金山科研平台，产品价格货期咨询微信：jinshanbio Source:E. coli-derived Accession #:NP_062908 N-terminal Sequence Analysis:Ala Purity:>95%, by SDS-PAGE under reducing conditions and visualized by silver stain. Endotoxin Level: Predicted Molecular Mass:28.5 kDa SDS-PAGE:28 kDa, reducing conditions Activity:Measured by its ability to cleave a fusion protein containing the recognition sequence Glu-Asn-Leu-Tyr-Phe-Gln, with the cleavage point after Gln.TEV Protease cleaves=50% of the control substrate, as measured under the described conditions. . It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant ViralTEV Protease, reaction time, or incubation temperature. Formulation:Supplied as a 0.2 µm filtered solution in Glycerol, Tris, NaCl, EDTA and DTT.See Certificate of Analysis for details. Molecule Information: TEV Protease Long Name: Tobacco Etch Virus Protease Aliases: NIa Background: TEV Protease 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 or in vitro following 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.