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2'/3'-O-(N-Methyl-anthraniloyl)-adenosine-5'-[(β,γ)-imido]-triphosphate, Triethylammonium salt

Cat. No. Amount Price (EUR) Buy / Note
NU-214S 10 μl (10 mM)165,50 Add to Basket/Quote Add to Notepad
NU-214L 5 x 10 μl (10 mM)484,70 Add to Basket/Quote Add to Notepad
Structural formula of Mant-AppNHp ((Mant-AMPPNP), 2'/3'-O-(N-Methyl-anthraniloyl)-adenosine-5'-[(β,γ)-imido]-triphosphate, Triethylammonium salt)
Structural formula of Mant-AppNHp

For general laboratory use.

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)

CAS#: 85287-56-6

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[1]
Displacement studies on TRP-MET-tyrosine kinase[2]
Nucleotide specific binding to membrane protein FeoB[3]
Inhibition of adenylyl cyclase[4]
X-ray studies of kinesin motors[5]
Agonistic ligand, mainly for nucleoside receptor A1
Nucleosidephosphates stabilized against hydrolytic degradation can directly bind to nucleoside receptors.

Specific Ligands:

ATP-binding sites of serine protease[6]


BIOZ Product Citations:

Selected References:
[1] 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.
[2] Hays et al. (2003) Oligomerization-induced modulation of TRP-MET tyrosine kinase activity. J. Biol. Chem. 278:27456.
[3] Marlovits et al. (2002) The membrane protein FeoB contains an intramolecular G protein essential for Fe (II) uptake in bacteria. PNAS USA 99:16243.
[4] 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.
[5] Bodey et al. (2009) 9-Angström structure of a microtubule-bound mitotic motor. J. Mol. Biol. 388 (2):218.
[6] 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.
[7] 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.