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eda gtp bdp fl  (Jena Bioscience)


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    Structured Review

    Jena Bioscience eda gtp bdp fl
    a , Nucleotide content of purified monomeric G-domains (Cdc10, Cdc3, Cdc12, Cdc11, Shs1) and co-expressed G-interface dimers (Cdc10-Cdc3, Cdc12-Cdc11, Cdc12-Shs1). Left: representative HPLC chromatograms from heat-denatured samples. Right: quantified nucleotide occupancy in dimers (arithmetic mean ± s.d., n = 3 independent experiments). Monomers are nucleotide-free; dimers are nucleotide-bound. b , Apparent GTP hydrolysis rates ( kcat,app ) measured by a malachite green assay at 100 µM GTP. Data are arithmetic means + symmetric 95% confidence intervals (CIs). Each data point represents the average of 2–12 technical replicates from independent experiments (Cdc10 n = 4, Cdc12 n = 4, Cdc3 n = 3, Cdc11 n = 3, Shs1 n = 3, Cdc10-Cdc3 n = 3 (MgCl2) or 4 (EDTA), Cdc12-Cdc11 n = 3 (MgCl2) or 4 (EDTA), Cdc12-Shs1 n = 4). For MBP, six replicates from the same snap-frozen protein preparation were measured on different occasions. Constructs with detectable activity are indicated (+). Significance brackets indicate results from one-way ANOVA with Tukey’s post hoc test. c , Representative stopped-flow fluorescence <t>traces</t> <t>of</t> <t>EDA-GTP-BDP-FL</t> association and dissociation with monomeric Cdc10. Global non-linear fits are shown in neon green. Kinetic parameters ( kon , koff , KD ) are geometric means with asymmetric 95% CIs from five independent experiments (association was measured at 1.0–4.2 µM Cdc10 (three preparations) or 1.0–3.1 µM (two preparations)). d , Investigation of dimer integrity via analytical SEC. Guanine nucleotide binding stabilizes G-interfaces. Co-expressed pairs (Cdc10-Cdc3, Cdc12-Cdc11, Cdc12-Shs1) form stable nucleotide-bound dimers. Incubation at 30 °C promotes dissociation, which is prevented by the addition of GTP and GDP. Phosphatase treatment (rSAP) amplifies dimer disruption.
    Eda Gtp 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+gtp+bdp+fl/EDA-GTP-BDP-FL/bio_rxiv__64898__2026__05__07__723466-255-27-28
    Average 94 stars, based on 1 article reviews
    eda gtp bdp fl - by Bioz Stars, 2026-09
    94/100 stars

