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fus recombinant protein  (Novus Biologicals)


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    Structured Review

    Novus Biologicals fus recombinant protein
    a-b: <t>Recombinant</t> <t>FUS</t> protein was incubated in presence of ETV5-CFP or/and MEF2A-mCherry recombinant proteins. After immunoprecipitation using FUS antibody then pulled out with A/G-coupled magnetic beads, immunoprecipitated proteins were examined by western blot using FUS, ETV5 and MEF2A antibody. The band intensities of co-immunoprecipitated MEF2A-mCherry and ETV5-CFP were quantified using iBright Analysis Software (B). Error bars represent SEM of four independent experiments. c-d Cooperative binding assay of FUS, ETV5, MEF2A recombinant proteins to FAM labelled Mrpl30 promoter-derived DNA probe. EMSA experiments performed by using increasing concentrations of ETV5 (60, 120, 180 and 240 nM) and constant concentration of FUS (300 nM) and/or MEF2A (50 nM). Panel D shows the percentage of Mrpl30 probe bound across 3 independent experiments. The intensity of the signals of the protein- Mrpl30 probe complex was quantified using the iBright Analysis Software. Error bars represent SEM of three independent experiments. e: Representative confocal images of FUS-EGFP condensates (5 µM) in absence or presence of ETV5-CFP (3 µM) and/or MEF2A-mCherry (0.85 µM) upon protease-mediated cleavage of the MBP-solubility tags. No condensates were observed for ETV5 or MEF2A alone or mixed together in absence of FUS condensates. Bar, 10 µm. f-g: Quantification of FUS-EGFP condensate roundness (F) and size (G). Mean ± SEM of three independent replicates with at least 179 condensates in total from ≥3 different fields of view analyzed. * p<0.05, *** p<0.005 by one-way ANOVA with Tukey’s multiple comparison test. h: Light units relative to Empty vector in C2C12 cells 24 h after transfection of 3xMEF2 luciferase plasmid and an expression plasmid for either hFUS WT, hFUS R495X, LLPS deficient hFUS (hFUS YnCA), LLPS-deficient hFUS with SV40 NLS or empty control plasmid. Nested one-way ANOVA with Tukey’s multiple comparisons test; ***P < 0.001, **P<0.01, *P < 0.05. Each dot represents the mean of an individual experiment (n=3), each consisting of 4 technical replicates. Data represent the mean ± SEM. Expression of human wild type FUS but neither R495X nor LLPS deficient FUS increases activity of the MEF2 reporter.
    Fus Recombinant Protein, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fus recombinant protein/product/Novus Biologicals
    Average 92 stars, based on 2 article reviews
    fus recombinant protein - by Bioz Stars, 2026-05
    92/100 stars

    Images

    1) Product Images from "FUS controls muscle differentiation and structure through LLPS mediated recruitment of MEF2 and ETV5"

    Article Title: FUS controls muscle differentiation and structure through LLPS mediated recruitment of MEF2 and ETV5

