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2'-Deoxyuridine-5'-diphosphate, Triethylammonium salt

Cat. No. Amount Price (EUR) Buy / Note
NU-901S 150 μl (10 mM) 142,60 Add to Basket/Quote Add to Notepad
NU-901L 5 x 150 μl (10 mM) 417,60 Add to Basket/Quote Add to Notepad
Structural formula of dUDP (2'-Deoxyuridine-5'-diphosphate, Triethylammonium salt)
Structural formula of dUDP

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: C9H14N2O11P2 (free acid)

Molecular Weight: 388.16 g/mol (free acid)

Exact Mass: 388.01 g/mol (free acid)

CAS#: 4208-67-7

Purity: ≥ 95 % (HPLC)

Form: solution in water

Color: colorless to slightly yellow

Concentration: 10 mM - 11 mM

pH: 7.5 ±0.5

Spectroscopic Properties: λmax 262 nm, ε 10.0 L mmol-1 cm-1 (Tris-HCl pH 7.5)

BIOZ Product Citations:
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Selected References:
Tóth et al. (2007) Kinetic Mechanism of Human dUTPase, an Essential Nucleotide Pyrophosphatase Enzyme. J. Biol. Chem. 282 (46):33572.
Hidalgo-Zarco et al. (2001) Kinetic properties and inhibition of the dimeric dUTPase-dUDPase from Leishmania major. Protein Sci. 10 (7): 1426.
Persson et al. (2001) Crystallization and preliminary crystallographic analysis of deoxyuridine 5 '-triphosphate nucleotidohydrolase from Bacillus subtilis. Acta Cryst. D 57:876.
Prasad et al. (2000) Structures of feline immunodeficiency virus dUTP pyrophosphatase and its nucleotide complexes in three crystal forms. Acta Cryst. D 56:1100.
Camacho et al. (2000) Properties of Leishmania major dUTP nucleotidehydrolase, a distinct nucleotide-hydrolysing enzyme in kinetoplastids. Biochem. J. 346:163.
Dauter et al. (1999) Crystal structure of dUTPase from equine infectious anaemia virus, active site metal binding in a substrate analogue complex. J. Mol. Biol. 285 (2):655.
Dauter et al. (1998) The refined structure of dUTPase from Escherichia coli. Acta Cryst. D 54:735.
Vertessy et al. (1998) The complete triphosphate moiety of non-hydrolyzable substrate analogues is required for a conformational shift of the flexible C-terminus in E-coli dUTP pyrophosphatase. FEBS Lett. 421 (1):83.
Shao et al. (1997) Characterization and mutational studies of equine infectious anemia virus dUTPase. BBA-Protein Struct. M 1339 (2):181.
Persson et al. (1997) Crystallization and preliminary X-ray crystallographic studies of dUTPase from equine infectious anemia virus. Protein Peptide Lett. 4 (2):145.
Larsson et al. (1996) Kinetic characterization of dUTPase from Escherichia coli. J. Biol. Chem. 271 (39):24010.
Larsson et al. (1996) Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP). Nat. Struct. Biol. 3 (6):532.