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tirf polymerization  (Cytoskeleton Inc)


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    Cytoskeleton Inc tirf polymerization
    Tirf Polymerization, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 95/100, based on 54 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rhodamine+muscle+actin/Actin+protein+rhodamine+rabbit+skeletal+muscle/bio_rxiv__64898__2026__05__08__723880-311-1-10
    Average 95 stars, based on 54 article reviews
    tirf polymerization - by Bioz Stars, 2026-10
    95/100 stars

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    Incubation:

    Article Title: Adseverin, an actin binding protein, regulates articular chondrocyte phenotype.
    Article Snippet: This article is protected by copyright.. All rights reserved.. Chondrocytes dedifferentiate as a result of monolayer culture for cell number expansion.

    Article Title: Adseverin plays a role in osteoclast differentiation and periodontal disease-mediated bone loss.
    Article Snippet: Osteoclast differentiation and function are highly dependent on the assembly and turnover of actin filaments, but little is knownabout the roles of actinbinding proteins in these processes.. Adseverin (Ads), a member of the gelsolin superfamily of actin capping and severing proteins, regulates actinfilament turnover and can regulate the turnover of cortical actin filaments of chromaffin cells during exocytosis.Using a conditionalAds knockoutmouse model, we confirmed our previous finding in cultured cells that Ads plays a role in osteoclastogenesis (OCG) and actin cytoskeletal organization in osteoclasts.. Here we show that Ads is required for osteoclast formation and that when alveolar bone resorption is experimentally induced in mice, genetic deletion of Ads prevents osteoclast-mediated bone loss.

    Suspension:

    Article Title: Adseverin, an actin binding protein, regulates articular chondrocyte phenotype.
    Article Snippet: This article is protected by copyright.. All rights reserved.. Chondrocytes dedifferentiate as a result of monolayer culture for cell number expansion.

    Article Title: Adseverin plays a role in osteoclast differentiation and periodontal disease-mediated bone loss.
    Article Snippet: Osteoclast differentiation and function are highly dependent on the assembly and turnover of actin filaments, but little is knownabout the roles of actinbinding proteins in these processes.. Adseverin (Ads), a member of the gelsolin superfamily of actin capping and severing proteins, regulates actinfilament turnover and can regulate the turnover of cortical actin filaments of chromaffin cells during exocytosis.Using a conditionalAds knockoutmouse model, we confirmed our previous finding in cultured cells that Ads plays a role in osteoclastogenesis (OCG) and actin cytoskeletal organization in osteoclasts.. Here we show that Ads is required for osteoclast formation and that when alveolar bone resorption is experimentally induced in mice, genetic deletion of Ads prevents osteoclast-mediated bone loss.

    Staining:

    Article Title: Adseverin, an actin binding protein, regulates articular chondrocyte phenotype.
    Article Snippet: This article is protected by copyright.. All rights reserved.. Chondrocytes dedifferentiate as a result of monolayer culture for cell number expansion.



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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