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n 6 methyl atp  (Jena Bioscience)


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    Structured Review

    Jena Bioscience n 6 methyl atp
    N 6 Methyl Atp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 93/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/n+6+methyl+atp/N6-Methyl-ATP/pmc12222634-90-0-3
    Average 93 stars, based on 23 article reviews
    n 6 methyl atp - by Bioz Stars, 2026-09
    93/100 stars

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    Related Articles

    other:

    Article Title: Evidence that the nadA motif is a bacterial riboswitch for the ubiquitous enzyme cofactor NAD +
    Article Snippet: Chemicals were purchased from Sigma-Aldrich with the following exceptions: NADPH (Santa Cruz Biotechnology); 7-deaza-ATP, 2-amino-ATP, N 6 -methyl-ATP, and 8-oxo-ATP (TriLink BioTechnologies); 2-hydroxy-ATP, 1-CH 3 -ATP, 3′-dATP (Jena Bioscience); 8-NH 2 -ADP and β-nicotinamide-1, N 6 -ethenoadenine dinucleotide (Biolog).

    Modification:

    Article Title: Structural effects of m 6 A modification of the Xist A-repeat AUCG tetraloop and its recognition by YTHDC1
    Article Snippet: DNA template (5′-GGCGCCGATGCGCC TATAGTGAGTCGTATTA -3′) containing the T7 promoter sequence (underlined) was purchased from Eurofins Genomics as a standard desalted DNA oligo. .. 13 C- 15 N-labeled rCTP, rGTP and rUTP were purchased from Silantes, and N 6 -methyl-ATP, for the transcription of the m 6 A modified RNA, was purchased from Jena Bioscience. ..



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    Binding of variant ligands to the NAD + riboswitch domain 1. The RNA was cocrystallized with ligand variants and the structures solved either by SAD phasing or by molecular replacement using the structure bound to NADH (see Supplemental Table S1 ). For each structure is shown the C6:G47 base pair, metal M2, and the ligand with its electron density contoured at 2σ. The density maps are either omit maps (omit) or experimental phasing maps (exp). The ligands are: ( A ) ADP (omit); ( B ) NAD + (omit), ( C ) AMP (exp); ( D ) ATP (exp); ( E ) <t>N</t> <t>6</t> <t>-methylATP</t> (exp); ( F ) 3′dATP (omit); ( G ) APPS (omit).
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    Image Search Results


    Binding of variant ligands to the NAD + riboswitch domain 1. The RNA was cocrystallized with ligand variants and the structures solved either by SAD phasing or by molecular replacement using the structure bound to NADH (see Supplemental Table S1 ). For each structure is shown the C6:G47 base pair, metal M2, and the ligand with its electron density contoured at 2σ. The density maps are either omit maps (omit) or experimental phasing maps (exp). The ligands are: ( A ) ADP (omit); ( B ) NAD + (omit), ( C ) AMP (exp); ( D ) ATP (exp); ( E ) N 6 -methylATP (exp); ( F ) 3′dATP (omit); ( G ) APPS (omit).

    Journal: RNA

    Article Title: Structure and ligand binding of the ADP-binding domain of the NAD + riboswitch

    doi: 10.1261/rna.074898.120

    Figure Lengend Snippet: Binding of variant ligands to the NAD + riboswitch domain 1. The RNA was cocrystallized with ligand variants and the structures solved either by SAD phasing or by molecular replacement using the structure bound to NADH (see Supplemental Table S1 ). For each structure is shown the C6:G47 base pair, metal M2, and the ligand with its electron density contoured at 2σ. The density maps are either omit maps (omit) or experimental phasing maps (exp). The ligands are: ( A ) ADP (omit); ( B ) NAD + (omit), ( C ) AMP (exp); ( D ) ATP (exp); ( E ) N 6 -methylATP (exp); ( F ) 3′dATP (omit); ( G ) APPS (omit).

    Article Snippet: N 6 -methylATP (NU-1101L) was obtained from Jena Bioscience.

    Techniques: Binding Assay, Variant Assay

    Ligand binding to the NAD + riboswitch domain 1 analyzed by isothermal titration calorimetry and mutagenesis. A solution of NAD, ADP, or N 6 -methylATP was titrated into a wild-type or mutant NAD + riboswitch domain 1 solution, and the heat evolved was measured as the power required to maintain zero temperature difference with a reference cell. Integration over time gives the heat required to maintain thermal equilibrium between cells. In each case, the upper panel shows the raw data for sequential injections of 2 µL volumes (following an initial injection of 0.4 µL) of a 1 mM solution of ligands into 200 µL of a 100 µM RNA solution in 40 mM HEPES (pH 7.2), 100 mM KCl, 10 mM MgCl 2 . This represents the differential of the total heat (i.e., enthalpy Δ H ° under conditions of constant pressure) for each domain 1 concentration. Integrated heat data were analyzed using a one-set-of-sites model in MicroCal Origin following the manufacturer's instructions. The first data point was excluded in the analysis. All ITC experiments were repeated a total of three times. ( A – C ) Titration of ADP ( A ), NAD + ( B ), and N 6 -methylATP ( C ) into unmodified domain 1 RNA. ( D – F ) Titration of ADP into modified domain 1 RNA; C6U:G47A mutant ( D ), and atomic mutants generated by removing the 2′-hydroxyl groups of C6 ( E ) and G47 ( F ). ( G ) Chemical structures of the interactions showing the mutations used in the ITC experiments.

    Journal: RNA

    Article Title: Structure and ligand binding of the ADP-binding domain of the NAD + riboswitch

    doi: 10.1261/rna.074898.120

    Figure Lengend Snippet: Ligand binding to the NAD + riboswitch domain 1 analyzed by isothermal titration calorimetry and mutagenesis. A solution of NAD, ADP, or N 6 -methylATP was titrated into a wild-type or mutant NAD + riboswitch domain 1 solution, and the heat evolved was measured as the power required to maintain zero temperature difference with a reference cell. Integration over time gives the heat required to maintain thermal equilibrium between cells. In each case, the upper panel shows the raw data for sequential injections of 2 µL volumes (following an initial injection of 0.4 µL) of a 1 mM solution of ligands into 200 µL of a 100 µM RNA solution in 40 mM HEPES (pH 7.2), 100 mM KCl, 10 mM MgCl 2 . This represents the differential of the total heat (i.e., enthalpy Δ H ° under conditions of constant pressure) for each domain 1 concentration. Integrated heat data were analyzed using a one-set-of-sites model in MicroCal Origin following the manufacturer's instructions. The first data point was excluded in the analysis. All ITC experiments were repeated a total of three times. ( A – C ) Titration of ADP ( A ), NAD + ( B ), and N 6 -methylATP ( C ) into unmodified domain 1 RNA. ( D – F ) Titration of ADP into modified domain 1 RNA; C6U:G47A mutant ( D ), and atomic mutants generated by removing the 2′-hydroxyl groups of C6 ( E ) and G47 ( F ). ( G ) Chemical structures of the interactions showing the mutations used in the ITC experiments.

    Article Snippet: N 6 -methylATP (NU-1101L) was obtained from Jena Bioscience.

    Techniques: Ligand Binding Assay, Isothermal Titration Calorimetry, Mutagenesis, Injection, Concentration Assay, Titration, Modification, Generated