    Journal: bioRxiv

    doi: 10.1101/2024.09.18.613669

    a-b: Recombinant FUS protein was incubated in presence of ETV5-CFP or/and MEF2A-mCherry recombinant proteins. After immunoprecipitation using FUS antibody then pulled out with A/G-coupled magnetic beads, immunoprecipitated proteins were examined by western blot using FUS, ETV5 and MEF2A antibody. The band intensities of co-immunoprecipitated MEF2A-mCherry and ETV5-CFP were quantified using iBright Analysis Software (B). Error bars represent SEM of four independent experiments. c-d Cooperative binding assay of FUS, ETV5, MEF2A recombinant proteins to FAM labelled Mrpl30 promoter-derived DNA probe. EMSA experiments performed by using increasing concentrations of ETV5 (60, 120, 180 and 240 nM) and constant concentration of FUS (300 nM) and/or MEF2A (50 nM). Panel D shows the percentage of Mrpl30 probe bound across 3 independent experiments. The intensity of the signals of the protein- Mrpl30 probe complex was quantified using the iBright Analysis Software. Error bars represent SEM of three independent experiments. e: Representative confocal images of FUS-EGFP condensates (5 µM) in absence or presence of ETV5-CFP (3 µM) and/or MEF2A-mCherry (0.85 µM) upon protease-mediated cleavage of the MBP-solubility tags. No condensates were observed for ETV5 or MEF2A alone or mixed together in absence of FUS condensates. Bar, 10 µm. f-g: Quantification of FUS-EGFP condensate roundness (F) and size (G). Mean ± SEM of three independent replicates with at least 179 condensates in total from ≥3 different fields of view analyzed. * p<0.05, *** p<0.005 by one-way ANOVA with Tukey’s multiple comparison test. h: Light units relative to Empty vector in C2C12 cells 24 h after transfection of 3xMEF2 luciferase plasmid and an expression plasmid for either hFUS WT, hFUS R495X, LLPS deficient hFUS (hFUS YnCA), LLPS-deficient hFUS with SV40 NLS or empty control plasmid. Nested one-way ANOVA with Tukey’s multiple comparisons test; ***P < 0.001, **P<0.01, *P < 0.05. Each dot represents the mean of an individual experiment (n=3), each consisting of 4 technical replicates. Data represent the mean ± SEM. Expression of human wild type FUS but neither R495X nor LLPS deficient FUS increases activity of the MEF2 reporter.
    Figure Legend Snippet: a-b: Recombinant FUS protein was incubated in presence of ETV5-CFP or/and MEF2A-mCherry recombinant proteins. After immunoprecipitation using FUS antibody then pulled out with A/G-coupled magnetic beads, immunoprecipitated proteins were examined by western blot using FUS, ETV5 and MEF2A antibody. The band intensities of co-immunoprecipitated MEF2A-mCherry and ETV5-CFP were quantified using iBright Analysis Software (B). Error bars represent SEM of four independent experiments. c-d Cooperative binding assay of FUS, ETV5, MEF2A recombinant proteins to FAM labelled Mrpl30 promoter-derived DNA probe. EMSA experiments performed by using increasing concentrations of ETV5 (60, 120, 180 and 240 nM) and constant concentration of FUS (300 nM) and/or MEF2A (50 nM). Panel D shows the percentage of Mrpl30 probe bound across 3 independent experiments. The intensity of the signals of the protein- Mrpl30 probe complex was quantified using the iBright Analysis Software. Error bars represent SEM of three independent experiments. e: Representative confocal images of FUS-EGFP condensates (5 µM) in absence or presence of ETV5-CFP (3 µM) and/or MEF2A-mCherry (0.85 µM) upon protease-mediated cleavage of the MBP-solubility tags. No condensates were observed for ETV5 or MEF2A alone or mixed together in absence of FUS condensates. Bar, 10 µm. f-g: Quantification of FUS-EGFP condensate roundness (F) and size (G). Mean ± SEM of three independent replicates with at least 179 condensates in total from ≥3 different fields of view analyzed. * p<0.05, *** p<0.005 by one-way ANOVA with Tukey’s multiple comparison test. h: Light units relative to Empty vector in C2C12 cells 24 h after transfection of 3xMEF2 luciferase plasmid and an expression plasmid for either hFUS WT, hFUS R495X, LLPS deficient hFUS (hFUS YnCA), LLPS-deficient hFUS with SV40 NLS or empty control plasmid. Nested one-way ANOVA with Tukey’s multiple comparisons test; ***P < 0.001, **P<0.01, *P < 0.05. Each dot represents the mean of an individual experiment (n=3), each consisting of 4 technical replicates. Data represent the mean ± SEM. Expression of human wild type FUS but neither R495X nor LLPS deficient FUS increases activity of the MEF2 reporter.

    Techniques Used: Recombinant, Incubation, Immunoprecipitation, Magnetic Beads, Western Blot, Software, Binding Assay, Derivative Assay, Concentration Assay, Solubility, Comparison, Plasmid Preparation, Transfection, Luciferase, Expressing, Control, Activity Assay



