Appearance (Form)
Liquid
Appearance (Colour)
Colourless
Appearance (Clarity)
Clear
Purity
Electrophoretic purity is 90% by SDS PAGE
Description
Recombinant TEV Protease is a highly site-specific cysteine protease, which is found in the Tobacco Etch Virus. Due to its sequence specificity, the TEV Protease is a very powerful reagent for the removal of fusion tags from recombinant proteins after protein purification. The enzyme has been genetically modified to increase its activity and resistance to autolysis. It consists of the 27kDa catalytic domain with an N-terminal polyhistidine tag.
TEV Protease specifically recognizes a seven amino acid sequence of the general form
Glu-X-X-Tyr-X-Glnâ(Gly/Ser), most commonly Glu-Asn-Leu-Tyr-Phe-GlnâGly, and cleaves between glutamine and glycine or serine.
TEV Protease can also be used to cleave the affinity tag from a fusion protein immobilized on the affinity resin. Following digestion, the TEV Protease can be easily removed from the cleavage reaction by affinity chromatography using the polyhistidine tag at the N-terminal of the protease.
Application
Removal of affinity tags from fusion protein
