rabbit skeletal muscle Search Results


non fluorescent actin  (Cytoskeleton Inc)
96
Cytoskeleton Inc non fluorescent actin
Non Fluorescent Actin, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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hc growth supplement  (Cell Applications Inc)
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Cell Applications Inc hc growth supplement
Hc Growth Supplement, supplied by Cell Applications Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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actin protein  (Cytoskeleton Inc)
95
Cytoskeleton Inc actin protein
Actin Protein, 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
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rhodamine actin  (Cytoskeleton Inc)
94
Cytoskeleton Inc rhodamine actin
Rhodamine Actin, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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α actinin  (Cytoskeleton Inc)
94
Cytoskeleton Inc α actinin
a Schematic of <t>the</t> <t>α-actinin</t> crosslinked actin network under varying α-actinin concentration. b Time-lapse images of actomyosin contraction at 80 nM myosin and 6 µM actin (left) with 0.6 µM α-actinin (center) or 2.4 µM α-actinin (right), with NADH fluorescence (bottom). c NADH fluorescence over time, normalized to the initial time point ( n = 7 droplets, N = 3 independent experiments in NADH only; n = 12, N = 6 in [α-actinin]/[Actin] = 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). d Boxplot showing ATP consumption rate from ( c ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). e Actomyosin network contraction (left) at 80 nM myosin, [α-actinin][Actin] = 0.1; black arrows indicate total displacement over 10 min, with local apparent strain fields shown on the right. f Mean compressive apparent strain of the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). g Instantaneous power performed by myosin on the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). h Mean inferred mechanical power averaged over 10 min in ( g ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). i Mean inferred mechanical power vs. energy consumption rate ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 11, N = 5 in 1). Data are presented as mean ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; n.s. not significant. Scale bars, 10 μm.
α Actinin, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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unlabeled rabbit skeletal muscle actin  (Cytoskeleton Inc)
94
Cytoskeleton Inc unlabeled rabbit skeletal muscle actin
a Schematic of <t>the</t> <t>α-actinin</t> crosslinked actin network under varying α-actinin concentration. b Time-lapse images of actomyosin contraction at 80 nM myosin and 6 µM actin (left) with 0.6 µM α-actinin (center) or 2.4 µM α-actinin (right), with NADH fluorescence (bottom). c NADH fluorescence over time, normalized to the initial time point ( n = 7 droplets, N = 3 independent experiments in NADH only; n = 12, N = 6 in [α-actinin]/[Actin] = 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). d Boxplot showing ATP consumption rate from ( c ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). e Actomyosin network contraction (left) at 80 nM myosin, [α-actinin][Actin] = 0.1; black arrows indicate total displacement over 10 min, with local apparent strain fields shown on the right. f Mean compressive apparent strain of the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). g Instantaneous power performed by myosin on the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). h Mean inferred mechanical power averaged over 10 min in ( g ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). i Mean inferred mechanical power vs. energy consumption rate ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 11, N = 5 in 1). Data are presented as mean ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; n.s. not significant. Scale bars, 10 μm.
Unlabeled Rabbit Skeletal Muscle Actin, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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skeletal muscle myosin ii  (Cytoskeleton Inc)
94
Cytoskeleton Inc skeletal muscle myosin ii
