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28 kDa (Reducing)
＞98% by SDS-PAGE & RP-HPLC
- TEV Protease;
- 10X TEV Protease Buffer + Salt: 500mM Tris-HCl, pH8.0, 500mM NaCl, 5mM EDTA, 10mM DTT;
- 10X TEV Protease Buffer – Salt: 500mM Tris-HCl, pH8.0, 5mM EDTA, 10mM DTT.
The tobacco etch virus (TEV) protease is a useful tool for the removal of fusion tags from recombinant proteins. TEV protease has a strict 7 amino acid cleavage recognition sequence of 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. 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) has (NIa) protease catalytic domain which corresponds to a molecular weight of 28 kDa. It is unique with high specificity and is active at low temperature. rTEV Protease has a 6*His-tag for easy removal from a reaction using nickel affinity resins and has been engineered to improve thermal stability and decrease autolysis.
· 12 months from date of receipt, -20 to -70 °C as supplied.
· 6 months, -20 to -70 °C under sterile conditions after reconstitution.
· 1 week, 2 to 8 °C under sterile conditions after reconstitution.
· Please avoid repeated freeze-thaw cycles.
参考图片
The substrate of 3 μg fusion protein was digested by enzyme,
and the addition amount of rTEV Protease in the sample was 0.3U, 0.6U, 1.0U,
1.3U and 2U, respectively. The substrate is a fusion protein with a molecular
weight of 27 KD and
reacted at 30 ℃ for 1 hour, and the target band of 18kD is produced after rTEV Protease
digestion.
1μg (R: reducing conditions, N: non-reducing conditions).