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dUpNHpp

(dUMPNPP)

2'-Deoxyuridine-5'-[(α,β)-imido]triphosphate, Sodium salt

Datasheet (PDF)
Catálogo Nº Apresentação Preço (R$) Comprar
NU-903S 50 μl (10 mM)Sob demanda Adicionar ao Carrinho
NU-903L 5 x 50 μl (10 mM)Sob demanda Adicionar ao Carrinho
Structural formula of dUpNHpp ((dUMPNPP), 2'-Deoxyuridine-5'-[(α,β)-imido]triphosphate, Sodium salt)
Structural formula of dUpNHpp

For general laboratory use.

Envio: shipped on gel packs

Condições de armazenamento: store at -20 °C
Short term exposure (up to 1 week cumulative) to ambient temperature possible.

Validade: 12 months after date of delivery

Fórmula molecular: C9H16N3O13P3 (free acid)

Peso molecular: 467.15 g/mol (free acid)

CAS#: 170428-86-1

Pureza: ≥ 95 % (HPLC)

Forma: solution in water

Concentração: 10 mM - 11 mM

pH: 7.5 ±0.5

Propriedades espectroscópicas: λmax 262 nm, ε 10.2 L mmol-1 cm-1 (Tris-HCl pH 7.5)

Formulários:
X-ray analysis of vaccinia virus dUTPase[1]
X-ray analysis of DNA-polymerase β[2]
Kinetic of dUTPase[3]
Inhibition of dUTPase[4]

Specific Ligands:

Vaccine virus dUTPase[1]

DNA-polymerase β[2]

Referências selecionadas:
[1] Samal et al. (2007) Structures of vaccinia virus dUTPase and ist nucleotide complexes. Acta crystallographica Section D D63:571.

[2] Batra et al. (2006) Magnesium-induced assembly of a complex DNA polymerase catalytic complex. Structure 14:757.

[3] Tóth et al. (2007) Kinetic Mechanism of Human dUTPase, an Essential Nucleotide Pyrophosphatase Enzyme. The journal of bioogical chemistry 282 (46):33572.

[4] Persson et al. (1996) Synthesis of 2'-deoxyuridine 5'- (alpha,beta-imido)triphosphate: A substrate analogue and potent inhibitor of dUTPase. Bioorgan. Med. Chem. 4 (4):553.

Xia et al. (2011) Structural insights into complete metal ion coordination from ternary complexes of B family RB69 DNA polymerase. Biochemistry. 50 (42): 9114.

Badalucco et al. (2011) Crystallization of Chlorella deoxyuridine triphosphatase. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 (Pt 12): 1599.

Pecsi et al. (2010) Aromatic stacking between nucleobase and enzyme promotes phosphate ester hydrolysis in dUTPase. Nucleic Acids Res. 38 (20):7179.

Siggaard et al. (2009) Concerted bifunctionality of the dCTP deaminase-dUTPase from Methanocaldococcus jannaschii: A structural and pre-steady state kinetic analysis. Archives of Biochemistry and Biophysics 490 (1):42.

Varga et al. (2008) Active site of mycobacterial dUTPase: Structural characteristics and a built-in sensor. Biochemical and Biophysical Research Communications 373:8.

Vertessy et al. (2007) Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins. Nucleic Acids Research 35 (2):495.