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Key Documents

10102547001

Roche

AMP-PNP

Adenylyl-imidodiphosphate

Synonyme(s) :

Adenosine 5′-(β,γ-imido)triphosphate lithium salt hydrate, β,γ-Imidoadenosine 5′-triphosphate lithium salt hydrate, AMP-PNP, ATP[β,γ-NH], Adenylyl imidodiphosphate lithium salt hydrate, App(NH)p

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About This Item

Formule empirique (notation de Hill):
C10H17N6O12P3 · xLi+ · yH2O
Numéro CAS:
Poids moléculaire :
506.20 (free acid basis)
Numéro Beilstein :
6047109
Code UNSPSC :
12352204

Niveau de qualité

Forme

powder

Poids mol.

Mr 506.2 (ANP-PNP)
Mr 529.9 (AMP-PNP-Li4)

Conditionnement

pkg of 25 mg

Fabricant/nom de marque

Roche

Chaîne SMILES 

[Li+].[Li+].[Li+].[Li+].[H]O[H].Nc1ncnc2n(cnc12)[C@@H]3O[C@H](COP([O-])(=O)OP([O-])(=O)NP([O-])([O-])=O)[C@@H](O)[C@H]3O

InChI

1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1

Clé InChI

PVKSNHVPLWYQGJ-KQYNXXCUSA-N

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Catégories apparentées

Description générale

AMP-PNP (adenylyl-imidodiphosphate) is a non-hydrolysable analogue of ATP. It inhibits fast axonal transport and facilitates the interaction between membranous organelles and microtubules.
AMP-PNP(adenylyl-imidodiphosphate) is an artificial substrate of enzyme, adenylate cyclase. Adenylate cyclase helps to hydrolyze adenylyl-imidodiphosphate slowly than ATP.

Application

AMP-PNP has been used in the preparation of nucleotide solutions, two-motor fluorescence assay, preparation of flow-cells with kinesin and cascade binding assays.
AMP-PNP is a competitive inhibitor of most ATP-dependent systems. A good substrate for enzymes hydrolyzing between the α- and β-phosphorus atom, yet is resistant to enzymes cleaving between the β- and γ-phosphorus atom. Substrate of snake venom phosphodiesterase and adenylate cyclase.
AMP-PNP has been used for two-motor fluorescence assay.

Caractéristiques et avantages

Contents
88% AMP-PNP (from N), 4.5% lithium, 6% water

Qualité

Contaminants: ≤1.5% Pi , <0.1% ATP (enzymatically)

Stockage et stabilité

Store at -15–-25 °C. (Store dry!)

Autres remarques

For life science research only. Not for use in diagnostic procedures.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Cristina Olivieri et al.
eLife, 9 (2020-04-28)
In the nucleus, the spatiotemporal regulation of the catalytic subunit of cAMP-dependent protein kinase A (PKA-C) is orchestrated by an intrinsically disordered protein kinase inhibitor, PKI, which recruits the CRM1/RanGTP nuclear exporting complex. How the PKA-C/PKI complex assembles and recognizes
Arthur Chow et al.
Methods in enzymology, 667, 365-402 (2022-05-08)
Pseudokinases often operate through functionally related enzymes and receptors. A prime example is the pseudokinase KSR (Kinase Suppressor of RAS), which can act as both an amplifier and inhibitor of members in the RAS-MAPK (Mitogen Activated Protein Kinase) signaling pathway.
Maximilian M Biebl et al.
Nature communications, 12(1), 828-828 (2021-02-07)
The co-chaperone p23 is a central part of the Hsp90 machinery. It stabilizes the closed conformation of Hsp90, inhibits its ATPase and is important for client maturation. Yet, how this is achieved has remained enigmatic. Here, we show that a
Luke A Yates et al.
Structure (London, England : 1993), 28(1), 96-104 (2019-11-20)
Yeast Tel1 and its highly conserved human ortholog ataxia-telangiectasia mutated (ATM) are large protein kinases central to the maintenance of genome integrity. Mutations in ATM are found in ataxia-telangiectasia (A-T) patients and ATM is one of the most frequently mutated
Nucleotide dependence of the dimerization of ATP binding cassette nucleotide binding domains
Fendley GA, et al.
Biochemical and Biophysical Research Communications, 480(2), 268-272 (2016)

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