AcTEV™ Protease
AcTEV™ Protease
인용 및 참조 문헌 (6)
Invitrogen™

AcTEV™ Protease

AcTEV™ Protease는 Tobacco Etch Virus (TEV) protease의 개선된 버전으로 원래 TEV protease 보다 영역 특이성, 활성, 안정성이 높아 개선된 장기자세히 알아보기
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카탈로그 번호수량
1257502310,000 U
125750151000 U
카탈로그 번호 12575023
제품 가격(KRW)
3,093,000
Online offer
Ends: 31-Dec-2025
3,638,000
할인액 545,000 (15%)
Each
카트에 추가하기
수량:
10,000 U
제품 가격(KRW)
3,093,000
Online offer
Ends: 31-Dec-2025
3,638,000
할인액 545,000 (15%)
Each
카트에 추가하기
AcTEV™ Protease는 Tobacco Etch Virus (TEV) protease의 개선된 버전으로 원래 TEV protease 보다 영역 특이성, 활성, 안정성이 높아 개선된 장기 활성을 제공합니다. AcTEV™ Protease는 7개 아미노산 서열(Glu-Asn-Leu-Tyr-Phe-Gln-Gly, Gln과 Gly 사이 절단)을 특이적으로 인식하여 fusion proteins에서 친화도 태그를 제거하는 데 유용합니다(1,2). AcTEV™ Protease의 특징:

• 특이성 높은 절단 활성을 가짐

• protease 활성 연장으로 효소 안정성이 강화됨(그림 1)

• 폭넓은 온도 범위(+4°C ∼ 30°C) 및 pH (6.0 ∼ 8.5)에서 활성됨

• 6-histidine sequence로 digested protein 샘플에서 제거가 용이함

• 비특이적 protease 오염이 없고 single-band 순도가 85% 이상임

어플리케이션: AcTEV™ Protease로 배양하면 fusion tag에서 관심 단백질이 분리됩니다. 이는 재조합 단백질에서 용해성, 분비, 검출, 순도 태그를 제거하는 효율적인 방법입니다.
Enzyme 상세: AcTEV™ Protease gene을 발현하는 E. coli 에서 정제함. 단위 정의: AcTEV™ Protease 한 단위는 30°C에서 1시간 동안 대조 기질 3 μg을 85% 절단합니다. 단위 반응 조건: 50 mM Tris-HCl (pH 8.0), 0.5 mM EDTA, 1 mM DTT, 3 μg control substrate, 1 unit enzyme- 30 μl, 30°C에서 1시간. AcTEV™ Protease에는 비특이적 protease 활성 부정시험을 실시합니다.
For Research Use Only. Not for use in diagnostic procedures.
사양
함께 사용가능한 버퍼TEV Buffer
제품 유형Protease
수량10,000 U
배송 조건Dry Ice
농도1,000 Units
효소TEV Protease
최적 반응 온도+4°C to +30°C
제품라인AcTEV
Unit SizeEach
구성 및 보관
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.

자주 묻는 질문(FAQ)

Why does AcTEV Protease require DTT?

A final concentration of 1 mM DTT is required for the AcTEV protease reaction. The DTT serves as a stabilizer of secondary structure, i.e., it ensures that the enzyme does not undergo oxidation. If you are unable to use DTT due to a column purification after digestion, you can leave it out and still see a successful AcTEV digestion, however we recommend using it.

No rigorous quantitative data for activity in the absence of DTT and EDTA has been collected in-house. Incubations using reaction buffer +/-DTT and +/- EDTA; have been performed, but the products were analyzed only at t=0 and t=2 hr at 30 degrees C. No difference in the amount of product generated +/-DTT or +/-EDTA was noticed, but it is possible that the detailed kinetics in a time course reaction may be a little different.

What is the cleavage recognition site for AcTEV Protease?

The recognition site for AcTEV Protease is ENLYFQS/G

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

What products do you offer for enzymatic cleavage of fusion tags from recombinant proteins?

We offer the following products:

-AcTEV Protease (Cat. Nos. 12575015, 12575023)
-EKMax Enterokinase (Cat. Nos. E18001, E18002)
-SUMO Protease (Cat. No. 12588018)


Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

인용 및 참조 문헌 (6)

인용 및 참조 문헌
Abstract
Structure and function of an irreversible agonist-ß(2) adrenoceptor complex.
Authors:Rosenbaum DM, Zhang C, Lyons JA, Holl R, Aragao D, Arlow DH, Rasmussen SG, Choi HJ, Devree BT, Sunahara RK, Chae PS, Gellman SH, Dror RO, Shaw DE, Weis WI, Caffrey M, Gmeiner P, Kobilka BK,
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 ... More
Quantitative reactivity profiling predicts functional cysteines in proteomes.
Authors:Weerapana E, Wang C, Simon GM, Richter F, Khare S, Dillon MB, Bachovchin DA, Mowen K, Baker D, Cravatt BF,
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 ... More
Widespread bidirectional promoters are the major source of cryptic transcripts in yeast.
Authors:Neil H, Malabat C, d'Aubenton-Carafa Y, Xu Z, Steinmetz LM, Jacquier A,
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 ... More
Non-muscle myosin IIA is a functional entry receptor for herpes simplex virus-1.
Authors:Arii J, Goto H, Suenaga T, Oyama M, Kozuka-Hata H, Imai T, Minowa A, Akashi H, Arase H, Kawaoka Y, Kawaguchi Y,
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 ... More
Hexameric assembly of the proteasomal ATPases is templated through their C termini.
Authors:Park S, Roelofs J, Kim W, Robert J, Schmidt M, Gygi SP, Finley D,
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 ... More
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