Tobacco Etch Virus (TEV) protease is a highly site-specific cysteine protease commonly used to remove affinity tags from fusion proteins. It recognizes the sequence Glu-Asn-Leu-Tyr-Phe-GlnGly/Ser (ENLYFQG/S), with cleavage occurring between the Gln and Gly or Ser residue. The most frequently used recognition site is ENLYFQG. The optimal cleavage temperature is 30 C, though conditions such as enzyme amount, incubation time, and temperature may require optimization for different substrates. TEV protease includes an N-terminal 6*His tag, allowing for convenient removal after digestion via Ni affinity chromatography. The recombinant enzyme consists of 231 amino acids, has a molecular mass of approximately 28.4 kDa, and is fully biologically active following purification.
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>95%
TMPS-00131
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