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eda gdp bdp fl  (Jena Bioscience)


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    Structured Review

    Jena Bioscience eda gdp bdp fl
    a , Nucleotide-content analysis of purified, heat-denatured monomeric G-domains after incubation with 3 mM GTP and GDP followed by desalting. No stably bound nucleotide was detected. A protein-free desalting control is shown for comparison. b , GTP hydrolysis by monomeric Cdc10 and Cdc12 quantified by malachite green assays over a range of initial GTP concentrations (20–300 µM). Data points show arithmetic means ± s.d. of three independent experiments, each averaged from 1–4 technical replicates. c , Representative stopped-flow fluorescence traces of EDA-GTP-BDP-FL association and dissociation with monomeric Cdc12. Global non-linear fits are shown in neon green. Kinetic parameters ( k1 , k−1 , k2 , k−2 , KD ) are geometric means with asymmetric 95% CIs from six independent association experiments (association was measured at 1.0–4.2 µM Cdc12 (four preparations) or 1.0–3.1 µM (two preparations)) and four independent dissociation experiments. d , As in c for Cdc11 with kinetic constants from four independent experiments. e , f , Stopped-flow fluorescence traces for Cdc3 ( e ) and Shs1 ( f ) revealing no detectable binding to EDA-GTP-BDP-FL or <t>EDA-GDP-BDP-FL.</t> However, we cannot exclude the possibility that these subunits are incompatible with the fluorescent nucleotide analogs.
    Eda Gdp Bdp Fl, 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
    https://www.bioz.com/product/eda+gdp+bdp+fl/EDA-GDP-BDP-FL/bio_rxiv__64898__2026__05__07__723466-256-18-19
    Average 94 stars, based on 1 article reviews
    eda gdp bdp fl - by Bioz Stars, 2026-09
    94/100 stars

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    1) Product Images from "A nucleotide-triggered molecular switch orchestrating septin polymerization"

    Article Title: A nucleotide-triggered molecular switch orchestrating septin polymerization

    Journal: bioRxiv

    doi: 10.64898/2026.05.07.723466

    a , Nucleotide-content analysis of purified, heat-denatured monomeric G-domains after incubation with 3 mM GTP and GDP followed by desalting. No stably bound nucleotide was detected. A protein-free desalting control is shown for comparison. b , GTP hydrolysis by monomeric Cdc10 and Cdc12 quantified by malachite green assays over a range of initial GTP concentrations (20–300 µM). Data points show arithmetic means ± s.d. of three independent experiments, each averaged from 1–4 technical replicates. c , Representative stopped-flow fluorescence traces of EDA-GTP-BDP-FL association and dissociation with monomeric Cdc12. Global non-linear fits are shown in neon green. Kinetic parameters ( k1 , k−1 , k2 , k−2 , KD ) are geometric means with asymmetric 95% CIs from six independent association experiments (association was measured at 1.0–4.2 µM Cdc12 (four preparations) or 1.0–3.1 µM (two preparations)) and four independent dissociation experiments. d , As in c for Cdc11 with kinetic constants from four independent experiments. e , f , Stopped-flow fluorescence traces for Cdc3 ( e ) and Shs1 ( f ) revealing no detectable binding to EDA-GTP-BDP-FL or EDA-GDP-BDP-FL. However, we cannot exclude the possibility that these subunits are incompatible with the fluorescent nucleotide analogs.
    Figure Legend Snippet: a , Nucleotide-content analysis of purified, heat-denatured monomeric G-domains after incubation with 3 mM GTP and GDP followed by desalting. No stably bound nucleotide was detected. A protein-free desalting control is shown for comparison. b , GTP hydrolysis by monomeric Cdc10 and Cdc12 quantified by malachite green assays over a range of initial GTP concentrations (20–300 µM). Data points show arithmetic means ± s.d. of three independent experiments, each averaged from 1–4 technical replicates. c , Representative stopped-flow fluorescence traces of EDA-GTP-BDP-FL association and dissociation with monomeric Cdc12. Global non-linear fits are shown in neon green. Kinetic parameters ( k1 , k−1 , k2 , k−2 , KD ) are geometric means with asymmetric 95% CIs from six independent association experiments (association was measured at 1.0–4.2 µM Cdc12 (four preparations) or 1.0–3.1 µM (two preparations)) and four independent dissociation experiments. d , As in c for Cdc11 with kinetic constants from four independent experiments. e , f , Stopped-flow fluorescence traces for Cdc3 ( e ) and Shs1 ( f ) revealing no detectable binding to EDA-GTP-BDP-FL or EDA-GDP-BDP-FL. However, we cannot exclude the possibility that these subunits are incompatible with the fluorescent nucleotide analogs.

    Techniques Used: Purification, Incubation, Stable Transfection, Control, Comparison, Fluorescence, Binding Assay

    Related Articles

    Construct:

    Article Title: A nucleotide-triggered molecular switch orchestrating septin polymerization
    Article Snippet: For association kinetics, constructs #1 and #2 were measured under pseudo-first-order conditions at final protein concentrations between 1.0 and 4.2 μM in the presence of 0.08 μM EDA-GTP-BDP-FL (Jena Bioscience), whereas construct #4 was assayed at final protein concentrations of 21 to 104 μM with 0.8 μM EDA-GTP-BDP-FL. .. Constructs #3 and #5 were measured at final concentrations of 104 μM protein with 2.5 μM EDA-GTP-BDP-FL or EDA-GDP-BDP-FL (Jena Bioscience). ..



