Alexa Fluor® 647 adenosina 5´trifosfato (Alexa Fluor® 647 ATP) es un isómero mixto compuesto por el fluoróforo Alexa Fluor® 647,Más información
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Número de catálogo
Cantidad
A22362
también denominado A-22362
100 μl
Número de catálogo A22362
también denominado A-22362
Precio (MXN)
-
Cantidad:
100 μl
Alexa Fluor® 647 adenosina 5´trifosfato (Alexa Fluor® 647 ATP) es un isómero mixto compuesto por el fluoróforo Alexa Fluor® 647, un colorante fluorescente rojo lejano excepcionalmente brillante conectado a la posición 2´ o 3´ del anillo de ribosa a través de un enlazador aminoetilcarbamoil.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Etiqueta o tinteAlexa Fluor™ 647
Tipo de productoATP 647
Cantidad100 μl
Condiciones de envíoHielo húmedo
Concentración5 mM
Línea de productosAlexa Fluor
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador de -5 °C a -30 °C y proteger de la luz.
Citations & References (9)
Citations & References
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