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AppCp

(AMPPCP)

Adenosine-5'-[(β,γ)-methyleno]triphosphate, Sodium salt

Cat. No. Amount Price (EUR) Buy / Note
NU-422-10 10 mg69,30 Add to Basket/Quote Add to Notepad
NU-422-25 25 mg141,00 Add to Basket/Quote Add to Notepad
Structural formula of AppCp ((AMPPCP), Adenosine-5'-[(β,γ)-methyleno]triphosphate, Sodium salt)
Structural formula of AppCp

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: 12 months after date of delivery

Molecular Formula: C11H18N5O12P3 (free acid)

Molecular Weight: 505.21 g/mol (free acid)

Exact Mass: 505.02 g/mol (free acid)

CAS#: 7414-56-4

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)

Applications:
Conformational studies on complex with mevalonate diphosphate decarboxylase[1]
Structure of the complex with folylpolyglutamate synthetase[2]
Structure of complex with p90 ribosomal S6 kinases[3]
Crystal structure of complex with Ca2+-ATPase[4]
NMR-studies of complex with yeast hexokinase[5]
Agonistic ligand, mainly for nucleoside receptor A1
Nucleosidephosphates stabilized against hydrolytic degradation can directly bind to nucleoside receptors.

Specific Ligands:

Tubulin[6]

Nonhydrolyzable ligand for P2X purinoreceptor[7,8]

BIOZ Product Citations:

Selected References:
[1] Reuther et al. (2011) Backbone 1H, 13C, 15N NMR assignments of the unliganded and substrate ternary complex forms of mevalonate diphosphate decarboxylase from Streptococcus pneumoniae. Biomol. NMR Assign. 5 (1):11.
[2] Young et al. (2008) Structures of Mycobacterium tuberculosis folylpolyglutamate synthase complexed with ADP and AMPPCP. Acta Crystallogr D Biol Crystallogr. D64 (Pt 7):745.
[3] Ikuta et al. (2007) Crystal structures of the N-terminal kinase domain of human RSK1 bound to three different ligands: Implications for the design of RSK1 specific inhibitors. Protein Sci. 16 (12):2626.
[4] Picard et al. (2005) The average conformation at micromolar [Ca2+] of Ca2+-atpase with bound nucleotide differs from that adopted with the transition state analog ADP.AlFx or with AMPPCP under crystallization conditions at millimolar [Ca2+]. J. Biol. Chem. 280 (19):18745.
[5] Maity et al. (2002) Structure of triphosphoryl nucleotide bound at the active site of yeast hexokinase: 1H-nuclear magnetic resonance study. J. Protein Chem. 21 (4):265.
[6] Kubala (2006) ATP-binding to P-type ATPases as revealed by biochemical, spectroscopic, and crystallographic experiments. Proteins. 64 (1):1.
[7] Trezise et al. (1995) The selective P2X purinoceptor agonist, beta,gamma-methylene-L-adenosine 5'-triphosphate, discriminates between smooth muscle and neuronal P2X purinoceptors. Arch. Pharmacol. 351 (6):603.
O'Connor et al. (1990) Characterization of P2x-receptors in rabbit isolated ear artery. Br. J. Pharmacol. 101 (3):640.
Del Toro Duany et al. (2008) The reverse gyrase helicase-like domain is a nucleotide-dependent switch that is attenuated by the topoisomerase domain. Nucleic Acids Research 36 (18):5882.
Toyoshima et al. (2004) Crystal structure of the calcium pump with a bound ATP analogue. Nature 430:529.
Mayer et al. (1991) Re-evaluation of the specificity of adenylyl (beta,gamma-methylene)diphosphonate as a substrate for adenylate cyclase. Histochem J. 23 (2):100.
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.
Mayer et al. (1985) Specificity of cytochemical demonstration of adenylate cyclase in liver using adenylate- (beta, gammamethylene) diphosphate as substrate. Histochemistry. 82 (2):135.
Meghji et al. (1984) The effect of adenylyl compounds on the heart of the dogfish, Scyliorhinus canicula. Comparative Biochem. and Physiol.Part C: Pharmacol., Toxicol.& Endocrin. 77C (2):295.
Meghji et al. (1983) The effect of adenylyl compounds on the heart of the axolotl (Ambystema mexicanum). Comparative Biochem. and Physiol.Part C: Pharmacol., Toxicol.& Endocrin. 76 (2):319.