Alexa Fluor™ 647 ATP (Adenosine 5'-Triphosphate, Alexa Fluor™ 647 2'-(or-3')-O-(N-(2-Aminoethyl) Urethane), Hexa(Triethylammonium) Salt)
Alexa Fluor&trade; 647 ATP (Adenosine 5'-Triphosphate, Alexa Fluor&trade; 647 2'-(or-3')-<i>O</i>-(<i>N</i>-(2-Aminoethyl) Urethane), Hexa(Triethylammonium) Salt)
Invitrogen™

Alexa Fluor™ 647 ATP (Adenosine 5'-Triphosphate, Alexa Fluor™ 647 2'-(or-3')-O-(N-(2-Aminoethyl) Urethane), Hexa(Triethylammonium) Salt)

Alexa Fluor® 647 adenosine 5´triphosphate (Alexa Fluor® 647 ATP) is a mixed-isomer comprised of the Alexa Fluor® 647 fluorophore, an자세히 알아보기
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카탈로그 번호수량
A22362
A-22362으로도 사용됨
100 μL
카탈로그 번호 A22362
A-22362으로도 사용됨
제품 가격(KRW)
634,000
온라인 행사
Ends: 31-Mar-2026
745,000
할인액 111,000 (15%)
Each
카트에 추가하기
수량:
100 μL
제품 가격(KRW)
634,000
온라인 행사
Ends: 31-Mar-2026
745,000
할인액 111,000 (15%)
Each
카트에 추가하기
Alexa Fluor® 647 adenosine 5´triphosphate (Alexa Fluor® 647 ATP) is a mixed-isomer comprised of the Alexa Fluor® 647 fluorophore, an exceptionally bright far-red fluorescent dye attached to the 2´ or 3´ position of the ribose ring via an aminoethylcarbamoyl linker.
For Research Use Only. Not for use in diagnostic procedures.
사양
라벨 또는 염료Alexa Fluor™ 647
제품 유형647 ATP
수량100 μL
배송 조건Wet Ice
농도5 mM
제품라인Alexa Fluor
Unit SizeEach
구성 및 보관
Store in freezer -5°C to -30°C and protect from light.

인용 및 참조 문헌 (9)

인용 및 참조 문헌
Abstract
Effects of surface adsorption on catalytic activity of heavy meromyosin studied using a fluorescent ATP analogue.
Authors:Balaz M, Sundberg M, Persson M, Kvassman J, Månsson A
Journal:Biochemistry
PubMed ID:17523677
'Biochemical studies in solution and with myosin motor fragments adsorbed to surfaces (in vitro motility assays) are invaluable for elucidation of actomyosin function. However, there is limited understanding of how surface adsorption affects motor properties, e.g., catalytic activity. Here we address this issue by comparing the catalytic activity of heavy ... More
Correlation between mechanical and enzymatic events in contracting skeletal muscle fiber.
Authors:Shepard A, Borejdo J
Journal:Biochemistry
PubMed ID:15005615
'The conventional hypothesis of muscle contraction postulates that the interaction between actin and myosin involves tight coupling between the power stroke and hydrolysis of ATP. However, some in vitro experiments suggested that hydrolysis of a single molecule of ATP caused multiple mechanical cycles. To test whether the tight coupling is ... More
Fluorescence measurements of nucleotide association with the Na(+)/K(+)-ATPase.
Authors:Pratap PR, Mikhaylyants LO, Olden-Stahl N,
Journal:Biochim Biophys Acta
PubMed ID:19595797
'The Na(+)/K(+)-ATPase, a membrane-associated ion pump, uses energy from the hydrolysis of ATP to pump 3 Na(+) ions out of and 2 K(+) into cells. The dependence of ATP hydrolysis on ATP concentration was measured using a fluorescence coupled-enzyme assay. The dependence on concentration of nucleotide association with the ATPase ... More
Simultaneous measurement of rotations of myosin, actin and ADP in a contracting skeletal muscle fiber.
Authors:Shepard AA, Dumka D, Akopova I, Talent J, Borejdo J
Journal:J Muscle Res Cell Motil
PubMed ID:15711885
'The rotation of myosin heads and actin were measured simultaneously with an indicator of the enzymatic activity of myosin. To minimize complications due to averaging of signals from many molecules, the signal was measured in a small population residing in a femtoliter volume of a muscle fiber. The onset of ... More
Anisotropic diffusion of fluorescently labeled ATP in rat cardiomyocytes determined by raster image correlation spectroscopy.
Authors:Vendelin M, Birkedal R,
Journal:Am J Physiol Cell Physiol
PubMed ID:18815224
A series of experimental data points to the existence of profound diffusion restrictions of ADP/ATP in rat cardiomyocytes. This assumption is required to explain the measurements of kinetics of respiration, sarcoplasmic reticulum loading with calcium, and kinetics of ATP-sensitive potassium channels. To be able to analyze and estimate the role ... More