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    a-b: <t>Recombinant</t> <t>FUS</t> protein was incubated in presence of ETV5-CFP or/and MEF2A-mCherry recombinant proteins. After immunoprecipitation using FUS antibody then pulled out with A/G-coupled magnetic beads, immunoprecipitated proteins were examined by western blot using FUS, ETV5 and MEF2A antibody. The band intensities of co-immunoprecipitated MEF2A-mCherry and ETV5-CFP were quantified using iBright Analysis Software (B). Error bars represent SEM of four independent experiments. c-d Cooperative binding assay of FUS, ETV5, MEF2A recombinant proteins to FAM labelled Mrpl30 promoter-derived DNA probe. EMSA experiments performed by using increasing concentrations of ETV5 (60, 120, 180 and 240 nM) and constant concentration of FUS (300 nM) and/or MEF2A (50 nM). Panel D shows the percentage of Mrpl30 probe bound across 3 independent experiments. The intensity of the signals of the protein- Mrpl30 probe complex was quantified using the iBright Analysis Software. Error bars represent SEM of three independent experiments. e: Representative confocal images of FUS-EGFP condensates (5 µM) in absence or presence of ETV5-CFP (3 µM) and/or MEF2A-mCherry (0.85 µM) upon protease-mediated cleavage of the MBP-solubility tags. No condensates were observed for ETV5 or MEF2A alone or mixed together in absence of FUS condensates. Bar, 10 µm. f-g: Quantification of FUS-EGFP condensate roundness (F) and size (G). Mean ± SEM of three independent replicates with at least 179 condensates in total from ≥3 different fields of view analyzed. * p<0.05, *** p<0.005 by one-way ANOVA with Tukey’s multiple comparison test. h: Light units relative to Empty vector in C2C12 cells 24 h after transfection of 3xMEF2 luciferase plasmid and an expression plasmid for either hFUS WT, hFUS R495X, LLPS deficient hFUS (hFUS YnCA), LLPS-deficient hFUS with SV40 NLS or empty control plasmid. Nested one-way ANOVA with Tukey’s multiple comparisons test; ***P < 0.001, **P<0.01, *P < 0.05. Each dot represents the mean of an individual experiment (n=3), each consisting of 4 technical replicates. Data represent the mean ± SEM. Expression of human wild type FUS but neither R495X nor LLPS deficient FUS increases activity of the MEF2 reporter.
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    ag2150 fus recombinant polypeptide 3  (Proteintech)
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    Proteintech ag2150 fus recombinant polypeptide 3
    a-b: <t>Recombinant</t> <t>FUS</t> protein was incubated in presence of ETV5-CFP or/and MEF2A-mCherry recombinant proteins. After immunoprecipitation using FUS antibody then pulled out with A/G-coupled magnetic beads, immunoprecipitated proteins were examined by western blot using FUS, ETV5 and MEF2A antibody. The band intensities of co-immunoprecipitated MEF2A-mCherry and ETV5-CFP were quantified using iBright Analysis Software (B). Error bars represent SEM of four independent experiments. c-d Cooperative binding assay of FUS, ETV5, MEF2A recombinant proteins to FAM labelled Mrpl30 promoter-derived DNA probe. EMSA experiments performed by using increasing concentrations of ETV5 (60, 120, 180 and 240 nM) and constant concentration of FUS (300 nM) and/or MEF2A (50 nM). Panel D shows the percentage of Mrpl30 probe bound across 3 independent experiments. The intensity of the signals of the protein- Mrpl30 probe complex was quantified using the iBright Analysis Software. Error bars represent SEM of three independent experiments. e: Representative confocal images of FUS-EGFP condensates (5 µM) in absence or presence of ETV5-CFP (3 µM) and/or MEF2A-mCherry (0.85 µM) upon protease-mediated cleavage of the MBP-solubility tags. No condensates were observed for ETV5 or MEF2A alone or mixed together in absence of FUS condensates. Bar, 10 µm. f-g: Quantification of FUS-EGFP condensate roundness (F) and size (G). Mean ± SEM of three independent replicates with at least 179 condensates in total from ≥3 different fields of view analyzed. * p<0.05, *** p<0.005 by one-way ANOVA with Tukey’s multiple comparison test. h: Light units relative to Empty vector in C2C12 cells 24 h after transfection of 3xMEF2 luciferase plasmid and an expression plasmid for either hFUS WT, hFUS R495X, LLPS deficient hFUS (hFUS YnCA), LLPS-deficient hFUS with SV40 NLS or empty control plasmid. Nested one-way ANOVA with Tukey’s multiple comparisons test; ***P < 0.001, **P<0.01, *P < 0.05. Each dot represents the mean of an individual experiment (n=3), each consisting of 4 technical replicates. Data represent the mean ± SEM. Expression of human wild type FUS but neither R495X nor LLPS deficient FUS increases activity of the MEF2 reporter.
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    Image Search Results