    Images

    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 of purified monomeric G-domains (Cdc10, Cdc3, Cdc12, Cdc11, Shs1) and co-expressed G-interface dimers (Cdc10-Cdc3, Cdc12-Cdc11, Cdc12-Shs1). Left: representative HPLC chromatograms from heat-denatured samples. Right: quantified nucleotide occupancy in dimers (arithmetic mean ± s.d., n = 3 independent experiments). Monomers are nucleotide-free; dimers are nucleotide-bound. b , Apparent GTP hydrolysis rates ( kcat,app ) measured by a malachite green assay at 100 µM GTP. Data are arithmetic means + symmetric 95% confidence intervals (CIs). Each data point represents the average of 2–12 technical replicates from independent experiments (Cdc10 n = 4, Cdc12 n = 4, Cdc3 n = 3, Cdc11 n = 3, Shs1 n = 3, Cdc10-Cdc3 n = 3 (MgCl2) or 4 (EDTA), Cdc12-Cdc11 n = 3 (MgCl2) or 4 (EDTA), Cdc12-Shs1 n = 4). For MBP, six replicates from the same snap-frozen protein preparation were measured on different occasions. Constructs with detectable activity are indicated (+). Significance brackets indicate results from one-way ANOVA with Tukey’s post hoc test. c , Representative stopped-flow fluorescence traces of EDA-GTP-BDP-FL association and dissociation with monomeric Cdc10. Global non-linear fits are shown in neon green. Kinetic parameters ( kon , koff , KD ) are geometric means with asymmetric 95% CIs from five independent experiments (association was measured at 1.0–4.2 µM Cdc10 (three preparations) or 1.0–3.1 µM (two preparations)). d , Investigation of dimer integrity via analytical SEC. Guanine nucleotide binding stabilizes G-interfaces. Co-expressed pairs (Cdc10-Cdc3, Cdc12-Cdc11, Cdc12-Shs1) form stable nucleotide-bound dimers. Incubation at 30 °C promotes dissociation, which is prevented by the addition of GTP and GDP. Phosphatase treatment (rSAP) amplifies dimer disruption.
    Figure Legend Snippet: a , Nucleotide content of purified monomeric G-domains (Cdc10, Cdc3, Cdc12, Cdc11, Shs1) and co-expressed G-interface dimers (Cdc10-Cdc3, Cdc12-Cdc11, Cdc12-Shs1). Left: representative HPLC chromatograms from heat-denatured samples. Right: quantified nucleotide occupancy in dimers (arithmetic mean ± s.d., n = 3 independent experiments). Monomers are nucleotide-free; dimers are nucleotide-bound. b , Apparent GTP hydrolysis rates ( kcat,app ) measured by a malachite green assay at 100 µM GTP. Data are arithmetic means + symmetric 95% confidence intervals (CIs). Each data point represents the average of 2–12 technical replicates from independent experiments (Cdc10 n = 4, Cdc12 n = 4, Cdc3 n = 3, Cdc11 n = 3, Shs1 n = 3, Cdc10-Cdc3 n = 3 (MgCl2) or 4 (EDTA), Cdc12-Cdc11 n = 3 (MgCl2) or 4 (EDTA), Cdc12-Shs1 n = 4). For MBP, six replicates from the same snap-frozen protein preparation were measured on different occasions. Constructs with detectable activity are indicated (+). Significance brackets indicate results from one-way ANOVA with Tukey’s post hoc test. c , Representative stopped-flow fluorescence traces of EDA-GTP-BDP-FL association and dissociation with monomeric Cdc10. Global non-linear fits are shown in neon green. Kinetic parameters ( kon , koff , KD ) are geometric means with asymmetric 95% CIs from five independent experiments (association was measured at 1.0–4.2 µM Cdc10 (three preparations) or 1.0–3.1 µM (two preparations)). d , Investigation of dimer integrity via analytical SEC. Guanine nucleotide binding stabilizes G-interfaces. Co-expressed pairs (Cdc10-Cdc3, Cdc12-Cdc11, Cdc12-Shs1) form stable nucleotide-bound dimers. Incubation at 30 °C promotes dissociation, which is prevented by the addition of GTP and GDP. Phosphatase treatment (rSAP) amplifies dimer disruption.

    Techniques Used: Purification, Malachite Green Assay, Construct, Activity Assay, Fluorescence, Binding Assay, Incubation, Disruption

    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 gtp bdp fl  (Jena Bioscience)
    94
    Jena Bioscience eda gtp bdp fl
    a , Nucleotide content of purified monomeric G-domains (Cdc10, Cdc3, Cdc12, Cdc11, Shs1) and co-expressed G-interface dimers (Cdc10-Cdc3, Cdc12-Cdc11, Cdc12-Shs1). Left: representative HPLC chromatograms from heat-denatured samples. Right: quantified nucleotide occupancy in dimers (arithmetic mean ± s.d., n = 3 independent experiments). Monomers are nucleotide-free; dimers are nucleotide-bound. b , Apparent GTP hydrolysis rates ( kcat,app ) measured by a malachite green assay at 100 µM GTP. Data are arithmetic means + symmetric 95% confidence intervals (CIs). Each data point represents the average of 2–12 technical replicates from independent experiments (Cdc10 n = 4, Cdc12 n = 4, Cdc3 n = 3, Cdc11 n = 3, Shs1 n = 3, Cdc10-Cdc3 n = 3 (MgCl2) or 4 (EDTA), Cdc12-Cdc11 n = 3 (MgCl2) or 4 (EDTA), Cdc12-Shs1 n = 4). For MBP, six replicates from the same snap-frozen protein preparation were measured on different occasions. Constructs with detectable activity are indicated (+). Significance brackets indicate results from one-way ANOVA with Tukey’s post hoc test. c , Representative stopped-flow fluorescence <t>traces</t> <t>of</t> <t>EDA-GTP-BDP-FL</t> association and dissociation with monomeric Cdc10. Global non-linear fits are shown in neon green. Kinetic parameters ( kon , koff , KD ) are geometric means with asymmetric 95% CIs from five independent experiments (association was measured at 1.0–4.2 µM Cdc10 (three preparations) or 1.0–3.1 µM (two preparations)). d , Investigation of dimer integrity via analytical SEC. Guanine nucleotide binding stabilizes G-interfaces. Co-expressed pairs (Cdc10-Cdc3, Cdc12-Cdc11, Cdc12-Shs1) form stable nucleotide-bound dimers. Incubation at 30 °C promotes dissociation, which is prevented by the addition of GTP and GDP. Phosphatase treatment (rSAP) amplifies dimer disruption.
    Eda Gtp 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+gtp+bdp+fl/EDA-GTP-BDP-FL/bio_rxiv__64898__2026__05__07__723466-255-27-28
    Average 94 stars, based on 1 article reviews
    eda gtp bdp fl - by Bioz Stars, 2026-09
    94/100 stars
    		  Buy from Supplier

