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f actin polymerization g actin powder  (Cytoskeleton Inc)


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    Cytoskeleton Inc f actin polymerization g actin powder
    The positively charged patches at monoubiquitination sites are required for fascin bundling activity. A, sequence alignment of fascin across species. The bold and italic Us indicate optimal and suboptimal ubiquitination sites, respectively. P indicates the PKC phosphorylation site. Red dots indicate residues critical for <t>actin</t> bundling activity, as identified in a previous alanine scan mutagenesis study. B, C, and E–G, surface presentation showing electrostatic properties on the solvent-accessible surface of fascin, as derived from 3LLP using PyMOL and APBS software. β1–β4 indicate the four β-trefoil domains of fascin. Residues critical for actin bundling activity are labeled in red. The ubiquitination and phosphorylation sites are labeled as in A. The molecule in B is viewed from the N- and C-terminal plane. The three positively charged patches are marked by ovals and a circle. C, the view of fascin electrostatic surface turned 90° clockwise along the y axis relative to the view in B, with residues constituting the positively charged patch at ABS1 clearly visible. D, ribbon representation showing the salt bridge between Glu27 and Lys43 at actin binding site 1. E and F, view of fascin turned 90° counterclockwise along the y axis relative to B. F shows details of the electrostatic properties in the vicinity of the 241–250 lysine-rich loop. G shows view of fascin 90° clockwise along the x axis relative to B. H, relative actin bundling activity by wild type and mutant fascin proteins at different concentrations, as determined by low speed sedimentation assays and quantified using ImageJ.
    F Actin Polymerization G Actin Powder, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 96/100, based on 183 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/f actin polymerization g actin powder/product/Cytoskeleton Inc
    Average 96 stars, based on 183 article reviews
    f actin polymerization g actin powder - by Bioz Stars, 2026-02
    96/100 stars

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    1) Product Images from "Monoubiquitination Inhibits the Actin Bundling Activity of Fascin * "

    Article Title: Monoubiquitination Inhibits the Actin Bundling Activity of Fascin *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M116.767640

    The positively charged patches at monoubiquitination sites are required for fascin bundling activity. A, sequence alignment of fascin across species. The bold and italic Us indicate optimal and suboptimal ubiquitination sites, respectively. P indicates the PKC phosphorylation site. Red dots indicate residues critical for actin bundling activity, as identified in a previous alanine scan mutagenesis study. B, C, and E–G, surface presentation showing electrostatic properties on the solvent-accessible surface of fascin, as derived from 3LLP using PyMOL and APBS software. β1–β4 indicate the four β-trefoil domains of fascin. Residues critical for actin bundling activity are labeled in red. The ubiquitination and phosphorylation sites are labeled as in A. The molecule in B is viewed from the N- and C-terminal plane. The three positively charged patches are marked by ovals and a circle. C, the view of fascin electrostatic surface turned 90° clockwise along the y axis relative to the view in B, with residues constituting the positively charged patch at ABS1 clearly visible. D, ribbon representation showing the salt bridge between Glu27 and Lys43 at actin binding site 1. E and F, view of fascin turned 90° counterclockwise along the y axis relative to B. F shows details of the electrostatic properties in the vicinity of the 241–250 lysine-rich loop. G shows view of fascin 90° clockwise along the x axis relative to B. H, relative actin bundling activity by wild type and mutant fascin proteins at different concentrations, as determined by low speed sedimentation assays and quantified using ImageJ.
    Figure Legend Snippet: The positively charged patches at monoubiquitination sites are required for fascin bundling activity. A, sequence alignment of fascin across species. The bold and italic Us indicate optimal and suboptimal ubiquitination sites, respectively. P indicates the PKC phosphorylation site. Red dots indicate residues critical for actin bundling activity, as identified in a previous alanine scan mutagenesis study. B, C, and E–G, surface presentation showing electrostatic properties on the solvent-accessible surface of fascin, as derived from 3LLP using PyMOL and APBS software. β1–β4 indicate the four β-trefoil domains of fascin. Residues critical for actin bundling activity are labeled in red. The ubiquitination and phosphorylation sites are labeled as in A. The molecule in B is viewed from the N- and C-terminal plane. The three positively charged patches are marked by ovals and a circle. C, the view of fascin electrostatic surface turned 90° clockwise along the y axis relative to the view in B, with residues constituting the positively charged patch at ABS1 clearly visible. D, ribbon representation showing the salt bridge between Glu27 and Lys43 at actin binding site 1. E and F, view of fascin turned 90° counterclockwise along the y axis relative to B. F shows details of the electrostatic properties in the vicinity of the 241–250 lysine-rich loop. G shows view of fascin 90° clockwise along the x axis relative to B. H, relative actin bundling activity by wild type and mutant fascin proteins at different concentrations, as determined by low speed sedimentation assays and quantified using ImageJ.

