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rhodamine labelled f actin  (Cytoskeleton Inc)


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    Cytoskeleton Inc rhodamine labelled f actin
    (a) Schematic of pseudo-2D actomyosin network crowded by Methylcellulose on the lipid bilayer. (b) Confocal fluorescence microscopy image of pseudo-2D actomyosin network crosslinked by fascin (top) and α-actinin (bottom) on a supported lipid bilayer. Left is before crosslinking, and right is post crosslinker addition. Scalebar is 5 µm. (c) Kymograph of the yellow dashed line in b), scalebars are 5µm (horizontal) and 10s (vertical). (d) Exemplary linescan intensity (normalized) for conditions in e. (e) Bundling metric λ of fascin and α-actinin crosslinked networks as well <t>as</t> <t>F-actin</t> network without crosslinkers. N = 3 for each condition. (f) Exemplary autocorrelation function of actin network fluctuations as function of lag time Δ t . (g) Characteristic time τ for different conditions. N = 5,3,3,3,3,3 respectively. (h) Confocal fluorescence microscopy image of 2D actomyosin network crosslinked by fascin (top) and α-actinin (bottom) deformed and contracted under myosin active stress over time. Scalebars are 20 µm. Heatmaps show accumulative strain of the final frame. Quiver plot overlay shows the instantaneous velocity. (i) Kymograph of α-actinin network rupture (dashed red line in h). Scalebars are 10µm and 10s. (j) Mean strain < ε > of the network during deformation caused by myosin induced active stress over time. The slope of the strain curve is the strain rate (k) Maximum mean strain < ε > max of fascin and α-actinin crosslinked networks at R c = 0.2. N = 3 for each condition. p fas − aa = 0.0101. (l) Strain rate of the network crosslinked by α-actinin at R c = 0.1 at various myosin concentrations. N = 2,3,3,3,2,2,2 from low to high concentration respectively.
    Rhodamine Labelled F Actin, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 95/100, based on 88 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+skeletal+f+actin/Actin+protein+rhodamine+rabbit+skeletal+muscle/bio_rxiv__64898__2026__04__22__720181-171-6-11
    Average 95 stars, based on 88 article reviews
    rhodamine labelled f actin - by Bioz Stars, 2026-09
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    Images

    1) Product Images from "Mechanical organization yields degenerate dissipation beyond linear response"

    Article Title: Mechanical organization yields degenerate dissipation beyond linear response

    Journal: bioRxiv

    doi: 10.64898/2026.04.22.720181

    (a) Schematic of pseudo-2D actomyosin network crowded by Methylcellulose on the lipid bilayer. (b) Confocal fluorescence microscopy image of pseudo-2D actomyosin network crosslinked by fascin (top) and α-actinin (bottom) on a supported lipid bilayer. Left is before crosslinking, and right is post crosslinker addition. Scalebar is 5 µm. (c) Kymograph of the yellow dashed line in b), scalebars are 5µm (horizontal) and 10s (vertical). (d) Exemplary linescan intensity (normalized) for conditions in e. (e) Bundling metric λ of fascin and α-actinin crosslinked networks as well as F-actin network without crosslinkers. N = 3 for each condition. (f) Exemplary autocorrelation function of actin network fluctuations as function of lag time Δ t . (g) Characteristic time τ for different conditions. N = 5,3,3,3,3,3 respectively. (h) Confocal fluorescence microscopy image of 2D actomyosin network crosslinked by fascin (top) and α-actinin (bottom) deformed and contracted under myosin active stress over time. Scalebars are 20 µm. Heatmaps show accumulative strain of the final frame. Quiver plot overlay shows the instantaneous velocity. (i) Kymograph of α-actinin network rupture (dashed red line in h). Scalebars are 10µm and 10s. (j) Mean strain < ε > of the network during deformation caused by myosin induced active stress over time. The slope of the strain curve is the strain rate (k) Maximum mean strain < ε > max of fascin and α-actinin crosslinked networks at R c = 0.2. N = 3 for each condition. p fas − aa = 0.0101. (l) Strain rate of the network crosslinked by α-actinin at R c = 0.1 at various myosin concentrations. N = 2,3,3,3,2,2,2 from low to high concentration respectively.
    Figure Legend Snippet: (a) Schematic of pseudo-2D actomyosin network crowded by Methylcellulose on the lipid bilayer. (b) Confocal fluorescence microscopy image of pseudo-2D actomyosin network crosslinked by fascin (top) and α-actinin (bottom) on a supported lipid bilayer. Left is before crosslinking, and right is post crosslinker addition. Scalebar is 5 µm. (c) Kymograph of the yellow dashed line in b), scalebars are 5µm (horizontal) and 10s (vertical). (d) Exemplary linescan intensity (normalized) for conditions in e. (e) Bundling metric λ of fascin and α-actinin crosslinked networks as well as F-actin network without crosslinkers. N = 3 for each condition. (f) Exemplary autocorrelation function of actin network fluctuations as function of lag time Δ t . (g) Characteristic time τ for different conditions. N = 5,3,3,3,3,3 respectively. (h) Confocal fluorescence microscopy image of 2D actomyosin network crosslinked by fascin (top) and α-actinin (bottom) deformed and contracted under myosin active stress over time. Scalebars are 20 µm. Heatmaps show accumulative strain of the final frame. Quiver plot overlay shows the instantaneous velocity. (i) Kymograph of α-actinin network rupture (dashed red line in h). Scalebars are 10µm and 10s. (j) Mean strain < ε > of the network during deformation caused by myosin induced active stress over time. The slope of the strain curve is the strain rate (k) Maximum mean strain < ε > max of fascin and α-actinin crosslinked networks at R c = 0.2. N = 3 for each condition. p fas − aa = 0.0101. (l) Strain rate of the network crosslinked by α-actinin at R c = 0.1 at various myosin concentrations. N = 2,3,3,3,2,2,2 from low to high concentration respectively.