a Schematic of <t>the</t> <t>α-actinin</t> crosslinked actin network under varying α-actinin concentration. b Time-lapse images of actomyosin contraction at 80 nM myosin and 6 µM actin (left) with 0.6 µM α-actinin (center) or 2.4 µM α-actinin (right), with NADH fluorescence (bottom). c NADH fluorescence over time, normalized to the initial time point ( n = 7 droplets, N = 3 independent experiments in NADH only; n = 12, N = 6 in [α-actinin]/[Actin] = 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). d Boxplot showing ATP consumption rate from ( c ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). e Actomyosin network contraction (left) at 80 nM myosin, [α-actinin][Actin] = 0.1; black arrows indicate total displacement over 10 min, with local apparent strain fields shown on the right. f Mean compressive apparent strain of the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). g Instantaneous power performed by myosin on the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). h Mean inferred mechanical power averaged over 10 min in ( g ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). i Mean inferred mechanical power vs. energy consumption rate ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 11, N = 5 in 1). Data are presented as mean ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; n.s. not significant. Scale bars, 10 μm.
Skeletal Muscle Myosin Ii, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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actin polymerization biochem kit  (Cytoskeleton Inc)
95
Cytoskeleton Inc actin polymerization biochem kit
a Schematic of <t>the</t> <t>α-actinin</t> crosslinked actin network under varying α-actinin concentration. b Time-lapse images of actomyosin contraction at 80 nM myosin and 6 µM actin (left) with 0.6 µM α-actinin (center) or 2.4 µM α-actinin (right), with NADH fluorescence (bottom). c NADH fluorescence over time, normalized to the initial time point ( n = 7 droplets, N = 3 independent experiments in NADH only; n = 12, N = 6 in [α-actinin]/[Actin] = 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). d Boxplot showing ATP consumption rate from ( c ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). e Actomyosin network contraction (left) at 80 nM myosin, [α-actinin][Actin] = 0.1; black arrows indicate total displacement over 10 min, with local apparent strain fields shown on the right. f Mean compressive apparent strain of the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). g Instantaneous power performed by myosin on the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). h Mean inferred mechanical power averaged over 10 min in ( g ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). i Mean inferred mechanical power vs. energy consumption rate ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 11, N = 5 in 1). Data are presented as mean ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; n.s. not significant. Scale bars, 10 μm.
Actin Polymerization Biochem Kit, 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
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rabbit skeletal muscle actin  (Cytoskeleton Inc)
94
Cytoskeleton Inc rabbit skeletal muscle actin
a Schematic of <t>the</t> <t>α-actinin</t> crosslinked actin network under varying α-actinin concentration. b Time-lapse images of actomyosin contraction at 80 nM myosin and 6 µM actin (left) with 0.6 µM α-actinin (center) or 2.4 µM α-actinin (right), with NADH fluorescence (bottom). c NADH fluorescence over time, normalized to the initial time point ( n = 7 droplets, N = 3 independent experiments in NADH only; n = 12, N = 6 in [α-actinin]/[Actin] = 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). d Boxplot showing ATP consumption rate from ( c ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). e Actomyosin network contraction (left) at 80 nM myosin, [α-actinin][Actin] = 0.1; black arrows indicate total displacement over 10 min, with local apparent strain fields shown on the right. f Mean compressive apparent strain of the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). g Instantaneous power performed by myosin on the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). h Mean inferred mechanical power averaged over 10 min in ( g ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). i Mean inferred mechanical power vs. energy consumption rate ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 11, N = 5 in 1). Data are presented as mean ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; n.s. not significant. Scale bars, 10 μm.
Rabbit Skeletal Muscle Actin, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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protein biochem kit bk001  (Cytoskeleton Inc)
93
Cytoskeleton Inc protein biochem kit bk001
