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n methyl anthraniloyl adp mant adp  (Jena Bioscience)


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    Jena Bioscience n methyl anthraniloyl adp mant adp
    N Methyl Anthraniloyl Adp Mant Adp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mant+adp/bio_rxiv__64898__2026__05__06__723347-122-11-18?v=Jena+Bioscience
    Average 94 stars, based on 31 article reviews
    n methyl anthraniloyl adp mant adp - by Bioz Stars, 2026-07
    94/100 stars

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    <t>A–B</t> <t>MANT-ADP</t> (1 µM; black trace) binds to the wild-type translocase ( A ; grey trace; 0.4 µM SecA 2 ; 1 µM SecYEG-IMVs) or to the wild-type SecA 2 ( B ; grey trace), at 25 o C, increases its fluorescence intensity and then remains relatively stable. The black arrow indicates time of translocase ( A ) or SecA 2 ( B ) addition. Subsequent addition of 1 µM MANT-ADP buffer (50 µl; red arrow) containing preprotein (10 µM; purple trace), or HSI#6 (10 µM; orange trace), caused an immediate drop in the fluorescence intensity, while addition of only buffer (grey trace), or buffer with DMSO (yellow trace), did not have that effect. All samples, except the grey trace-sample (buffer), contain the same final DMSO concentration. n = 3. Repeats were normalized (to 0% = MANT-ADP intensity; 100% = MANT-ADP plus partner intensity) and averaged. The effect of higher HSI#6 concentrations is shown in Supplementary Fig. .
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    mant adp  (Jena Bioscience)
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    <t>A–B</t> <t>MANT-ADP</t> (1 µM; black trace) binds to the wild-type translocase ( A ; grey trace; 0.4 µM SecA 2 ; 1 µM SecYEG-IMVs) or to the wild-type SecA 2 ( B ; grey trace), at 25 o C, increases its fluorescence intensity and then remains relatively stable. The black arrow indicates time of translocase ( A ) or SecA 2 ( B ) addition. Subsequent addition of 1 µM MANT-ADP buffer (50 µl; red arrow) containing preprotein (10 µM; purple trace), or HSI#6 (10 µM; orange trace), caused an immediate drop in the fluorescence intensity, while addition of only buffer (grey trace), or buffer with DMSO (yellow trace), did not have that effect. All samples, except the grey trace-sample (buffer), contain the same final DMSO concentration. n = 3. Repeats were normalized (to 0% = MANT-ADP intensity; 100% = MANT-ADP plus partner intensity) and averaged. The effect of higher HSI#6 concentrations is shown in Supplementary Fig. .
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    mant adp  (Tecan Systems)
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    <t>A–B</t> <t>MANT-ADP</t> (1 µM; black trace) binds to the wild-type translocase ( A ; grey trace; 0.4 µM SecA 2 ; 1 µM SecYEG-IMVs) or to the wild-type SecA 2 ( B ; grey trace), at 25 o C, increases its fluorescence intensity and then remains relatively stable. The black arrow indicates time of translocase ( A ) or SecA 2 ( B ) addition. Subsequent addition of 1 µM MANT-ADP buffer (50 µl; red arrow) containing preprotein (10 µM; purple trace), or HSI#6 (10 µM; orange trace), caused an immediate drop in the fluorescence intensity, while addition of only buffer (grey trace), or buffer with DMSO (yellow trace), did not have that effect. All samples, except the grey trace-sample (buffer), contain the same final DMSO concentration. n = 3. Repeats were normalized (to 0% = MANT-ADP intensity; 100% = MANT-ADP plus partner intensity) and averaged. The effect of higher HSI#6 concentrations is shown in Supplementary Fig. .
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    Effect of [Mg 2+ ] free on <t>ADP</t> release from actomyosin. Relative <t>mantADP-fluorescence</t> time traces as observed upon mixing 1 μM A∙Myo1B F387Y (A) or 1 μM A∙Myo1E Y388F (C) pre-equilibrated with 80 µM mADP at 0.05 mM and 4.55 mM free Mg 2+ -concentrations, with excess ADP. Rate of ADP release ( k -AD ) from A∙Myo1B wt and A∙Myo1B F388Y (B) and related Myo1E constructs (D) as a function of the free Mg 2+ -concentration as obtained from single exponential fits to the mantADP-fluorescence time traces.
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    Effect of [Mg 2+ ] free on <t>ADP</t> release from actomyosin. Relative <t>mantADP-fluorescence</t> time traces as observed upon mixing 1 μM A∙Myo1B F387Y (A) or 1 μM A∙Myo1E Y388F (C) pre-equilibrated with 80 µM mADP at 0.05 mM and 4.55 mM free Mg 2+ -concentrations, with excess ADP. Rate of ADP release ( k -AD ) from A∙Myo1B wt and A∙Myo1B F388Y (B) and related Myo1E constructs (D) as a function of the free Mg 2+ -concentration as obtained from single exponential fits to the mantADP-fluorescence time traces.
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    adp analog mant adp  (Jena Bioscience)
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    Jena Bioscience adp analog mant adp
    Effect of [Mg 2+ ] free on <t>ADP</t> release from actomyosin. Relative <t>mantADP-fluorescence</t> time traces as observed upon mixing 1 μM A∙Myo1B F387Y (A) or 1 μM A∙Myo1E Y388F (C) pre-equilibrated with 80 µM mADP at 0.05 mM and 4.55 mM free Mg 2+ -concentrations, with excess ADP. Rate of ADP release ( k -AD ) from A∙Myo1B wt and A∙Myo1B F388Y (B) and related Myo1E constructs (D) as a function of the free Mg 2+ -concentration as obtained from single exponential fits to the mantADP-fluorescence time traces.
    Adp Analog Mant Adp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    A–B MANT-ADP (1 µM; black trace) binds to the wild-type translocase ( A ; grey trace; 0.4 µM SecA 2 ; 1 µM SecYEG-IMVs) or to the wild-type SecA 2 ( B ; grey trace), at 25 o C, increases its fluorescence intensity and then remains relatively stable. The black arrow indicates time of translocase ( A ) or SecA 2 ( B ) addition. Subsequent addition of 1 µM MANT-ADP buffer (50 µl; red arrow) containing preprotein (10 µM; purple trace), or HSI#6 (10 µM; orange trace), caused an immediate drop in the fluorescence intensity, while addition of only buffer (grey trace), or buffer with DMSO (yellow trace), did not have that effect. All samples, except the grey trace-sample (buffer), contain the same final DMSO concentration. n = 3. Repeats were normalized (to 0% = MANT-ADP intensity; 100% = MANT-ADP plus partner intensity) and averaged. The effect of higher HSI#6 concentrations is shown in Supplementary Fig. .