    Techniques Used: Fluorescence, Microscopy, Concentration Assay

    Related Articles

    other:

    Article Title: Discovery of a novel cardiac-specific myosin modulator using artificial intelligence-based virtual screening
    Article Snippet: Rabbit skeletal F-actin was purchased from Cytoskeleton Inc. and prepared for experiments according to manufacturer’s instructions.

    Article Title: Discovery of a novel cardiac-specific myosin modulator using artificial intelligence-based virtual screening.
    Article Snippet: Rabbit skeletal F-actin was purchased from Cytoskeleton Inc. and prepared for experiments according to manufacturer’s instructions.

    Article Title: Site-specific acetyl-mimetic modification of cardiac troponin I modulates myofilament relaxation and calcium sensitivity
    Article Snippet: The surface was blocked with 2 mg/mL BSA, and enzymatically active myosin was bound to ~10 nM Alexa568-phalloidin-labeled rabbit skeletal F-actin (Cytoskeleton Cat. # AKL95).

    Article Title: Missense mutations in the central domains of cardiac myosin binding protein-C and their potential contribution to hypertrophic cardiomyopathy.
    Article Snippet: Received for publication, June 1, 2023, and in revised form, November 5, 2023 Published, Papers in Press, November 30, 2023, https://doi.org/10.1016/j.jbc.2023.105511 Amy Pearce, Saraswathi Ponnam, Mark R. Holt , Thomas Randall, Rylan Beckingham, Ay Lin Kho , Thomas Kampourakis, and Elisabeth Ehler* From the School of Cardiovascular and Metabolic Medicine and Sciences, British Heart Foundation Centre of Research Excellence, and Randall Centre for Cell and Molecular Biophysics (School of Basic and Biosciences), King’s College London, London, United Kingdom

    Article Title: Missense mutations in the central domains of cardiac myosin binding protein-C and their potential contribution to hypertrophic cardiomyopathy
    Article Snippet: Rabbit skeletal F-actin was purchased from Cytoskeleton, Inc and prepared for experiments according to the manufacturer’s instructions.

    Purification:

    Article Title: The impact of tropomyosins on actin filament assembly is isoform specific.
    Article Snippet: .. Increasing concentrations of Tpm (0.5–16 mM for Tpm2.1 and 0.2–6 mM for all other Tpm isoforms) were mixed with 3 mM rabbit skeletal F-actin or human cytoskeletal actin (85 % b-actin and 15 % g-actin purified from platelets, Cytoskeleton, Inc., Cat. #APHL99) in a buffer solution containing 10 mM Tris-HCl pH 7.5, 150 mM NaCl, 2 mM MgCl2 and 0.5 mM DTT in a total volume of 50 mL. .. Samples were incubated for D ow nl oa de d by [ U ni ve rs ity o f C al if or ni a, S an D ie go ] at 0 2: 55 1 8 Ju ly 2 01 6 20 min at room temperature and then centrifuged at 435,680 g for 30 min at 20 C (TLA120.1 rotor, Beckman-Coulter) to pellet F-actin and associated Tpm.



