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Citations & References (6)
Invitrogen™
AcTEV™ Protease
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 removingRead more
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| Catalog Number | Quantity |
|---|---|
| 12575015 | 1000 U |
| 12575023 | 10,000 U |
Catalog number 12575015
Price (JPY)Contact Us ›
55,600
Each
Quantity:
1000 U
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. 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 features:
• Highly specific cleavage activity
• Enhanced enzyme stability for prolonged protease activity (see figure)
• 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 nonspecific protease contamination
Applications
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 hr 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 hr at 30°C. AcTEV™ Protease is functionally tested for the absence of any nonspecific protease activity.
• Highly specific cleavage activity
• Enhanced enzyme stability for prolonged protease activity (see figure)
• 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 nonspecific protease contamination
Applications
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 hr 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 hr at 30°C. AcTEV™ Protease is functionally tested for the absence of any nonspecific protease activity.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Compatible BufferTEV Buffer
Product TypeProtease
Quantity1000 U
Shipping ConditionDry Ice
Concentration1,000 Units
EnzymeTEV Protease
Optimal Reaction Temperature+4°C to +30°C
Product LineAcTEV
Unit SizeEach
Contents & Storage
AcTEV™ Protease is supplied with a vial of 20X TEV buffer [1 M Tris-HCl (pH 8.0), 10 mM EDTA] and a vial of 100 mM DTT.
Store at -20° C. Guaranteed stable for 1 year when properly stored.
Store at -20° C. Guaranteed stable for 1 year when properly stored.
Frequently asked questions (FAQs)
Why does AcTEV Protease require DTT?
What is the cleavage recognition site for AcTEV Protease?
What products do you offer for enzymatic cleavage of fusion tags from recombinant proteins?
Citations & References (6)
Citations & References
Abstract
Structure and function of an irreversible agonist-ß(2) adrenoceptor complex.
Journal:Nature
PubMed ID:21228876
'G-protein-coupled receptors (GPCRs) are eukaryotic integral membrane proteins that modulate biological function by initiating cellular signalling in response to chemically diverse agonists. Despite recent progress in the structural biology of GPCRs, the molecular basis for agonist binding and allosteric modulation of these proteins is poorly understood. Structural knowledge of agonist-bound
Quantitative reactivity profiling predicts functional cysteines in proteomes.
Journal:Nature
PubMed ID:21085121
'Cysteine is the most intrinsically nucleophilic amino acid in proteins, where its reactivity is tuned to perform diverse biochemical functions. The absence of a consensus sequence that defines functional cysteines in proteins has hindered their discovery and characterization. Here we describe a proteomics method to profile quantitatively the intrinsic reactivity
Widespread bidirectional promoters are the major source of cryptic transcripts in yeast.
Journal:Nature
PubMed ID:19169244
'Pervasive and hidden transcription is widespread in eukaryotes, but its global level, the mechanisms from which it originates and its functional significance are unclear. Cryptic unstable transcripts (CUTs) were recently described as a principal class of RNA polymerase II transcripts in Saccharomyces cerevisiae. These transcripts are targeted for degradation immediately
Non-muscle myosin IIA is a functional entry receptor for herpes simplex virus-1.
Journal:Nature
PubMed ID:20944748
Herpes simplex virus-1 (HSV-1), the prototype of the a-herpesvirus family, causes life-long infections in humans. Although generally associated with various mucocutaneous diseases, HSV-1 is also involved in lethal encephalitis. HSV-1 entry into host cells requires cellular receptors for both envelope glycoproteins B (gB) and D (gD). However, the gB receptors
Hexameric assembly of the proteasomal ATPases is templated through their C termini.
Journal:Nature
PubMed ID:19412160
Substrates of the proteasome are recognized and unfolded by the regulatory particle, and then translocated into the core particle (CP) to be degraded. A hetero-hexameric ATPase ring, containing subunits Rpt1-6, is situated within the base subassembly of the regulatory particle. The ATPase ring sits atop the CP, with the Rpt