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Swiss Army Knives for NTPase Analysis

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BODIPY® FL NTPs are multipurpose tools for

  • Nucleotide binding studies on Gα, Ras, FHIT and RNAse L proteins
  • GTPase activity assays
  • Activity-based covalent labeling of bacterial two-component systems

See how it works:

Scheme 1: BODIPY® FL NTPs as fluorescent probes for protein-NTP-interactions.

Scheme 1: BODIPY® FL NTPs as fluorescent probes for protein-NTP-interactions. Binding equilibria of BODIPY®-NTP/protein complexes as well as their conversion by hydrolysis or phosphorothioate transfer can be analyzed by numerous fluorescence-based, chromatographic, electrophoretic and imaging approaches. Most strikingly, GTPγS - BDP-FL shows an increase of fluorescence by a factor of 5 upon protein binding.

Regulatory ATPase and GTPase are the ubiquitous regulators of cellular signaling in all domains of life. Their activity is modulated by binding and cleavage of their cognate NTP. For the characterization of protein-nucleotide interactions and subsequent conversion steps, BODIPY® FL NTPs have been established as fluorescent multipurpose tools. Applications include:

Application Protein examples Analytical technique
Qualitative/quantitative analysis of protein-nucleotide equilibria (KD, kon, koff)[1-4] Cdc42, Gα0/i, Rac, Ras, Rho, RNAse L Fluorescence increase
Fluorescence polarization (FP)
Capillary electrophoresis (CE)
Kinetic analysis of nucleotide cleavage[5-6] FHIT, Gα0/i Fluorescence increase
Thin layer chromatography (TLC)
Activity-based kinase labeling[7] Two-component system Imaging

BODIPY® FL NTPγS conjugates for NTPase analysis offered by Jena Bioscience

Nucleotide Cat. No. Amount Price (€)
ATPγS - BDP-FL NU-978 50 μl (5 mM) 477,05
GTPγS - BDP-FL NU-973 50 μl (5 mM) 477,05

Get in contact with us!

Dr. Thomas Waldbach

You haven't found the particular nucleotiode analog you're looking for? You have questions or need further information? Do not hesitate to contact us at nucleotides@jenabioscience.com !

Selected References:

[1] Huang et al. (2014) Dimeric structure of pseudokinase RNase L bound to 2-5A reveals a basis for interferon-induced antiviral activity. Mol. Cell. 53 (2):221.
[2] Korlach et al. (2004) Spontaneous nucleotide exchange in low molecularweight GTPases by fluorescently labeled gamma-phosphate-linked GTPanalogs. Proc. Natl. Acad. Sci. USA 101 (9):2008.
[3] McEwen et al. (2001) Fluorescent BODIPY-GTP analogs: real-time measurement of nucleotide binding to G proteins. Anal. Biochem. 291 (1):109.
[4] Whelan et al. (2004) Affinity Assays Using Fluorescence Anisotropy with Capillary Electrophoresis Separation. Anal. Chem. 76 (24):7380.
[5] Draganescu et al. (2000) Fhit-nucleotide specificity probed with novel fluorescent and fluorogenic substrates. J. Biol. Chem. 275 (7):4555.
[6] Jameson et al. (2007) Capillary Electrophoresis Assay for G Protein-Coupled Receptor-Mediated GTPase Activity. Anal. Chem. 79 (3):1158.
[7] Wilke et al. (2012) Activity-based probe for histidine kinase signaling. J. Am. Chem. Soc. 134 (22):9150.