli)
TEV protease are pure active, highly site specific and stable recombinant TEV protease.

  • Biological activity: ≥10000 units/mg

EZCut™ TEV protease is a cysteine protease that recognises the cleavage site of Glu-Xaa- Xaa-Y- Xaa-Gln-(Gly/Ser) and cleaves between Gln and Gly/Ser. The optimal sequence is Glu-Asn-Leu-Tyr-Phe-Gln-Ser/Glycine (ENLYFQS/G). It contains an enhanced form of a catalytic fragment of the NIa protein of tobacco etch virus (TEV).

TEV Protease is a restriction grade protease that has robust activity at 4 °C with high specificity and great stability. The optimal temperature for cleavage with this enzyme is 34 °C. The protease can be used for the removal of affinity tags from fusion proteins. It contains a C-terminal His tag and can be easily removed after cleavage reactions by passing the reaction through a Ni-chelating resin. It is an improved version of TEV protease that is highly site-specific, highly active, and significantly more stable than native TEV protease, resulting in enhanced long-term activity.
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