Our compact, low molecular weight intrinsically fluorescent nucleotides combine fluorescence with close mimicry of the properties of natural nucleotides in respect of protein binding and interaction. They display environmentally sensitive fluorescence and therefore give strong signals upon a binding event which makes them perfect probes for stopped-flow and equilibrium analysis. The Mant-fluorophore is a commonly used FRET-probe in combination with Tryptophan or Tyrosin residues of the protein of interest.
| Fluorescent analog | λexc | λem | ε | Notes/Advantages |
|---|---|---|---|---|
| [nm] | [nm] | [L*mmol-1 *cm-1] | ||
| 2',3'-TNP... | 470 | 552 | 18.5 | Historically the first fluorescent analogs used as substrates for G-proteins and ATP binding proteins. Also available as pyrimidine probes. |
| 2',3'-Mant... | 355 | 448 | 5.8 | "THE CLASSICS" for small GTPases, heterotrimeric G-proteins, GPCRs, and motor protein kinetics. Small MW and environmentally sensitive fluorescence. FRET-probe for protein-intrinsic Tyr and Trp residues. |
| 2',3'-Ant... | 332 | 423 | 4.6 | Substitute for Mant-probes. Specific for tubulin, dynein, CaM, and disulfide isomerase. FRET-probe for protein-intrinsic Tyr and Trp residues. |
| ε-ATP... | 300 | 415 | 6.0 | Commonly used substrate of motor proteins, kinases, and other ATP binding proteins. |
| 2-Aminopurine- riboside- triphosphate | 305 | 370 | 8.0 | Fluorescent analog of ATP and/or GTP. |
Gromadski et al. (2004) Streptomycin interferes with conformational coupling between codon recognition and GTPase activation on the ribosome. Nature Struct. & Molec. Biol. 11:316.
Gille et al. (2004) Xanthine nucleotide-specific G-protein a-subunits: a novel approach for the analysis of G-protein-mediated signal transduction. NS Arch. Pharmacol. 369:141.
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Gille et al. (2003) Fluorescent and colored trinitrophenylated analogs of ATP and GTP. NS Arch. Pharmacol. 368:210.
Bagshaw et al. (2001) ATP analogues at a glance. J. Cell Sci. 114:459.
Jameson et al. (1997) Fluorescent nucleotide analogs: Synthesis and applications. Methods Enzymol. 278:363 and references therein.
