AcTEV™ Protease is an improved version of Tobacco Etch Virus (TEV) protease that is highly site-specific, highly active, and significantly more stable than native TEV protease, resulting in enhanced long-term activity. AcTEV™ Protease specifically recognizes a seven amino acid sequence (Glu-Asn-Leu-Tyr-Phe-Gln-Gly, cleaving between Gln and Gly), making it useful for removing affinity tags from fusion proteins (1,2). AcTEV™ Protease features:
- Highly specific cleavage activity
- Enhanced enzyme stability for prolonged protease activity (Figure 1)
- Activity over a broad temperature (+4°C to 30°C) and pH (6.0 to 8.5) range
- Six-histidine sequence to facilitate its removal from the digested protein sample
- Greater than 85% single-band purity with no non-specific protease contamination
Incubation with AcTEV™ Protease releases the protein of interest from the fusion tag. This is an effective way to remove solubility, secretion, detection, and purification tags from recombinant proteins.Enzyme Specifications: Purified from E. coli
expressing the AcTEV™ Protease gene. Unit Definition: One unit of AcTEV™ Protease cleaves 85% of a 3 µg control substrate in 1 h at 30°C. Unit Reaction Conditions: 50 mM Tris-HCl (pH 8.0), 0.5 mM EDTA, 1 mM DTT, 3 µg control substrate, and 1 unit enzyme in 30 µl for 1 h at 30°C. AcTEV™ Protease is functionally tested for the absence of any non-specific protease activity.