    Techniques Used: Activity Assay, Sequencing, Mutagenesis, Derivative Assay, Software, Labeling, Binding Assay, Sedimentation

    Monoubiquitination inhibits fascin bundling activity. A, the effects of fascin mutations and monoubiquitination on actin bundling activity as determined by low speed sedimentation assay. The increased amount of actin in pellet and the decrease in supernatant indicate the cross-linking of actin into bundles. B, F-actin was incubated with different concentrations of wild type, mutant, or mUb-fascin at the indicated concentrations. The individual actin filaments and F-actin bundles were separated by low speed sedimentation. The relative bundling activity was quantified by densitometry measurement of SDS-PAGE gels. C and E, F-actin (2.5 μm) was incubated with fascin proteins (0.25 μm) for 1 h at room temperature, and the formation of actin bundles was visualized using fluorescence microscopy (C, after staining with Alexa 488-phalloidin) or with TEM (E, after negative staining with uranyl acetate). D, quantitation of fluorescence intensity of fluorescent micrographs from C. F, measurement of actin bundle width from E. G, TEM micrograph showing details of actin bundles cross-linked by wild type fascin (0.25 μm) or mUb-fascin (2 μm). ****, p < 0.0001 as determined by two-tailed two sample t test.
    Figure Legend Snippet: Monoubiquitination inhibits fascin bundling activity. A, the effects of fascin mutations and monoubiquitination on actin bundling activity as determined by low speed sedimentation assay. The increased amount of actin in pellet and the decrease in supernatant indicate the cross-linking of actin into bundles. B, F-actin was incubated with different concentrations of wild type, mutant, or mUb-fascin at the indicated concentrations. The individual actin filaments and F-actin bundles were separated by low speed sedimentation. The relative bundling activity was quantified by densitometry measurement of SDS-PAGE gels. C and E, F-actin (2.5 μm) was incubated with fascin proteins (0.25 μm) for 1 h at room temperature, and the formation of actin bundles was visualized using fluorescence microscopy (C, after staining with Alexa 488-phalloidin) or with TEM (E, after negative staining with uranyl acetate). D, quantitation of fluorescence intensity of fluorescent micrographs from C. F, measurement of actin bundle width from E. G, TEM micrograph showing details of actin bundles cross-linked by wild type fascin (0.25 μm) or mUb-fascin (2 μm). ****, p < 0.0001 as determined by two-tailed two sample t test.

    Techniques Used: Activity Assay, Sedimentation, Incubation, Mutagenesis, SDS Page, Fluorescence, Microscopy, Staining, Negative Staining, Quantitation Assay, Two Tailed Test

    The effects of monoubiquitination on fascin bundling dynamics. A, light scattering data showing the effects of monoubiquitination and mutations on fascin bundle formation dynamics. The increase in F-actin light scattering after incubation with fascin suggested the cross-linking of actin filaments and the increase in bundle size. B, the effects of monoubiquitination on actin bundle disassembly dynamics measured via phalloidin fluorescent staining.
    Figure Legend Snippet: The effects of monoubiquitination on fascin bundling dynamics. A, light scattering data showing the effects of monoubiquitination and mutations on fascin bundle formation dynamics. The increase in F-actin light scattering after incubation with fascin suggested the cross-linking of actin filaments and the increase in bundle size. B, the effects of monoubiquitination on actin bundle disassembly dynamics measured via phalloidin fluorescent staining.

