Recombinant EN-TEV Protease Protein, ＞98% (SDS-PAGE), high purity

Item Number

rp156465

• Product Name: Recombinant EN-TEV Protease Protein, ＞98% (SDS-PAGE), high purity
• Synonyms: NIa; P1 Protease; TEV Protease; Tobacco Etch Virus Protease
• Grade: ActiBioPure™, Azide Free, Bioactive, Carrier Free
• Specifications & Purity: ActiBioPure™, Bioactive, Carrier Free, Azide Free, ≥98%(SDS-PAGE), Lot by Lot
• Purity: ＞98% (SDS-PAGE)
• Bioactivity: Measured by its ability to cleave a fusion protein containing the recognition sequence Glu-Asn-Leu-Tyr-Phe-Gln-Gly/Ser , with the cleavage point after Gln. One unit of TEV protease cleaves > 85% of 3 μg of control substrate in 1 hour at pH 8.0 at 30°C.It
• Expression System: E. coli
• Species: Tobacco etch virus (TEV)
• Amino Acids: 2038-2279 aa
• Sequence: GHHHHHHHGESLFKGPRDYNPISSSICHLTNESDGHTTSLYGIGFGPFIITNKHLFRRNNGTLVVQSLHGVFKVKDTTTLQQHLVDERDMIIIRMPKDFPPFPQKLKFREPQREERICLVTTNFQTKSMSSMVSDTSSTFPSGDGIFWKHWIQTKDGQCGSPLVSTRDGFIVGIHSASNFANTNNYFTSVPKNFMELLTNQEAQQWVSGWRLNADSVLWGGHKVFMVKPEEPFQPVKEATQLMNRRRRR
• Protein Tag: N-His
• Predicted molecular weight: 28.6 kDa
• SDS-PAGE: 28.6 kDa

Product Description

Purity:
>98%, by SDS-PAGE visualized with Coomassie® Blue Staining.
Description:
TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification. Its high specificity and activity at a wide range of pH and ionic strength make TEV Protease more versatile than many other proteases used for the same purpose. Unlike factor Xa, enteropeptidase or thrombin, TEV Protease has not been found to cleave at unintended sites, even when present at a high concentration. TEV Protease is a 3C-type protease that cleaves substrates with a consensus sequence of ENLYFQG. Cleavage occurs between Q and G. Since the final aa remains on the cleaved protein where it could potentially affect structure or function, substitution of a variety of aa have been tested. In order of efficiency, S, A, M, Y, D, N, E, K or L may be effectively used in place of G. Several of the remaining aa may also vary, giving a final consensus sequence of ExxYF(M)Q(E)/G(S, A or others) where aa in parenthesis are alternatives and x is any aa. The autocatalytic site of NIa at S2256 has been mutated to an N for improved stability of the protease.
Tobacco Etch Virus Protease is a highly site-specific cysteine protease that is found in the tags from fusion proteins. The optimal temperature for cleavage is 30°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.