EDA-AppNHp
(EDA-AMPPNP)
2'/3'-O-(2-Aminoethyl-carbamoyl)-adenosine-5'-[(β,γ)-imido] triphosphate, Triethylammonium salt
| Catálogo Nº | Apresentação | Preço (R$) | Comprar / Observação |
|---|---|---|---|
| NU-810 | 500 μl (10 mM) | Sob demanda | Adicionar ao Carrinho |
![Structural formula of EDA-AppNHp ((EDA-AMPPNP), 2'/3'-O-(2-Aminoethyl-carbamoyl)-adenosine-5'-[(β,γ)-imido] triphosphate, Triethylammonium salt)](/images/Structures/NU-810_mix.png)
For general laboratory use.
Envio: shipped on dry ice
Condições de armazenamento: store at -20 °C
Short term exposure (up to 1 week cumulative) to ambient temperature possible.
Validade: 6 months after date of delivery
Fórmula molecular: C13H23N8O13P3 (free acid)
Peso molecular: 592.29 g/mol (free acid)
Pureza: ≥ 95 % (HPLC)
Forma: solution in water
Concentração: 10 mM - 11 mM
pH: 7.5 ±0.5
Propriedades espectroscópicas: λmax 259 nm, ε 15.4 L mmol-1 cm-1 (Tris-HCl pH 7.5)
Formulários:
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!
Referências selecionadas:
[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.