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Fluorescent TNP (Trinitrophenyl) nucleotide analogs, such as TNP-ATP or TNP-GTP, are able to mimic the binding characteristics of natural nucleotides in their interaction with various enzymes and proteins. They have been used as fluorescent probes in a wide range of applications[1] for protein functional analysis, including

  • Determination of kinetic parameters of nucleotide-protein interactions[2]
  • Fluorescence acceptors in FRET experiments[3]
  • Assessment of nucleotide-interacting properties of mutant proteins[1]
  • Antagonists of P2X receptors[4]
  • X-ray crystallography[5]
  • Fluorescence microscopy[6]
  • Ligand binding studies[7]

Chemical structure of TNP-ATP (JBS Cat.-No.: NU-221)


   
   TNP nucleotides exhibit several advantageous properties, such as:
   

  • Excitation at wavelengths (408 and 470 nm) far from where proteins or nucleotides absorb
  • Absorption spectrum overlaps with the emission spectra of many commonly used fluorescence donors
  • Weakly fluorescent in aqueous solutions - markedly enhanced fluorescence upon binding to a protein (intrinsic fluorescence)
  • Sensitivity to indicators of local environment such as polarity and viscosity


Jena Bioscience offers a diverse selection of TNP nucleotide analogs,
for more information please click:

www.jenabioscience.com/cms/en/1/catalog/309/


Selected References:
[1] Hiratsuka (2003) Fluorescent and colored trinitrophenylated analogs of ATP and GTP. Eur. J. Biochem. 270:3479.
[2] Moutin et al. (1994) Measurements of ATP binding on the large cytoplasmic loop of the sarcoplasmic reticulum Ca2+-ATPase overexpressed in Escherichia coli. J. Biol. Chem. 269:11147.
[3] Lin et al. (1996) Estimation of the distance change between cysteine-457 and the nucleotide binding site when sodium pump changes conformation from E1 to E2 by fluorescence energy transfer measurements. Biochemistry 35:8419.
[4] Virginio et al. (1998) Trinitrophenyl-substituted nucleotides are potent antagonists selective for P2X1, P2X3, and heteromeric P2X2/3 receptors. Mol. Pharmacol. 53:969.
[5] Vas et al. (2002) Nucleotide binding to pig muscle 3-phosphoglycerate kinase in the crystal and in solution: relationship between substrate antagonism and interdomain communication. Biochem. 41:111.
[6] Mockett et al. (1994) Fluorescence imaging of extracellular purinergic receptor sites and putative ecto-ATPase sites on isolated cochlear hair cells. J. Neurosci. 14:6992.
[7] Lutsenko et al. (2001) The Lys1010-Lys1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a Copper-dependent manner. J. Biol. Chem. 276:2234.

Nucleotide analogs not on stock may be available as custom synthesis, just send us an e-mail at nucleotides@jenabioscience.com with any questions you may have!


   
   

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