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EDA-AppNHp

(EDA-AMPPNP)

2'/3'-O-(2-Aminoethyl-carbamoyl)-adenosine-5'-[(β,γ)-imido] triphosphate, Triethylammonium salt

Product Cat. No. Amount Price (EUR) Buy / Note
EDA-AppNHp NU-810 500 μl (10 mM) 1.460,00 Add to Basket/Quote Add to Notepad

Structural formula of EDA-AppNHp

For research use only!

Shipping: shipped on blue ice

Storage Conditions: store at -20 °C
Short term exposure (up to 1 week cumulative) to ambient temperature possible. If stored as recommended, Jena Bioscience guarantees optimal performance of this product for 6 months after date of delivery.

Shelf Life: 6 months

Molecular Formula: C13H23N8O13P3 (free acid)

Molecular Weight: 592.29 g/mol (free acid)

Purity: ≥ 95 % (HPLC)

Form: clear aqueous solution, pH 7.5 ±0.5

Concentration: 10 mM - 11 mM

pH: 7.5 ±0.5

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

Applications:
X-ray analysis[1, 2]

Specific Ligands:

Kinesin[3]

Hsp70[4]


Please note: For reasons of stability, please make sure that the pH value of a solution of this product never drops below 7.0.
When stored at -20 °C, product may hydrolyze, thereby forming EDA-AppNH2 at a rate of up to 1 % per month!

Selected References:
[1] Terakado et al. (2010) Deleting two C-terminal α-helices is effective to crystallize the bacterial ABC transporter Escherichia coli MsbA complexed with AMP-PNP. Acta Cryst. D D66:319.
[2] Pakhomova et al. (2008) Crystal structure of fosfomycin resistance kinase FomA for streptomyces wedmorensis. J. Biol. Chem. 283:28518.
[3] Sugata et al. (2009) Nucleotide-induced flexibility change in neck linkers of dimeric kinesin as detected by distance measurements using spin-labeling EPR. J. Mol. Biol. 386:626.
[4] Shida et al. (2010) Direct inter-subdomain interactions switch between the closed and open forms of the Hsp70 nucleotide binding domain in the nucleotide-free state. Acta Cryst. D D66:223.
Mertens et al. (2012) Stepwise motion of a microcantilever driven by the hydrolysis of viral ATPases.Nanotechnology 23 (1):015501.
Lansky et al. (2011) Studying kinesin's enzymatic cycle using a single-motor confocal motility assay, employing Förster resonance energy transfer. Methods Mol. Biol. 778:19.
Matamaros et al. (2005) Suppression of Multidrug-resistant HIV-1 Reverse Transcriptase Primer Unblocking Activity by a-Phosphate-modified Thymidine Analogues. J. Mol. Biol. 349:451.