TEV Protease, recombinant
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Recombinant TEV Protease is a highly site-specific cysteine protease, which is
found in the Tobacco Etch Virus. Due to its sequence specificity, the enzyme
is a very powerful reagent for 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
catalytic domain with an N-terminal polyhistidine tag.
It recognizes a seven amino acid sequence of the general form Glu-X-X-Gln-Gly/Ser, most commonly Glu-Asn-Leu-Tyr-Phe-Gln-Gly, and cleaves between glutamine and glycine or serine. Using the polyhistidine tag at the N-terminus of the protease the enzyme can be easily removed from the cleavage reaction by affinity chromatography following digestion.
Specific activity: 10 U/µl
Unit definition: 1 µl cleaves >80 % of 50 µg control substrate in three hours at 30 °C.
Storage Temperature: -15 °C to -25 °C