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Adenosine-5'-[(β,γ)-imido]triphosphate, Tetralithium salt


Cat. No. Amount Price (EUR) Buy / Note
NU-407-10 10 mg104,40 Add to Basket/Quote Add to Notepad
NU-407-50 50 mg350,50 Add to Basket/Quote Add to Notepad
Structural formula of AppNHp ((AMPPNP), Adenosine-5'-[(β,γ)-imido]triphosphate, Tetralithium salt)
Structural formula of AppNHp

For general laboratory use.

Shipping: shipped on dry ice

Storage Conditions: store at -20 °C

Shelf Life: 6 months after date of delivery

Molecular Formula: C10H17N6O12P3 (free acid)

Molecular Weight: 506.19 g/mol (free acid)

Exact Mass: 506.01 g/mol (free acid)

CAS#: 72957-42-7

Purity: ≥ 95 % (HPLC)

Form: solid

Color: white to off-white

Spectroscopic Properties: λmax 259 nm, ε 15.4 L mmol-1 cm-1 (Tris-HCl pH 7.5)

X-ray analysis[1, 2]
Hydrolyse studies[3, 4]Agonistic ligand, mainly for nucleoside receptor A1
Nucleosidephosphates stabilized against hydrolytic degradation can directly bind to nucleoside receptors.

Specific Ligands:

Thymidylate kinase[1, 2]

for P2Y2 receptor[5]

Please note: For reasons of stability, please make sure that the pH value of a solution of this product never drops below 7.0. This can be achieved by dissolving the nucleotide in a buffer of your choice (50 - 100 mM, pH 7 - 10). Dissolve and adjust concentration photometrically.
When stored at -20 °C, product may hydrolyze, thereby forming AppNH2 at a rate of up to 1 % per month!

BIOZ Product Citations:

Selected References:
[1] Segura-Pena et al. (2007) Quartenary structure change as a mechanism for the regulation of thymidine kinase 1-like enzymes. Structure 15:1555.
[2] Ostermann et al. (2003) Structure of human thhymidilate kinase in complex with prodrugs:Implications for the structure-based design of novel compounds. Biochemistry 42:2568.
[3] Shimizu et al. (1997) Hydrolysis of AMPPNP by the motor domain of NCD, a kinesin-related protein. Mol. Biol. Cell 8:1497.
[4] Suzuki et al. (1997) Hydrolysis of AMPPNP by the motor domain of ncd, a kinesin-related protein. FEBS Lett. 409 (1):29.
[5] Lazarowski et al. (1995) Pharmacological selectivity of cloned human P2U-purinoreceptor: potent activation by diadenosine tetraphosphate. Br. J. Pharmacol. 116 (1):1619.
Bodey et al. (2009) 9-Angström structure of a microtubule-bound mitotic motor. J. Mol. Biol. 388 (2):218.
Karow et al. (2009) A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN. Nucleic Acids Research 37 (13):4464.
Chang et al. (2005) Nitric Oxide-dependent Allosteric Inhibitory Role of a Second Nucleotide Binding Site in Soluble Guanylyl Cyclase. J. Biol. Chem. 280 (12):11513.
Menendez-Arias et al. (2005) Supression of Multidrug-resistant HIV-1 Reverse Transscriptase Primer Unblocking Activity by a-Phosphate-modified Thymidine Analogues. J. Mol. Biol. 349 (3):451.
Menz et al. (2001) The structure and nucleotide occupancy of bovine mitochondrial F-1-ATPase are not influenced by crystallisation at high concentrations of nucleotide. FEBS Lett. 494 (1):11.
Tereshko et al. (2001) Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression. Nat. Struct. Biol. 8 (10):899.
Prodromou et al. (2000) The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains. EMBO J. 19 (16):4383.
Gil et al. (1999) N-Acetyl-L-glutamate kinase from Escherichia coli: cloning of the gene, purification and crystallization of the recombinant enzyme and preliminary X-ray analysis of the free and ligand-bound forms. Acta Cryst. D 55:1350.
Shi et al. (1999) EDC cross-linking of actin and myosin S1. II. AMPPNP induces an allosteric transition from pre-hydrolysis state to posthydrolysis state. Biophys. J. 76 (1):A163.
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.