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TNP-ATP (2'-(or-3')-O-(Trinitrophenyl) Adenosine 5'-Triphosphate, Trisodium Salt)
The nucleotide analog TNP-ATP is modified on the ribose moiety and is essentially non-fluorescent in water. The TNP nucleotides undergoRead more
| Catalog Number | Quantity |
|---|---|
| T7602 | 2 mL |
Catalog number T7602
Price (USD)
578.00
2 mL
-
Quantity:
2 mL
Price (USD)
578.00
2 mL
The nucleotide analog TNP-ATP is modified on the ribose moiety and is essentially non-fluorescent in water. The TNP nucleotides undergo an equilibrium transition to a semiquinoid structure that has relatively long-wavelength spectral properties; this form is only fluorescent when bound to the nucleotide-binding site of some proteins.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Label or DyeTNP
Product TypeTNP-ATP
Quantity2 mL
Shipping ConditionWet Ice
Unit Size2 mL
Contents & Storage
Store in freezer -5°C to -30°C and protect from light.
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2810914Certificate of AnalysisFeb 01, 2024T7602
2488980Certificate of AnalysisJul 29, 2022T7602
2406481Certificate of AnalysisDec 10, 2021T7602
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SDSMolecular Probes® Handbook
Frequently asked questions (FAQs)
The concentration is 5 mg/mL. This information can also be found on the product COA.
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Citations & References (250)
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Citations & References
Abstract
Fluorescence resonance energy transfer mapping of the fourth of six nucleotide-binding sites of chloroplast coupling factor 1.
Journal:J Biol Chem
PubMed ID:1832671
Equilibrium dialysis measurements of adenine nucleotide binding to chloroplast coupling factor 1 suggest that the enzyme has six binding sites for ADP, adenylyl-beta,gamma-imidodiphosphate (AMP-PNP), and 2'(3')-O-2,4,6-trinitrophenyl-ATP (TNP-ATP). High affinity binding at all six sites requires the divalent cation, Mg2+. Three of the nucleotide-binding sites, sites 1, 2, and 3, have
Site-site interaction on mitochondrial F1-ATPase. Functional symmetry of the high-affinity nucleotide binding sites.
Journal:Biol Chem Hoppe Seyler
PubMed ID:2876715
Interactions between the high affinity binding sites on mitochondrial F1 were analysed by combined use of the nucleotide analogues 3'-O-(1-naphthoyl)-ADP (N-ADP) and 2'-3'-O-(2,4,6-trinitrophenyl)-ADP (TNP-ADP). The binding behaviour of F1 with respect to these ligands was studied by measuring the fluorescence of F1 and of TNP-ADP and the fluorescence anisotropy of
Mitochondrial ATP synthase. cDNA cloning, amino acid sequence, overexpression, and properties of the rat liver alpha subunit.
Journal:J Biol Chem
PubMed ID:2137825
'The predicted amino acid sequence of the alpha subunit of the rat liver mitochondrial ATP synthase has been obtained by sequencing a cDNA for the alpha subunit. Analysis of the sequence shows that it contains the A and B consensus sequences found in many nucleotide-binding proteins. Twelve amino acids of
Elimination of the hydroxyl groups in the ribose ring of ATP reduces its ability to phosphorylate the sarcoplasmic reticulum Ca(2+)-ATPase.
Journal:J Biol Chem
PubMed ID:8463222
'2''-Deoxyadenosine 5''-triphosphate, 3''-deoxyadenosine 5''-triphosphate, and 3''-amino-3''-deoxyadenosine 5''-triphosphate were substituted for ATP in the Ca2+ pumping cycle of the sarcoplasmic reticulum Ca(2+)-ATPase. The rate of phosphorylation of the enzyme decreased by more than an order of magnitude when either of the hydroxyl groups was eliminated from the ribose ring. This resulted
Structural organization of chloroplast coupling factor.
Journal:Biochemistry
PubMed ID:2859887
'Fluorescence resonance energy transfer measurements have been used to construct spatial maps for the accessible sulfhydryl of the gamma subunit (dark site) and the essential tyrosine residue of the beta subunits relative to previously mapped sites on the H+-ATPase from chloroplasts. The extent of energy transfer was measured between a
250 total citations