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    Image Search Results


    (a) Schematic of pseudo-2D actomyosin network crowded by Methylcellulose on the lipid bilayer. (b) Confocal fluorescence microscopy image of pseudo-2D actomyosin network crosslinked by fascin (top) and α-actinin (bottom) on a supported lipid bilayer. Left is before crosslinking, and right is post crosslinker addition. Scalebar is 5 µm. (c) Kymograph of the yellow dashed line in b), scalebars are 5µm (horizontal) and 10s (vertical). (d) Exemplary linescan intensity (normalized) for conditions in e. (e) Bundling metric λ of fascin and α-actinin crosslinked networks as well as F-actin network without crosslinkers. N = 3 for each condition. (f) Exemplary autocorrelation function of actin network fluctuations as function of lag time Δ t . (g) Characteristic time τ for different conditions. N = 5,3,3,3,3,3 respectively. (h) Confocal fluorescence microscopy image of 2D actomyosin network crosslinked by fascin (top) and α-actinin (bottom) deformed and contracted under myosin active stress over time. Scalebars are 20 µm. Heatmaps show accumulative strain of the final frame. Quiver plot overlay shows the instantaneous velocity. (i) Kymograph of α-actinin network rupture (dashed red line in h). Scalebars are 10µm and 10s. (j) Mean strain < ε > of the network during deformation caused by myosin induced active stress over time. The slope of the strain curve is the strain rate (k) Maximum mean strain < ε > max of fascin and α-actinin crosslinked networks at R c = 0.2. N = 3 for each condition. p fas − aa = 0.0101. (l) Strain rate of the network crosslinked by α-actinin at R c = 0.1 at various myosin concentrations. N = 2,3,3,3,2,2,2 from low to high concentration respectively.

    Journal: bioRxiv

    Article Title: Mechanical organization yields degenerate dissipation beyond linear response

    doi: 10.64898/2026.04.22.720181

    Figure Lengend Snippet: (a) Schematic of pseudo-2D actomyosin network crowded by Methylcellulose on the lipid bilayer. (b) Confocal fluorescence microscopy image of pseudo-2D actomyosin network crosslinked by fascin (top) and α-actinin (bottom) on a supported lipid bilayer. Left is before crosslinking, and right is post crosslinker addition. Scalebar is 5 µm. (c) Kymograph of the yellow dashed line in b), scalebars are 5µm (horizontal) and 10s (vertical). (d) Exemplary linescan intensity (normalized) for conditions in e. (e) Bundling metric λ of fascin and α-actinin crosslinked networks as well as F-actin network without crosslinkers. N = 3 for each condition. (f) Exemplary autocorrelation function of actin network fluctuations as function of lag time Δ t . (g) Characteristic time τ for different conditions. N = 5,3,3,3,3,3 respectively. (h) Confocal fluorescence microscopy image of 2D actomyosin network crosslinked by fascin (top) and α-actinin (bottom) deformed and contracted under myosin active stress over time. Scalebars are 20 µm. Heatmaps show accumulative strain of the final frame. Quiver plot overlay shows the instantaneous velocity. (i) Kymograph of α-actinin network rupture (dashed red line in h). Scalebars are 10µm and 10s. (j) Mean strain < ε > of the network during deformation caused by myosin induced active stress over time. The slope of the strain curve is the strain rate (k) Maximum mean strain < ε > max of fascin and α-actinin crosslinked networks at R c = 0.2. N = 3 for each condition. p fas − aa = 0.0101. (l) Strain rate of the network crosslinked by α-actinin at R c = 0.1 at various myosin concentrations. N = 2,3,3,3,2,2,2 from low to high concentration respectively.

    Article Snippet: Dark G-actin (Cytoskeleton) is mixed with rhodamine labelled F-actin (20% fluorescent, Cytoskeleton) to a final molar concentration of 1.4 μM, and is stabilized with 1 μM phalloidin (Cytoskeleton) and crowded to the surface of a 97% Egg Phosphatidyl Choline (Avanti Polar Lipids)/3% FITC-DHPE (Molecular Probes) phospholipid bilayer, using 0.2% 14,000 MW methyl-cellulose (Sigma, 15 cP) as a depletion agent ( ).

    Techniques: Fluorescence, Microscopy, Concentration Assay