    Techniques Used: Incubation, Staining



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    The positively charged patches at monoubiquitination sites are required for fascin bundling activity. A, sequence alignment of fascin across species. The bold and italic Us indicate optimal and suboptimal ubiquitination sites, respectively. P indicates the PKC phosphorylation site. Red dots indicate residues critical for <t>actin</t> bundling activity, as identified in a previous alanine scan mutagenesis study. B, C, and E–G, surface presentation showing electrostatic properties on the solvent-accessible surface of fascin, as derived from 3LLP using PyMOL and APBS software. β1–β4 indicate the four β-trefoil domains of fascin. Residues critical for actin bundling activity are labeled in red. The ubiquitination and phosphorylation sites are labeled as in A. The molecule in B is viewed from the N- and C-terminal plane. The three positively charged patches are marked by ovals and a circle. C, the view of fascin electrostatic surface turned 90° clockwise along the y axis relative to the view in B, with residues constituting the positively charged patch at ABS1 clearly visible. D, ribbon representation showing the salt bridge between Glu27 and Lys43 at actin binding site 1. E and F, view of fascin turned 90° counterclockwise along the y axis relative to B. F shows details of the electrostatic properties in the vicinity of the 241–250 lysine-rich loop. G shows view of fascin 90° clockwise along the x axis relative to B. H, relative actin bundling activity by wild type and mutant fascin proteins at different concentrations, as determined by low speed sedimentation assays and quantified using ImageJ.
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    The positively charged patches at monoubiquitination sites are required for fascin bundling activity. A, sequence alignment of fascin across species. The bold and italic Us indicate optimal and suboptimal ubiquitination sites, respectively. P indicates the PKC phosphorylation site. Red dots indicate residues critical for actin bundling activity, as identified in a previous alanine scan mutagenesis study. B, C, and E–G, surface presentation showing electrostatic properties on the solvent-accessible surface of fascin, as derived from 3LLP using PyMOL and APBS software. β1–β4 indicate the four β-trefoil domains of fascin. Residues critical for actin bundling activity are labeled in red. The ubiquitination and phosphorylation sites are labeled as in A. The molecule in B is viewed from the N- and C-terminal plane. The three positively charged patches are marked by ovals and a circle. C, the view of fascin electrostatic surface turned 90° clockwise along the y axis relative to the view in B, with residues constituting the positively charged patch at ABS1 clearly visible. D, ribbon representation showing the salt bridge between Glu27 and Lys43 at actin binding site 1. E and F, view of fascin turned 90° counterclockwise along the y axis relative to B. F shows details of the electrostatic properties in the vicinity of the 241–250 lysine-rich loop. G shows view of fascin 90° clockwise along the x axis relative to B. H, relative actin bundling activity by wild type and mutant fascin proteins at different concentrations, as determined by low speed sedimentation assays and quantified using ImageJ.

    Journal: The Journal of Biological Chemistry

    Article Title: Monoubiquitination Inhibits the Actin Bundling Activity of Fascin *

    doi: 10.1074/jbc.M116.767640

    Figure Lengend Snippet: The positively charged patches at monoubiquitination sites are required for fascin bundling activity. A, sequence alignment of fascin across species. The bold and italic Us indicate optimal and suboptimal ubiquitination sites, respectively. P indicates the PKC phosphorylation site. Red dots indicate residues critical for actin bundling activity, as identified in a previous alanine scan mutagenesis study. B, C, and E–G, surface presentation showing electrostatic properties on the solvent-accessible surface of fascin, as derived from 3LLP using PyMOL and APBS software. β1–β4 indicate the four β-trefoil domains of fascin. Residues critical for actin bundling activity are labeled in red. The ubiquitination and phosphorylation sites are labeled as in A. The molecule in B is viewed from the N- and C-terminal plane. The three positively charged patches are marked by ovals and a circle. C, the view of fascin electrostatic surface turned 90° clockwise along the y axis relative to the view in B, with residues constituting the positively charged patch at ABS1 clearly visible. D, ribbon representation showing the salt bridge between Glu27 and Lys43 at actin binding site 1. E and F, view of fascin turned 90° counterclockwise along the y axis relative to B. F shows details of the electrostatic properties in the vicinity of the 241–250 lysine-rich loop. G shows view of fascin 90° clockwise along the x axis relative to B. H, relative actin bundling activity by wild type and mutant fascin proteins at different concentrations, as determined by low speed sedimentation assays and quantified using ImageJ.