a Schematic of <t>the</t> <t>α-actinin</t> crosslinked actin network under varying α-actinin concentration. b Time-lapse images of actomyosin contraction at 80 nM myosin and 6 µM actin (left) with 0.6 µM α-actinin (center) or 2.4 µM α-actinin (right), with NADH fluorescence (bottom). c NADH fluorescence over time, normalized to the initial time point ( n = 7 droplets, N = 3 independent experiments in NADH only; n = 12, N = 6 in [α-actinin]/[Actin] = 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). d Boxplot showing ATP consumption rate from ( c ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). e Actomyosin network contraction (left) at 80 nM myosin, [α-actinin][Actin] = 0.1; black arrows indicate total displacement over 10 min, with local apparent strain fields shown on the right. f Mean compressive apparent strain of the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). g Instantaneous power performed by myosin on the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). h Mean inferred mechanical power averaged over 10 min in ( g ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). i Mean inferred mechanical power vs. energy consumption rate ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 11, N = 5 in 1). Data are presented as mean ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; n.s. not significant. Scale bars, 10 μm.
Protein Biochem Kit Bk001, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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actin polymerization rabbit skeletal muscle actin  (Cytoskeleton Inc)
93
Cytoskeleton Inc actin polymerization rabbit skeletal muscle actin
a Schematic of <t>the</t> <t>α-actinin</t> crosslinked actin network under varying α-actinin concentration. b Time-lapse images of actomyosin contraction at 80 nM myosin and 6 µM actin (left) with 0.6 µM α-actinin (center) or 2.4 µM α-actinin (right), with NADH fluorescence (bottom). c NADH fluorescence over time, normalized to the initial time point ( n = 7 droplets, N = 3 independent experiments in NADH only; n = 12, N = 6 in [α-actinin]/[Actin] = 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). d Boxplot showing ATP consumption rate from ( c ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). e Actomyosin network contraction (left) at 80 nM myosin, [α-actinin][Actin] = 0.1; black arrows indicate total displacement over 10 min, with local apparent strain fields shown on the right. f Mean compressive apparent strain of the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). g Instantaneous power performed by myosin on the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). h Mean inferred mechanical power averaged over 10 min in ( g ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). i Mean inferred mechanical power vs. energy consumption rate ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 11, N = 5 in 1). Data are presented as mean ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; n.s. not significant. Scale bars, 10 μm.
Actin Polymerization Rabbit Skeletal Muscle Actin, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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rabbit skeletal heavy meromyosin  (Cytoskeleton Inc)
95
Cytoskeleton Inc rabbit skeletal heavy meromyosin
a Schematic of <t>the</t> <t>α-actinin</t> crosslinked actin network under varying α-actinin concentration. b Time-lapse images of actomyosin contraction at 80 nM myosin and 6 µM actin (left) with 0.6 µM α-actinin (center) or 2.4 µM α-actinin (right), with NADH fluorescence (bottom). c NADH fluorescence over time, normalized to the initial time point ( n = 7 droplets, N = 3 independent experiments in NADH only; n = 12, N = 6 in [α-actinin]/[Actin] = 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). d Boxplot showing ATP consumption rate from ( c ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). e Actomyosin network contraction (left) at 80 nM myosin, [α-actinin][Actin] = 0.1; black arrows indicate total displacement over 10 min, with local apparent strain fields shown on the right. f Mean compressive apparent strain of the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). g Instantaneous power performed by myosin on the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). h Mean inferred mechanical power averaged over 10 min in ( g ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). i Mean inferred mechanical power vs. energy consumption rate ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 11, N = 5 in 1). Data are presented as mean ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; n.s. not significant. Scale bars, 10 μm.
Rabbit Skeletal Heavy Meromyosin, 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
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Image Search Results


