Review



rhodamine labeled actin ar05  (Cytoskeleton Inc)


Bioz Verified Symbol Cytoskeleton Inc is a verified supplier
Bioz Manufacturer Symbol Cytoskeleton Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 95
      Buy from Supplier

    Structured Review

    Cytoskeleton Inc rhodamine labeled actin ar05
    Rhodamine Labeled Actin Ar05, 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/ar05/Actin+protein+rhodamine+rabbit+skeletal+muscle/bio_rxiv__64898__2026__05__08__723880-311-4-10
    Average 95 stars, based on 88 article reviews
    rhodamine labeled actin ar05 - by Bioz Stars, 2026-09
    95/100 stars

    Images

    Related Articles

    Labeling:

    Article Title: Reconstitution of Phase-Separated Signaling Clusters and Actin Polymerization on Supported Lipid Bilayers
    Article Snippet: Actin (>99% pure) from Rabbit Skeletal Muscle , Cytoskeleton, Inc. , Cat# AKL99. .. Actin protein (Rhodamine labeled) , Cytoskeleton, Inc. , Cat# AR05. .. Arp2/3 Protein Complex: Porcine Brain , Cytoskeleton, Inc. , Cat# RP01P.

    other:

    Article Title: Mechanosensing through direct binding of tensed F-actin by LIM domains
    Article Snippet: Rhodamine-labeled G-actin (Rabbit skeletal muscle) , Cytoskeleton , Cat# AR05.



    Similar Products

    rhodamine labeled actin ar05  (Cytoskeleton Inc)
    95
    Cytoskeleton Inc rhodamine labeled actin ar05
    Rhodamine Labeled Actin Ar05, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ar05/Actin+protein+rhodamine+rabbit+skeletal+muscle/bio_rxiv__64898__2026__05__08__723880-311-4-10
    Average 95 stars, based on 1 article reviews
    rhodamine labeled actin ar05 - by Bioz Stars, 2026-09
    95/100 stars
    		  Buy from Supplier
    tirf polymerization  (Cytoskeleton Inc)
    95
    Cytoskeleton Inc tirf polymerization
    Tirf Polymerization, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ar05/Actin+protein+rhodamine+rabbit+skeletal+muscle/bio_rxiv__64898__2026__05__08__723880-311-1-10
    Average 95 stars, based on 1 article reviews
    tirf polymerization - by Bioz Stars, 2026-09
    95/100 stars
    		  Buy from Supplier
    actin protein rhodamine rabbit skeletal muscle  (Cytoskeleton Inc)
    95
    Cytoskeleton Inc actin protein rhodamine rabbit skeletal muscle
    Actin Protein Rhodamine Rabbit Skeletal Muscle, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ar05/Actin+protein+rhodamine+rabbit+skeletal+muscle/custom%40ar05%4010%2E64898%2F2026%2E05%2E08%2E723880
    Average 95 stars, based on 1 article reviews
    actin protein rhodamine rabbit skeletal muscle - by Bioz Stars, 2026-09
    95/100 stars
    		  Buy from Supplier
    rhodamine labelled f actin  (Cytoskeleton Inc)
    95
    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 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ar05/Actin+protein+rhodamine+rabbit+skeletal+muscle/bio_rxiv__64898__2026__04__22__720181-171-6-11
    Average 95 stars, based on 1 article reviews
    rhodamine labelled f actin - by Bioz Stars, 2026-09
    95/100 stars
    		  Buy from Supplier
    rhodamine labelled rabbit skeletal muscle g actin  (Cytoskeleton Inc)
    95
    Cytoskeleton Inc rhodamine labelled rabbit skeletal muscle g 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 Rabbit Skeletal Muscle G Actin, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ar05/Actin+protein+rhodamine+rabbit+skeletal+muscle/pm42020745-665-95-100
    Average 95 stars, based on 1 article reviews
    rhodamine labelled rabbit skeletal muscle g actin - by Bioz Stars, 2026-09
    95/100 stars
    		  Buy from Supplier
    rhodamine g actin  (Cytoskeleton Inc)
    95
    Cytoskeleton Inc rhodamine g 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 G Actin, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ar05/Actin+protein+rhodamine+rabbit+skeletal+muscle/pm42020745-651-20-22
    Average 95 stars, based on 1 article reviews
    rhodamine g actin - by Bioz Stars, 2026-09
    95/100 stars
    		  Buy from Supplier
    rhodamine actin  (Cytoskeleton Inc)
    95
    Cytoskeleton Inc rhodamine 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 Actin, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ar05/Actin+protein+rhodamine+rabbit+skeletal+muscle/pmc13106796-259-9-11
    Average 95 stars, based on 1 article reviews
    rhodamine actin - by Bioz Stars, 2026-09
    95/100 stars
    		  Buy from Supplier

    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