    Image Search Results


    a , Nucleotide content of purified monomeric G-domains (Cdc10, Cdc3, Cdc12, Cdc11, Shs1) and co-expressed G-interface dimers (Cdc10-Cdc3, Cdc12-Cdc11, Cdc12-Shs1). Left: representative HPLC chromatograms from heat-denatured samples. Right: quantified nucleotide occupancy in dimers (arithmetic mean ± s.d., n = 3 independent experiments). Monomers are nucleotide-free; dimers are nucleotide-bound. b , Apparent GTP hydrolysis rates ( kcat,app ) measured by a malachite green assay at 100 µM GTP. Data are arithmetic means + symmetric 95% confidence intervals (CIs). Each data point represents the average of 2–12 technical replicates from independent experiments (Cdc10 n = 4, Cdc12 n = 4, Cdc3 n = 3, Cdc11 n = 3, Shs1 n = 3, Cdc10-Cdc3 n = 3 (MgCl2) or 4 (EDTA), Cdc12-Cdc11 n = 3 (MgCl2) or 4 (EDTA), Cdc12-Shs1 n = 4). For MBP, six replicates from the same snap-frozen protein preparation were measured on different occasions. Constructs with detectable activity are indicated (+). Significance brackets indicate results from one-way ANOVA with Tukey’s post hoc test. c , Representative stopped-flow fluorescence traces of EDA-GTP-BDP-FL association and dissociation with monomeric Cdc10. Global non-linear fits are shown in neon green. Kinetic parameters ( kon , koff , KD ) are geometric means with asymmetric 95% CIs from five independent experiments (association was measured at 1.0–4.2 µM Cdc10 (three preparations) or 1.0–3.1 µM (two preparations)). d , Investigation of dimer integrity via analytical SEC. Guanine nucleotide binding stabilizes G-interfaces. Co-expressed pairs (Cdc10-Cdc3, Cdc12-Cdc11, Cdc12-Shs1) form stable nucleotide-bound dimers. Incubation at 30 °C promotes dissociation, which is prevented by the addition of GTP and GDP. Phosphatase treatment (rSAP) amplifies dimer disruption.

    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 of purified monomeric G-domains (Cdc10, Cdc3, Cdc12, Cdc11, Shs1) and co-expressed G-interface dimers (Cdc10-Cdc3, Cdc12-Cdc11, Cdc12-Shs1). Left: representative HPLC chromatograms from heat-denatured samples. Right: quantified nucleotide occupancy in dimers (arithmetic mean ± s.d., n = 3 independent experiments). Monomers are nucleotide-free; dimers are nucleotide-bound. b , Apparent GTP hydrolysis rates ( kcat,app ) measured by a malachite green assay at 100 µM GTP. Data are arithmetic means + symmetric 95% confidence intervals (CIs). Each data point represents the average of 2–12 technical replicates from independent experiments (Cdc10 n = 4, Cdc12 n = 4, Cdc3 n = 3, Cdc11 n = 3, Shs1 n = 3, Cdc10-Cdc3 n = 3 (MgCl2) or 4 (EDTA), Cdc12-Cdc11 n = 3 (MgCl2) or 4 (EDTA), Cdc12-Shs1 n = 4). For MBP, six replicates from the same snap-frozen protein preparation were measured on different occasions. Constructs with detectable activity are indicated (+). Significance brackets indicate results from one-way ANOVA with Tukey’s post hoc test. c , Representative stopped-flow fluorescence traces of EDA-GTP-BDP-FL association and dissociation with monomeric Cdc10. Global non-linear fits are shown in neon green. Kinetic parameters ( kon , koff , KD ) are geometric means with asymmetric 95% CIs from five independent experiments (association was measured at 1.0–4.2 µM Cdc10 (three preparations) or 1.0–3.1 µM (two preparations)). d , Investigation of dimer integrity via analytical SEC. Guanine nucleotide binding stabilizes G-interfaces. Co-expressed pairs (Cdc10-Cdc3, Cdc12-Cdc11, Cdc12-Shs1) form stable nucleotide-bound dimers. Incubation at 30 °C promotes dissociation, which is prevented by the addition of GTP and GDP. Phosphatase treatment (rSAP) amplifies dimer disruption.

    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.

    Techniques: Purification, Malachite Green Assay, Construct, Activity Assay, Fluorescence, Binding Assay, Incubation, Disruption

    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: 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.

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