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Citations & References (9)
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, anRead more
| Catalog Number | Quantity |
|---|---|
| A22362 also known as A-22362 | 100 μL |
Catalog number A22362
also known as A-22362
Price (CNY)
6,549.00
Each
Quantity:
100 μL
Price (CNY)
6,549.00
Each
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.
Specifications
Label or DyeAlexa Fluor™ 647
Product Type647 ATP
Quantity100 μL
Shipping ConditionWet Ice
Concentration5 mM
Product LineAlexa Fluor
Unit SizeEach
Contents & Storage
Store in freezer -5°C to -30°C and protect from light.
Citations & References (9)
Citations & References
Abstract
Effects of surface adsorption on catalytic activity of heavy meromyosin studied using a fluorescent ATP analogue.
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
Correlation between mechanical and enzymatic events in contracting skeletal muscle fiber.
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
Fluorescence measurements of nucleotide association with the Na(+)/K(+)-ATPase.
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
Simultaneous measurement of rotations of myosin, actin and ADP in a contracting skeletal muscle fiber.
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
Anisotropic diffusion of fluorescently labeled ATP in rat cardiomyocytes determined by raster image correlation spectroscopy.
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