2'/3'-O-(N-Methyl-anthraniloyl)-adenosine-5'-[(β,γ )-imido] triphosphate,Triethylammonium salt
For research use only!
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: 6 months after date of delivery
Molecular Formula: C18H24N7O13P3 (free acid)
Molecular Weight: 639.35 g/mol (free acid)
Exact Mass: 639.06 g/mol (free acid)
Purity: ≥ 90 % (HPLC)
Form: solution in water
Color: colorless to slightly yellow
Concentration: 10 mM - 11 mM
pH: 7.5 ±0.5
Spectroscopic Properties: λmax 255/355 nm, ε 23.3/5.8 L mmol-1 cm-1 (Tris-HCl pH 7.5), λexc 355 nm, λem 448 nm
Fluorescence stop-flow kinetics: helicase DnaB protein
Displacement studies on TRP-MET-tyrosine kinase
Nucleotide specific binding to membrane protein FeoB
Inhibition of adenylyl cyclase
X-ray studies of kinesin motors
Agonistic ligand, mainly for nucleoside receptor A1
Nucleosidephosphates stabilized against hydrolytic degradation can directly bind to nucleoside receptors.
ATP-binding sites of serine protease
Please click the black arrow on the right to expand the citation list. Click publication title for the full text.
 Bujalowski et al. (2000) Kinetic mechanism of nucleotide cofactor binding to Escherichia coli replicative helicase DnaB protein. Stopped-flow kinetic studies using fluorescent, ribose-, and base-modified nucleotide analogues. Biochemistry 39:2106.
 Hays et al. (2003) Oligomerization-induced modulation of TRP-MET tyrosine kinase activity. J. Biol. Chem. 278:27456.
 Marlovits et al. (2002) The membrane protein FeoB contains an intramolecular G protein essential for Fe (II) uptake in bacteria. PNAS USA 99:16243.
 Wang et al. (2007) A conformational transition in the adenylyl cyclase catalytic site yields different binding modes for ribosyl-modified and unmodified nucleotide inhibitors. Bioorg. Med. Chem. 15:2993.
 Bodey et al. (2009) 9-Angström structure of a microtubule-bound mitotic motor. J. Mol. Biol. 388 (2):218.
 Vineyard et al. (2006) 1. Transient kinetic experiments demonstrate the existence of a unique catalytic enzyme form in the peptide-stimulated ATPase mechanism of Escherichia coli Lon protease. Biochemistry 45:11432.
 Rosenfeld et al. (1994) Structural and kinetic studies of the 10 S<==>6 S transition in smooth muscle myosin. J. Biol. Chem. 269:30187.
Jezewska et al. (1996) Interactions of Escherichia coli primary replicative helicase DnaB protein with nucleotide cofactors. Biophys. J. 71:2075.
Moore et al. (1994) Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer. 1. Use of fluorescent nucleotide analogues. Biochemistry 33:14550.
Williams et al. (1986) Effects of purine nucleotides on the binding of [3H]cyclopentyladenosine to adenosine A1-receptors in rat brain membranes. J. Neurochem. 47 (1):88.