Alexa Fluor® 647 Adenosin-5´-triphosphat (Alexa Fluor® 647 ATP) ist ein Misch-Isomer, das aus dem Alexa Fluor® 647 Fluorophor besteht, einemWeitere Informationen
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Katalognummer
Menge
A22362
auch als A-22362 bezeichnet
100 μl
Katalognummer A22362
auch als A-22362 bezeichnet
Preis (EUR)
752,00
Each
Menge:
100 μl
Preis (EUR)
752,00
Each
Alexa Fluor® 647 Adenosin-5´-triphosphat (Alexa Fluor® 647 ATP) ist ein Misch-Isomer, das aus dem Alexa Fluor® 647 Fluorophor besteht, einem außergewöhnlich hellen, fernrot fluoreszierenden Farbstoff, der über einen Aminoethylcarbamoyl-Linker an die 2´- oder 3´-Position des Riboserings gebunden ist.
Nur für Forschungszwecke. Darf nicht für diagnostische Verfahren eingesetzt werden.
Specifications
Marker oder FarbstoffAlexa Fluor™ 647
Produkttyp647 ATP
Menge100 μl
VersandbedingungNasses Eis, Nasseis
Konzentration5 mM
ProduktlinieAlexa Fluor
Unit SizeEach
Inhalt und Lagerung
In einem Tiefkühlgerät (-5 bis -30 °C) lagern und vor Licht schützen.
Zitierungen und Referenzen (9)
Zitierungen und Referenzen
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