    Article Snippet: F-Actin Polymerization G-Actin powder was purchased from Cytoskeleton (catalog no. AKL99-C).

    Techniques: Activity Assay, Sequencing, Mutagenesis, Derivative Assay, Software, Labeling, Binding Assay, Sedimentation

    Monoubiquitination inhibits fascin bundling activity. A, the effects of fascin mutations and monoubiquitination on actin bundling activity as determined by low speed sedimentation assay. The increased amount of actin in pellet and the decrease in supernatant indicate the cross-linking of actin into bundles. B, F-actin was incubated with different concentrations of wild type, mutant, or mUb-fascin at the indicated concentrations. The individual actin filaments and F-actin bundles were separated by low speed sedimentation. The relative bundling activity was quantified by densitometry measurement of SDS-PAGE gels. C and E, F-actin (2.5 μm) was incubated with fascin proteins (0.25 μm) for 1 h at room temperature, and the formation of actin bundles was visualized using fluorescence microscopy (C, after staining with Alexa 488-phalloidin) or with TEM (E, after negative staining with uranyl acetate). D, quantitation of fluorescence intensity of fluorescent micrographs from C. F, measurement of actin bundle width from E. G, TEM micrograph showing details of actin bundles cross-linked by wild type fascin (0.25 μm) or mUb-fascin (2 μm). ****, p < 0.0001 as determined by two-tailed two sample t test.

    Journal: The Journal of Biological Chemistry

    Article Title: Monoubiquitination Inhibits the Actin Bundling Activity of Fascin *

    doi: 10.1074/jbc.M116.767640

    Figure Lengend Snippet: Monoubiquitination inhibits fascin bundling activity. A, the effects of fascin mutations and monoubiquitination on actin bundling activity as determined by low speed sedimentation assay. The increased amount of actin in pellet and the decrease in supernatant indicate the cross-linking of actin into bundles. B, F-actin was incubated with different concentrations of wild type, mutant, or mUb-fascin at the indicated concentrations. The individual actin filaments and F-actin bundles were separated by low speed sedimentation. The relative bundling activity was quantified by densitometry measurement of SDS-PAGE gels. C and E, F-actin (2.5 μm) was incubated with fascin proteins (0.25 μm) for 1 h at room temperature, and the formation of actin bundles was visualized using fluorescence microscopy (C, after staining with Alexa 488-phalloidin) or with TEM (E, after negative staining with uranyl acetate). D, quantitation of fluorescence intensity of fluorescent micrographs from C. F, measurement of actin bundle width from E. G, TEM micrograph showing details of actin bundles cross-linked by wild type fascin (0.25 μm) or mUb-fascin (2 μm). ****, p < 0.0001 as determined by two-tailed two sample t test.

    Article Snippet: F-Actin Polymerization G-Actin powder was purchased from Cytoskeleton (catalog no. AKL99-C).

    Techniques: Activity Assay, Sedimentation, Incubation, Mutagenesis, SDS Page, Fluorescence, Microscopy, Staining, Negative Staining, Quantitation Assay, Two Tailed Test

    The effects of monoubiquitination on fascin bundling dynamics. A, light scattering data showing the effects of monoubiquitination and mutations on fascin bundle formation dynamics. The increase in F-actin light scattering after incubation with fascin suggested the cross-linking of actin filaments and the increase in bundle size. B, the effects of monoubiquitination on actin bundle disassembly dynamics measured via phalloidin fluorescent staining.

    Journal: The Journal of Biological Chemistry

    Article Title: Monoubiquitination Inhibits the Actin Bundling Activity of Fascin *

    doi: 10.1074/jbc.M116.767640

    Figure Lengend Snippet: The effects of monoubiquitination on fascin bundling dynamics. A, light scattering data showing the effects of monoubiquitination and mutations on fascin bundle formation dynamics. The increase in F-actin light scattering after incubation with fascin suggested the cross-linking of actin filaments and the increase in bundle size. B, the effects of monoubiquitination on actin bundle disassembly dynamics measured via phalloidin fluorescent staining.

    Article Snippet: F-Actin Polymerization G-Actin powder was purchased from Cytoskeleton (catalog no. AKL99-C).

    Techniques: Incubation, Staining