γ-(6-Aminohexyl)-ATP-ATTO-488
excitation and emission spectrum of ATTO 488
For research use only.
Please centrifuge briefly before opening (volume ≤2 ml).
Shipping: shipped on gel packs
Storage Conditions: store at -20 °C
Short term exposure (up to 1 week cumulative) to ambient temperature possible.
Shelf Life: 12 months after date of delivery
Molecular Formula: C41H50N9O22P3S2 (free acid)
Molecular Weight: 1177.93 g/mol (free acid)
Exact Mass: 1177.17 g/mol (free acid)
Purity: ≥ 95 % (HPLC)
Form: solution in water
Color: yellow
Concentration: 1.0 mM - 1.1 mM
pH: 7.5 ±0.5
Spectroscopic Properties: λexc 500 nm, λem 520 nm, ε 90.0 L mmol-1 cm-1 (Tris-HCl pH 7.5)
Selected References:
Biniuri et al. (2018) Probing ATP/ATP-Aptamer or ATP-Aptamer Mutant Complexes by Microscale Thermophoresis and Molecular Dynamics Simulations: Discovery of an ATP-Aptamer Sequence of Superior Binding Properties. J. Phys. Chem. B. 122 (39):9102.
Hammler et al. (2018) Fluorescence-Lifetime-Sensitive Probes for Monitoring ATP Cleavage. Chemistry 24 (57):15329.
Tran Van Nhieu et al. (2013) Actin-based confinement of calcium responses during Shigella invasion. Nat. Commun. 4:1567.
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Scientific citations for Jena Bioscience nu-833-488
2 scientific citations and 0 citation images found by Bioz.
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Redox-Switchable Binding Properties of the ATP-Aptamer.
Journal of the American Chemical Society, 2020-10-08 · PMID:31478647
.. covering a concentration range between 100 μM to 3 nM of the aptamer. ... To 10 μl of each of the serial dilutions, 10 μl of 400 nM stock of
ATTO-488 functionalized ATP (γ-(6-Aminohexyl)-ATP-ATTO-488, (Jena Bioscience GmbH , Jena, Germany) were added and allowed to incubate for 10 minutes at room temperature.. Subsequently, each sample was loaded onto a Nanotemper (Munich, Germany) KM-022 capillary tube and .. -
Probing ATP/ATP-Aptamer or ATP-Aptamer Mutant Complexes by Microscale Thermophoresis and Molecular Dynamics Simulations: Discovery of an ATP-Aptamer Sequence of Superior Binding Properties.
The Journal of Physical Chemistry B, 2019-10-21 · PMID:30188731
Abstract: Microscale thermophoresis (MST) is used to follow the dissociation constants corresponding to ATTO 488-labeled adenosine triphosphate (ATP) and the ATP-aptamer or ATP-aptamer mutants that include two binding sites for the ATP ligand. A set of eight ATP-aptamer mutants, where the thymidine bases, within the reported ATP binding aptamer sites, are substituted with cytosine bases, are examined. The MST-derived dissociation constant of ATP to the reported aptamer is K d = 31 ± 3 μM, whereas most of the aptamer mutants show lower affinity (higher K d values) toward the ATP ligand