    a-b: Recombinant FUS protein was incubated in presence of ETV5-CFP or/and MEF2A-mCherry recombinant proteins. After immunoprecipitation using FUS antibody then pulled out with A/G-coupled magnetic beads, immunoprecipitated proteins were examined by western blot using FUS, ETV5 and MEF2A antibody. The band intensities of co-immunoprecipitated MEF2A-mCherry and ETV5-CFP were quantified using iBright Analysis Software (B). Error bars represent SEM of four independent experiments. c-d Cooperative binding assay of FUS, ETV5, MEF2A recombinant proteins to FAM labelled Mrpl30 promoter-derived DNA probe. EMSA experiments performed by using increasing concentrations of ETV5 (60, 120, 180 and 240 nM) and constant concentration of FUS (300 nM) and/or MEF2A (50 nM). Panel D shows the percentage of Mrpl30 probe bound across 3 independent experiments. The intensity of the signals of the protein- Mrpl30 probe complex was quantified using the iBright Analysis Software. Error bars represent SEM of three independent experiments. e: Representative confocal images of FUS-EGFP condensates (5 µM) in absence or presence of ETV5-CFP (3 µM) and/or MEF2A-mCherry (0.85 µM) upon protease-mediated cleavage of the MBP-solubility tags. No condensates were observed for ETV5 or MEF2A alone or mixed together in absence of FUS condensates. Bar, 10 µm. f-g: Quantification of FUS-EGFP condensate roundness (F) and size (G). Mean ± SEM of three independent replicates with at least 179 condensates in total from ≥3 different fields of view analyzed. * p<0.05, *** p<0.005 by one-way ANOVA with Tukey’s multiple comparison test. h: Light units relative to Empty vector in C2C12 cells 24 h after transfection of 3xMEF2 luciferase plasmid and an expression plasmid for either hFUS WT, hFUS R495X, LLPS deficient hFUS (hFUS YnCA), LLPS-deficient hFUS with SV40 NLS or empty control plasmid. Nested one-way ANOVA with Tukey’s multiple comparisons test; ***P < 0.001, **P<0.01, *P < 0.05. Each dot represents the mean of an individual experiment (n=3), each consisting of 4 technical replicates. Data represent the mean ± SEM. Expression of human wild type FUS but neither R495X nor LLPS deficient FUS increases activity of the MEF2 reporter.

    Journal: bioRxiv

    Article Title: FUS controls muscle differentiation and structure through LLPS mediated recruitment of MEF2 and ETV5

    doi: 10.1101/2024.09.18.613669

    Figure Lengend Snippet: a-b: Recombinant FUS protein was incubated in presence of ETV5-CFP or/and MEF2A-mCherry recombinant proteins. After immunoprecipitation using FUS antibody then pulled out with A/G-coupled magnetic beads, immunoprecipitated proteins were examined by western blot using FUS, ETV5 and MEF2A antibody. The band intensities of co-immunoprecipitated MEF2A-mCherry and ETV5-CFP were quantified using iBright Analysis Software (B). Error bars represent SEM of four independent experiments. c-d Cooperative binding assay of FUS, ETV5, MEF2A recombinant proteins to FAM labelled Mrpl30 promoter-derived DNA probe. EMSA experiments performed by using increasing concentrations of ETV5 (60, 120, 180 and 240 nM) and constant concentration of FUS (300 nM) and/or MEF2A (50 nM). Panel D shows the percentage of Mrpl30 probe bound across 3 independent experiments. The intensity of the signals of the protein- Mrpl30 probe complex was quantified using the iBright Analysis Software. Error bars represent SEM of three independent experiments. e: Representative confocal images of FUS-EGFP condensates (5 µM) in absence or presence of ETV5-CFP (3 µM) and/or MEF2A-mCherry (0.85 µM) upon protease-mediated cleavage of the MBP-solubility tags. No condensates were observed for ETV5 or MEF2A alone or mixed together in absence of FUS condensates. Bar, 10 µm. f-g: Quantification of FUS-EGFP condensate roundness (F) and size (G). Mean ± SEM of three independent replicates with at least 179 condensates in total from ≥3 different fields of view analyzed. * p<0.05, *** p<0.005 by one-way ANOVA with Tukey’s multiple comparison test. h: Light units relative to Empty vector in C2C12 cells 24 h after transfection of 3xMEF2 luciferase plasmid and an expression plasmid for either hFUS WT, hFUS R495X, LLPS deficient hFUS (hFUS YnCA), LLPS-deficient hFUS with SV40 NLS or empty control plasmid. Nested one-way ANOVA with Tukey’s multiple comparisons test; ***P < 0.001, **P<0.01, *P < 0.05. Each dot represents the mean of an individual experiment (n=3), each consisting of 4 technical replicates. Data represent the mean ± SEM. Expression of human wild type FUS but neither R495X nor LLPS deficient FUS increases activity of the MEF2 reporter.

    Article Snippet: FUS recombinant protein was obtained from Novus biologicals (NBP1-42462, immunoprecipitation) or Origene (# TP301808, EMSAs)).

    Techniques: Recombinant, Incubation, Immunoprecipitation, Magnetic Beads, Western Blot, Software, Binding Assay, Derivative Assay, Concentration Assay, Solubility, Comparison, Plasmid Preparation, Transfection, Luciferase, Expressing, Control, Activity Assay