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TEV Protease, His

Tobacco Etch Virus Protease is a highly site-specific cysteine protease that is found in the Tobacco Etch Virus (TEV). The optimum recognition site for this enzyme is the sequence Glu-Asn-Leu-Tyr-Phe-Gln-(Gly/Ser) [ENLYFQ(G/S)] and cleavage occurs between the Gln and Gly/Ser residues, The most commonly used sequence is ENLYFQG. The protease is used to cleave affinity Tobacco Etch Virus Protease (rTEV) contains 231 amino acids with N-terminal His tagged. A fully biologically active molecule, rTEV has a molecular mass of 28.4 kDa and is obtained by proprietary chromatographic techniques at GenScript.
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Z03030-1K

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Product Introduction
Source E. coli
Purity > 95% by SDS-PAGE analyses.
Biological Activity 10 IU/μl.
Unit Definition One unit of TEV protease cleaves > 85% of 3 μg of control substrate in 1 hour at pH 8.0 at 30°C.
Molecular Weight 28.4 kDa, observed by reducing SDS-PAGE.
Formulation Sterile liquid solution contains 50mM Tris, 5mM DTT, 50% glycerol, pH7.5.
Storage & Stability Recombinant Tobacco Etch Virus Protease (rTEV) remains stable for 1 year at -20°C from date of receipt. Please avoid freeze-thaw cycles.
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TEV Protease, His

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TEV Protease, His

Lane 1: 2 μg of TEV Protease, His, non-reducing (NR)
Lane 2: 2 μg of TEV Protease, His, reducing (R)
> 95% as analyzed by SDS-PAGE »

TEV Protease, His

The fusion protein (20 μg) was incubated with varying enzyme doses (2U, 3U, 4U, 5U) in a 30°C water bath for 1 hour. »

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Background
Synonyms rTEV, TEV, P1 protease
Target Background Tobacco Etch Virus Protease is a highly site-specific cysteine protease that is found in the Tobacco Etch Virus (TEV). The optimum recognition site for this enzyme is the sequence Glu-Asn-Leu-Tyr-Phe-Gln- (Gly/Ser) [ENLYFQ(G/S)] and cleavage occurs between the Gln and Gly/Ser residues, The most commonly used sequence is ENLYFQG. The protease is used to cleave affinity tags from fusion proteins. The optimal temperature for cleavage is 30°C; also it can be used at temperature as low as 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of recombinant viral TEV protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin. Recombinant Tobacco Etch Virus Protease (rTEV) contains 231 amino acids with N-terminal His tagged.A fully biologically active molecule, rTEV has a molecular mass of 28.4 kDa and is obtained by proprietary chromatographic techniques at GenScript.
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For research use only. Not intended for human or animal clinical trials, therapeutic or diagnostic use.


Citations
Carlos Moreno-Yruela, et al. Structural basis of SIRT7 nucleosome engagement and substrate specificity. Nature Communications. (2025-02)
Paul Monassa , et al. Biochemical and structural analysis of N-myristoyltransferase mediated protein tagging. Methods Enzymol . (2024-03)
Jared Hollinger, et al. Expression and purification of the mitochondrial transmembrane protein FAM210A in Escherichia coli. Protein Expr Purif. (2023-06)
Danielle M Garshott, et al. iRQC, a surveillance pathway for 40S ribosomal quality control during mRNA translation initiation. Cell Rep. (2021-08)