    Journal: Communications Biology

    Article Title: A small molecule allosterically activates SecA dependent secretion

    doi: 10.1038/s42003-026-09623-w

    Figure Lengend Snippet: A–B MANT-ADP (1 µM; black trace) binds to the wild-type translocase ( A ; grey trace; 0.4 µM SecA 2 ; 1 µM SecYEG-IMVs) or to the wild-type SecA 2 ( B ; grey trace), at 25 o C, increases its fluorescence intensity and then remains relatively stable. The black arrow indicates time of translocase ( A ) or SecA 2 ( B ) addition. Subsequent addition of 1 µM MANT-ADP buffer (50 µl; red arrow) containing preprotein (10 µM; purple trace), or HSI#6 (10 µM; orange trace), caused an immediate drop in the fluorescence intensity, while addition of only buffer (grey trace), or buffer with DMSO (yellow trace), did not have that effect. All samples, except the grey trace-sample (buffer), contain the same final DMSO concentration. n = 3. Repeats were normalized (to 0% = MANT-ADP intensity; 100% = MANT-ADP plus partner intensity) and averaged. The effect of higher HSI#6 concentrations is shown in Supplementary Fig. .

    Article Snippet: The fluorescence intensity of 1 μM MANT-ADP increased upon addition of the holoenzyme (Fig. , black arrow; 0.4 μM SecA 2, 1 μM SecYEG-IMVs preincubated for 2 min, ice) and remained stable (grey trace), indicating tight ADP binding , .

    Techniques: Fluorescence, Concentration Assay

    Effect of [Mg 2+ ] free on ADP release from actomyosin. Relative mantADP-fluorescence time traces as observed upon mixing 1 μM A∙Myo1B F387Y (A) or 1 μM A∙Myo1E Y388F (C) pre-equilibrated with 80 µM mADP at 0.05 mM and 4.55 mM free Mg 2+ -concentrations, with excess ADP. Rate of ADP release ( k -AD ) from A∙Myo1B wt and A∙Myo1B F388Y (B) and related Myo1E constructs (D) as a function of the free Mg 2+ -concentration as obtained from single exponential fits to the mantADP-fluorescence time traces.

    Journal: Frontiers in Physiology

    Article Title: Switch-2 determines Mg 2+ ADP-release kinetics and fine-tunes the duty ratio of Dictyostelium class-1 myosins

    doi: 10.3389/fphys.2024.1393952

    Figure Lengend Snippet: Effect of [Mg 2+ ] free on ADP release from actomyosin. Relative mantADP-fluorescence time traces as observed upon mixing 1 μM A∙Myo1B F387Y (A) or 1 μM A∙Myo1E Y388F (C) pre-equilibrated with 80 µM mADP at 0.05 mM and 4.55 mM free Mg 2+ -concentrations, with excess ADP. Rate of ADP release ( k -AD ) from A∙Myo1B wt and A∙Myo1B F388Y (B) and related Myo1E constructs (D) as a function of the free Mg 2+ -concentration as obtained from single exponential fits to the mantADP-fluorescence time traces.

    Article Snippet: The 2’-(3’-)-O-(N′-Methylanthraniloyl) derivatives of ATP (mantATP) and ADP (mantADP) were purchased from Jena Bioscience.

    Techniques: Fluorescence, Construct, Concentration Assay