TEV

Tobacco Etch Virus Protease Recombinant
Cat. No.
BT4737
Source
Escherichia Coli.
Synonyms
rTEV, TEV, P1 protease.
Appearance
Sterile liquid formulation.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock
Quick Inquiry

Description

Recombinant TEV Protease (rTEV) is a site-specific protease purified from E. coli. The protease can be used for the removal of affinity tags from fusion proteins. The seven-amino-acid recognition site for rTEV is Glu-Asn-Leu-Tyr-Phe-Gln-Gly with cleavage occurring between Gln and Gly. The optimal temperature for cleavage is 30°C; however, the enzyme can be used at temperatures as low as 4°C.
The rTEV contains His tag.
The rTEV is purified by proprietary chromatographic techniques.

Product Specs

Introduction
TEV protease, also known as the 27 kDa catalytic domain of the Nuclear Inclusion a (NIa) protein from the tobacco etch virus (TEV), exhibits higher sequence specificity compared to factor Xa, thrombin, or enterokinase, making it a valuable tool for cleaving fusion proteins. TEV protease recognizes a linear epitope generally represented as E-Xaa-Xaa-Y-Xaa-Q-(G/S), with cleavage occurring between the Q and G or Q and S residues. The most frequently used sequence is ENLYFQG.
Description
Recombinant TEV Protease (rTEV), a site-specific protease derived from E. coli, facilitates the removal of affinity tags from fusion proteins. rTEV recognizes the seven-amino-acid sequence Glu-Asn-Leu-Tyr-Phe-Gln-Gly, cleaving between Gln and Gly. While the optimal cleavage temperature is 30°C, the enzyme remains active at temperatures as low as 4°C. rTEV is engineered with a His tag and purified using proprietary chromatographic methods.
Physical Appearance
Sterile liquid.
Formulation
rTEV is supplied in a buffer consisting of 25mM Tris, pH 8.0, 75mM NaCl, 5mM EDTA, 10mM GSH, and 50% Glycerol.
Unit Definition
One unit of rTEV is defined as the amount required to cleave 3 µg of fusion protein to 85% completion within 1 hour at 30°C in a buffer containing 50 mM Tris-HCl (pH 8.0), 0.5 mM EDTA, and 1 mM DTT.
Stability
For optimal storage, rTEV should be kept at temperatures below -18°C. While it can remain stable at 4°C for up to one week, repeated freeze-thaw cycles should be avoided.
Purity
The purity of rTEV is greater than 90%, as determined by SDS-PAGE analysis.
Cleavage Conditions
To achieve optimal cleavage for a specific protein, several factors can be adjusted, including the amount of rTEV used, incubation temperature, and incubation time. For heat-sensitive proteins, incubations at 4°C are recommended, potentially requiring longer incubation times or a higher concentration of rTEV.
Synonyms
rTEV, TEV, P1 protease.
Source
Escherichia Coli.

Product Science Overview

Introduction

Tobacco Etch Virus (TEV) protease is a highly specific protease derived from the Tobacco Etch Virus. It is widely used in biotechnology for its ability to cleave fusion proteins at specific recognition sites. The recombinant form of this protease, often referred to as rTEV, is produced in Escherichia coli (E. coli) and has become an invaluable tool in protein purification and structural biology.

Structure and Specificity

TEV protease is a 27 kDa enzyme that recognizes a specific seven-amino-acid sequence: Glu-Asn-Leu-Tyr-Phe-Gln-Gly. The cleavage occurs between the Gln and Gly residues . This high specificity makes TEV protease an excellent choice for removing affinity tags from fusion proteins without affecting the target protein.

Production and Mutations

Recombinant TEV protease is produced in E. coli and purified using affinity chromatography. However, the wild-type TEV protease has some limitations, such as low solubility, auto-proteolysis, and instability. To address these issues, researchers have introduced several point mutations to improve its stability and solubility . For example, a mutant called TEVp7M, which incorporates seven changes, has shown remarkable purification yields and improved thermal stability .

Applications

TEV protease is extensively used in various biotechnological applications, including:

  • Protein Purification: Removal of affinity tags from fusion proteins to obtain pure target proteins.
  • Structural Biology: Cleavage of fusion proteins to study the structure and function of individual protein domains.
  • Directed Evolution: Optimization of TEV protease variants for improved catalytic efficiency and stability .
Advances and Future Directions

Recent advances in directed evolution have further enhanced the catalytic efficiency of TEV protease. Researchers have developed yeast-based platforms to evolve high-turnover, low-affinity proteases, resulting in variants with improved performance in both yeast and mammalian cells . These advancements hold promise for expanding the utility of TEV protease in various biotechnological and therapeutic applications.

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *

Category

Service

THE BIOTEK
THE BioTek is a global biotech company offering highly purified proteins for research in cancer, apoptosis, development, endocrinology, immunology, neuroscience, proteases, and stem cells.
  • Contact
  • Address: 1925 E Maple Ave, El Segundo, CA 90245 United States
  • Phone : +1 201-285-7826
  • Email : info@thebiotek.com
  • Hours : Mon.-Fri. 9:00 AM - 5:00 PM
© Copyright 2024 Thebiotek. All Rights Reserved.