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Roche

AMP-PNP

Adenylyl-imidodiphosphate

Synonym(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

Empirical Formula (Hill Notation):
C10H17N6O12P3 · xLi+ · yH2O
CAS Number:
Molecular Weight:
506.20 (free acid basis)
Beilstein:
6047109
UNSPSC Code:
12352204

Quality Level

form

powder

mol wt

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

packaging

pkg of 25 mg

manufacturer/tradename

Roche

SMILES string

[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

InChI key

PVKSNHVPLWYQGJ-KQYNXXCUSA-N

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General description

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.

Features and Benefits

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

Quality

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

Storage and Stability

Store at -15–-25 °C. (Store dry!)

Other Notes

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
S T Brady
Nature, 317(6032), 73-75 (1985-09-05)
Identification of the ATPase involved in fast axonal transport of membranous organelles has proven difficult. Myosin and dynein, other ATPases known to be involved in cell motility, have properties that are inconsistent with the established properties of fast axonal transport
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
Laurel M Pegram et al.
Proceedings of the National Academy of Sciences of the United States of America, 116(31), 15463-15468 (2019-07-18)
Conformational selection by small molecules expands inhibitory possibilities for protein kinases. Nuclear magnetic resonance (NMR) measurements of the mitogen-activated protein (MAP) kinase ERK2 have shown that activation by dual phosphorylation induces global motions involving exchange between two states, L and

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