Recombinant TEV Protease, His 
Datasheet
COA
MSDS
SHIP
Recombinant :
Recombinant TEV Protease, His Source :
Escherichia coli. Molecular Weight :
28.4 kDa, observed by reducing SDS-PAGE. Purity :
> 95% by SDS-PAGE analyses. Biological Activity :
6 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. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Sterile liquid solution contains 50mM Tris, 5mM DTT, 50% glycerol, pH7.5. AA Sequence :
Endotoxin :
Reconstitution :
Storage :
Recombinant Tobacco Etch Virus Protease (rTEV) remains stable up to 1 year at -20°C from date of receipt. Please avoid freeze-thaw cycles. Usage :
This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only. Description :
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.
Recombinant TEV Protease, His Source :
Escherichia coli. Molecular Weight :
28.4 kDa, observed by reducing SDS-PAGE. Purity :
> 95% by SDS-PAGE analyses. Biological Activity :
6 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. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Sterile liquid solution contains 50mM Tris, 5mM DTT, 50% glycerol, pH7.5. AA Sequence :
Endotoxin :
Reconstitution :
Storage :
Recombinant Tobacco Etch Virus Protease (rTEV) remains stable up to 1 year at -20°C from date of receipt. Please avoid freeze-thaw cycles. Usage :
This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only. Description :
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.
Blocking peptide available as BK0165-10000IUP