a Schematic of the α-actinin crosslinked actin network under varying α-actinin concentration. b Time-lapse images of actomyosin contraction at 80 nM myosin and 6 µM actin (left) with 0.6 µM α-actinin (center) or 2.4 µM α-actinin (right), with NADH fluorescence (bottom). c NADH fluorescence over time, normalized to the initial time point ( n = 7 droplets, N = 3 independent experiments in NADH only; n = 12, N = 6 in [α-actinin]/[Actin] = 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). d Boxplot showing ATP consumption rate from ( c ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). e Actomyosin network contraction (left) at 80 nM myosin, [α-actinin][Actin] = 0.1; black arrows indicate total displacement over 10 min, with local apparent strain fields shown on the right. f Mean compressive apparent strain of the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). g Instantaneous power performed by myosin on the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). h Mean inferred mechanical power averaged over 10 min in ( g ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). i Mean inferred mechanical power vs. energy consumption rate ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 11, N = 5 in 1). Data are presented as mean ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; n.s. not significant. Scale bars, 10 μm.

Journal: Communications Biology

Article Title: Crosslinked F-actin networks regulate load-dependent energy conversion

doi: 10.1038/s42003-026-09843-0

Figure Lengend Snippet: a Schematic of the α-actinin crosslinked actin network under varying α-actinin concentration. b Time-lapse images of actomyosin contraction at 80 nM myosin and 6 µM actin (left) with 0.6 µM α-actinin (center) or 2.4 µM α-actinin (right), with NADH fluorescence (bottom). c NADH fluorescence over time, normalized to the initial time point ( n = 7 droplets, N = 3 independent experiments in NADH only; n = 12, N = 6 in [α-actinin]/[Actin] = 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). d Boxplot showing ATP consumption rate from ( c ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). e Actomyosin network contraction (left) at 80 nM myosin, [α-actinin][Actin] = 0.1; black arrows indicate total displacement over 10 min, with local apparent strain fields shown on the right. f Mean compressive apparent strain of the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). g Instantaneous power performed by myosin on the actin network over time ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). h Mean inferred mechanical power averaged over 10 min in ( g ) ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 14, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 12, N = 5 in 1). i Mean inferred mechanical power vs. energy consumption rate ( n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 11, N = 5 in 1). Data are presented as mean ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; n.s. not significant. Scale bars, 10 μm.

Article Snippet: In the experiments assembling crosslinked actin network, fascin (CS-FSC01; Cytoskeleton Inc.), Fimbrin (Methods), α-actinin (AT01; Cytoskeleton Inc.), and Filamin (8312-01; Hypermol) were used at varied concentrations.

Techniques: Concentration Assay, Fluorescence

a Boxplot showing relative duty ratio for α-actinin crosslinked network normalized by the mean of no-crosslinked condition. Duty ratio is estimated from the inverse of myosin ATPase activity ( n = 12 droplets, N = 6 independent experiments in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). b Boxplot showing relative duty ratio for fascin crosslinked network normalized by the mean of no-crosslinked condition ( n = 7, N = 4 in 0; n = 11, N = 6 in 0.01; n = 6, N = 3 in 0.1; n = 8, N = 4 in 0.4; n = 10, N = 5 in 1). c Boxplot showing relative duty ratio for fimbrin crosslinked network normalized by the mean of no-crosslinked condition ( n = 6, N = 3 in 0; n = 5, N = 3 in 0.01; n = 11, N = 6 in 0.1; n = 6, N = 3 in 0.4; n = 10, N = 6 in 1). d Boxplot showing relative duty ratio for filamin crosslinked network normalized by the mean of no-crosslinked condition ( n = 6, N = 3 in 0; n = 5, N = 3 in 0.01; n = 11, N = 6 in 0.04; n = 9, N = 6 in 0.1; n = 11, N = 5 in 1). e Relative inferred mechanical power, normalized by the mean of no-crosslinked condition, dependence on various crosslinker concentrations. Sample size is the same as ( a – d ). Inset is the boxplots showing relative power at [Crosslinker]/[Actin] = 1 ( n = 11, N = 5 in α-actinin; n = 10, N = 5 in fascin; n = 10, N = 6 in fimbrin; n = 11, N = 5 in filamin). f Summary of the crosslinker-induced load-dependence of inferred mechanical power. Fascin and filamin-crosslinked networks allow strongly load-dependent inferred mechanical power, whereas fimbrin and α-actinin-crosslinked networks allow weakly load-dependent inferred mechanical power. g Relative inferred mechanical power vs relative energy consumption rate on various crosslinkers (α-actinin: n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 11, N = 5 in 1; fascin: n = 7, N = 4 in 0; n = 9, N = 6 in 0.01; n = 6, N = 3 in 0.1; n = 7, N = 4 in 0.4; n = 10, N = 5 in 1; fimbrin: n = 6, N = 3 in 0; n = 5, N = 3 in 0.01; n = 11, N = 6 in 0.1; n = 6, N = 3 in 0.4; n = 10, N = 6 in 1; filamin: n = 6, N = 3 in 0; n = 5, N = 3 in 0.01; n = 9, N = 6 in 0.04; n = 9, N = 6 in 0.1; n = 11, N = 5 in 1). h Schematic summarizing crosslinker-induced control of inferred mechanical power and ATP consumption rate by myosin. Data are presented as mean ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; n.s. not significant. Scale bars, 10 μm.