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    eda gdp bdp fl  (Jena Bioscience)
    94
    Jena Bioscience eda gdp bdp fl
    a , Nucleotide-content analysis of purified, heat-denatured monomeric G-domains after incubation with 3 mM GTP and GDP followed by desalting. No stably bound nucleotide was detected. A protein-free desalting control is shown for comparison. b , GTP hydrolysis by monomeric Cdc10 and Cdc12 quantified by malachite green assays over a range of initial GTP concentrations (20–300 µM). Data points show arithmetic means ± s.d. of three independent experiments, each averaged from 1–4 technical replicates. c , Representative stopped-flow fluorescence traces of EDA-GTP-BDP-FL association and dissociation with monomeric Cdc12. Global non-linear fits are shown in neon green. Kinetic parameters ( k1 , k−1 , k2 , k−2 , KD ) are geometric means with asymmetric 95% CIs from six independent association experiments (association was measured at 1.0–4.2 µM Cdc12 (four preparations) or 1.0–3.1 µM (two preparations)) and four independent dissociation experiments. d , As in c for Cdc11 with kinetic constants from four independent experiments. e , f , Stopped-flow fluorescence traces for Cdc3 ( e ) and Shs1 ( f ) revealing no detectable binding to EDA-GTP-BDP-FL or <t>EDA-GDP-BDP-FL.</t> However, we cannot exclude the possibility that these subunits are incompatible with the fluorescent nucleotide analogs.
    Eda Gdp Bdp Fl, 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
    https://www.bioz.com/product/eda+gdp+bdp+fl/EDA-GDP-BDP-FL/bio_rxiv__64898__2026__05__07__723466-256-18-19
    Average 94 stars, based on 1 article reviews
    eda gdp bdp fl - by Bioz Stars, 2026-09
    94/100 stars
    		  Buy from Supplier

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    a , Nucleotide-content analysis of purified, heat-denatured monomeric G-domains after incubation with 3 mM GTP and GDP followed by desalting. No stably bound nucleotide was detected. A protein-free desalting control is shown for comparison. b , GTP hydrolysis by monomeric Cdc10 and Cdc12 quantified by malachite green assays over a range of initial GTP concentrations (20–300 µM). Data points show arithmetic means ± s.d. of three independent experiments, each averaged from 1–4 technical replicates. c , Representative stopped-flow fluorescence traces of EDA-GTP-BDP-FL association and dissociation with monomeric Cdc12. Global non-linear fits are shown in neon green. Kinetic parameters ( k1 , k−1 , k2 , k−2 , KD ) are geometric means with asymmetric 95% CIs from six independent association experiments (association was measured at 1.0–4.2 µM Cdc12 (four preparations) or 1.0–3.1 µM (two preparations)) and four independent dissociation experiments. d , As in c for Cdc11 with kinetic constants from four independent experiments. e , f , Stopped-flow fluorescence traces for Cdc3 ( e ) and Shs1 ( f ) revealing no detectable binding to EDA-GTP-BDP-FL or EDA-GDP-BDP-FL. However, we cannot exclude the possibility that these subunits are incompatible with the fluorescent nucleotide analogs.

    Journal: bioRxiv

    Article Title: A nucleotide-triggered molecular switch orchestrating septin polymerization

    doi: 10.64898/2026.05.07.723466

    Figure Lengend Snippet: a , Nucleotide-content analysis of purified, heat-denatured monomeric G-domains after incubation with 3 mM GTP and GDP followed by desalting. No stably bound nucleotide was detected. A protein-free desalting control is shown for comparison. b , GTP hydrolysis by monomeric Cdc10 and Cdc12 quantified by malachite green assays over a range of initial GTP concentrations (20–300 µM). Data points show arithmetic means ± s.d. of three independent experiments, each averaged from 1–4 technical replicates. c , Representative stopped-flow fluorescence traces of EDA-GTP-BDP-FL association and dissociation with monomeric Cdc12. Global non-linear fits are shown in neon green. Kinetic parameters ( k1 , k−1 , k2 , k−2 , KD ) are geometric means with asymmetric 95% CIs from six independent association experiments (association was measured at 1.0–4.2 µM Cdc12 (four preparations) or 1.0–3.1 µM (two preparations)) and four independent dissociation experiments. d , As in c for Cdc11 with kinetic constants from four independent experiments. e , f , Stopped-flow fluorescence traces for Cdc3 ( e ) and Shs1 ( f ) revealing no detectable binding to EDA-GTP-BDP-FL or EDA-GDP-BDP-FL. However, we cannot exclude the possibility that these subunits are incompatible with the fluorescent nucleotide analogs.

    Article Snippet: Constructs #3 and #5 were measured at final concentrations of 104 μM protein with 2.5 μM EDA-GTP-BDP-FL or EDA-GDP-BDP-FL (Jena Bioscience).

    Techniques: Purification, Incubation, Stable Transfection, Control, Comparison, Fluorescence, Binding Assay