Journal: Communications Biology

Article Title: Crosslinked F-actin networks regulate load-dependent energy conversion

doi: 10.1038/s42003-026-09843-0

Figure Lengend Snippet: a Boxplot showing relative duty ratio for α-actinin crosslinked network normalized by the mean of no-crosslinked condition. Duty ratio is estimated from the inverse of myosin ATPase activity ( n = 12 droplets, N = 6 independent experiments in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 17, N = 10 in 0.4; n = 11, N = 5 in 1). b Boxplot showing relative duty ratio for fascin crosslinked network normalized by the mean of no-crosslinked condition ( n = 7, N = 4 in 0; n = 11, N = 6 in 0.01; n = 6, N = 3 in 0.1; n = 8, N = 4 in 0.4; n = 10, N = 5 in 1). c Boxplot showing relative duty ratio for fimbrin crosslinked network normalized by the mean of no-crosslinked condition ( n = 6, N = 3 in 0; n = 5, N = 3 in 0.01; n = 11, N = 6 in 0.1; n = 6, N = 3 in 0.4; n = 10, N = 6 in 1). d Boxplot showing relative duty ratio for filamin crosslinked network normalized by the mean of no-crosslinked condition ( n = 6, N = 3 in 0; n = 5, N = 3 in 0.01; n = 11, N = 6 in 0.04; n = 9, N = 6 in 0.1; n = 11, N = 5 in 1). e Relative inferred mechanical power, normalized by the mean of no-crosslinked condition, dependence on various crosslinker concentrations. Sample size is the same as ( a – d ). Inset is the boxplots showing relative power at [Crosslinker]/[Actin] = 1 ( n = 11, N = 5 in α-actinin; n = 10, N = 5 in fascin; n = 10, N = 6 in fimbrin; n = 11, N = 5 in filamin). f Summary of the crosslinker-induced load-dependence of inferred mechanical power. Fascin and filamin-crosslinked networks allow strongly load-dependent inferred mechanical power, whereas fimbrin and α-actinin-crosslinked networks allow weakly load-dependent inferred mechanical power. g Relative inferred mechanical power vs relative energy consumption rate on various crosslinkers (α-actinin: n = 12, N = 6 in 0; n = 10, N = 5 in 0.01; n = 11, N = 8 in 0.1; n = 14, N = 10 in 0.4; n = 11, N = 5 in 1; fascin: n = 7, N = 4 in 0; n = 9, N = 6 in 0.01; n = 6, N = 3 in 0.1; n = 7, N = 4 in 0.4; n = 10, N = 5 in 1; fimbrin: n = 6, N = 3 in 0; n = 5, N = 3 in 0.01; n = 11, N = 6 in 0.1; n = 6, N = 3 in 0.4; n = 10, N = 6 in 1; filamin: n = 6, N = 3 in 0; n = 5, N = 3 in 0.01; n = 9, N = 6 in 0.04; n = 9, N = 6 in 0.1; n = 11, N = 5 in 1). h Schematic summarizing crosslinker-induced control of inferred mechanical power and ATP consumption rate by myosin. Data are presented as mean ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; n.s. not significant. Scale bars, 10 μm.

Article Snippet: In the experiments assembling crosslinked actin network, fascin (CS-FSC01; Cytoskeleton Inc.), Fimbrin (Methods), α-actinin (AT01; Cytoskeleton Inc.), and Filamin (8312-01; Hypermol) were used at varied concentrations.

Techniques: Activity Assay, Control