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plasmid pcdna nesprin tension sensor  (Addgene inc)


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    Addgene inc plasmid pcdna nesprin tension sensor
    Cyclic stretch disrupts perinuclear heterochromatin and reduces nuclear stiffness. a) Schematic illustrating the DNA adenine methyltransferase identification (DamID) technique for visualizing lamina‐associated domains (LADs). The Dam‐Lamin B1 fusion protein introduces N 6 ‐methyladenine (m 6 A) marks at GATC motifs in genomic regions near the nuclear lamina. These methylation marks are specifically recognized by the m 6 A‐Tracer and could be detected by a GFP‐tagged DNA‐binding protein to visualize lamina‐associated domains. b) Representative confocal images of cells co‐transfected with m 6 A‐Tracer and Dam‐LMNB1, showing a reduction in LAD‐associated heterochromatin upon cyclic stretch. (Scale bar: 5 µm) c) Fluorescence intensity profiles of the m 6 A‐Tracer and DAPI along the nuclear axis. d) Representative transmission electron microscopy (TEM) images of nuclear periphery with (ST(+)) and without stretch (ST(−)). e) Quantification of heterochromatin area at the nuclear periphery based on TEM images, corresponding to LAD‐associated regions, with a schematic illustrating the measurement area. Heterochromatin loss was consistently observed across all analyzed cells. Quantification was performed within a 0.5 µm band from the nuclear edge, covering the entire nuclear periphery of each cell. Stretch‐induced loss of peripheral heterochromatin and increased nuclear wrinkling. (Scale bar: 2 µm; n = 15). f) Schematic depiction of the fluorescence resonance energy transfer (FRET)‐based <t>Nesprin‐2</t> tension sensor (TS), a critical element of the LINC complex. g,h) FRET analysis shows increased FRET efficiency in stretched cells, indicating reduced membrane tension. Scale bar: 5 µm. ( n = 9). i,j) Atomic force microscopy (AFM) force indentation experiments reveal softening of the nucleus in the ST(+) group compared to ST(−). ( n = 7). Statistical significance is denoted as * p < 0.5 and ** p < 0.01, determined by Student's t ‐test. All experiments were conducted right after 15 min of stretching.
    Plasmid Pcdna Nesprin Tension Sensor, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/plasmid+pcdna+nesprin+tension+sensor/pmc12850466-251-6-12?v=Addgene+inc
    Average 93 stars, based on 12 article reviews
    plasmid pcdna nesprin tension sensor - by Bioz Stars, 2026-08
    93/100 stars

    Images

    1) Product Images from "Temporal Stretch‐Induced Nuclear Mechanosensing Coordinates Early Chromatin Accessibility and Genome Protection"

    Article Title: Temporal Stretch‐Induced Nuclear Mechanosensing Coordinates Early Chromatin Accessibility and Genome Protection

    Journal: Advanced Science

    doi: 10.1002/advs.202510554

    Cyclic stretch disrupts perinuclear heterochromatin and reduces nuclear stiffness. a) Schematic illustrating the DNA adenine methyltransferase identification (DamID) technique for visualizing lamina‐associated domains (LADs). The Dam‐Lamin B1 fusion protein introduces N 6 ‐methyladenine (m 6 A) marks at GATC motifs in genomic regions near the nuclear lamina. These methylation marks are specifically recognized by the m 6 A‐Tracer and could be detected by a GFP‐tagged DNA‐binding protein to visualize lamina‐associated domains. b) Representative confocal images of cells co‐transfected with m 6 A‐Tracer and Dam‐LMNB1, showing a reduction in LAD‐associated heterochromatin upon cyclic stretch. (Scale bar: 5 µm) c) Fluorescence intensity profiles of the m 6 A‐Tracer and DAPI along the nuclear axis. d) Representative transmission electron microscopy (TEM) images of nuclear periphery with (ST(+)) and without stretch (ST(−)). e) Quantification of heterochromatin area at the nuclear periphery based on TEM images, corresponding to LAD‐associated regions, with a schematic illustrating the measurement area. Heterochromatin loss was consistently observed across all analyzed cells. Quantification was performed within a 0.5 µm band from the nuclear edge, covering the entire nuclear periphery of each cell. Stretch‐induced loss of peripheral heterochromatin and increased nuclear wrinkling. (Scale bar: 2 µm; n = 15). f) Schematic depiction of the fluorescence resonance energy transfer (FRET)‐based Nesprin‐2 tension sensor (TS), a critical element of the LINC complex. g,h) FRET analysis shows increased FRET efficiency in stretched cells, indicating reduced membrane tension. Scale bar: 5 µm. ( n = 9). i,j) Atomic force microscopy (AFM) force indentation experiments reveal softening of the nucleus in the ST(+) group compared to ST(−). ( n = 7). Statistical significance is denoted as * p < 0.5 and ** p < 0.01, determined by Student's t ‐test. All experiments were conducted right after 15 min of stretching.
    Figure Legend Snippet: Cyclic stretch disrupts perinuclear heterochromatin and reduces nuclear stiffness. a) Schematic illustrating the DNA adenine methyltransferase identification (DamID) technique for visualizing lamina‐associated domains (LADs). The Dam‐Lamin B1 fusion protein introduces N 6 ‐methyladenine (m 6 A) marks at GATC motifs in genomic regions near the nuclear lamina. These methylation marks are specifically recognized by the m 6 A‐Tracer and could be detected by a GFP‐tagged DNA‐binding protein to visualize lamina‐associated domains. b) Representative confocal images of cells co‐transfected with m 6 A‐Tracer and Dam‐LMNB1, showing a reduction in LAD‐associated heterochromatin upon cyclic stretch. (Scale bar: 5 µm) c) Fluorescence intensity profiles of the m 6 A‐Tracer and DAPI along the nuclear axis. d) Representative transmission electron microscopy (TEM) images of nuclear periphery with (ST(+)) and without stretch (ST(−)). e) Quantification of heterochromatin area at the nuclear periphery based on TEM images, corresponding to LAD‐associated regions, with a schematic illustrating the measurement area. Heterochromatin loss was consistently observed across all analyzed cells. Quantification was performed within a 0.5 µm band from the nuclear edge, covering the entire nuclear periphery of each cell. Stretch‐induced loss of peripheral heterochromatin and increased nuclear wrinkling. (Scale bar: 2 µm; n = 15). f) Schematic depiction of the fluorescence resonance energy transfer (FRET)‐based Nesprin‐2 tension sensor (TS), a critical element of the LINC complex. g,h) FRET analysis shows increased FRET efficiency in stretched cells, indicating reduced membrane tension. Scale bar: 5 µm. ( n = 9). i,j) Atomic force microscopy (AFM) force indentation experiments reveal softening of the nucleus in the ST(+) group compared to ST(−). ( n = 7). Statistical significance is denoted as * p < 0.5 and ** p < 0.01, determined by Student's t ‐test. All experiments were conducted right after 15 min of stretching.

    Techniques Used: Methylation, Binding Assay, Transfection, Fluorescence, Transmission Assay, Electron Microscopy, Förster Resonance Energy Transfer, Membrane, Microscopy



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    Cyclic stretch disrupts perinuclear heterochromatin and reduces nuclear stiffness. a) Schematic illustrating the DNA adenine methyltransferase identification (DamID) technique for visualizing lamina‐associated domains (LADs). The Dam‐Lamin B1 fusion protein introduces N 6 ‐methyladenine (m 6 A) marks at GATC motifs in genomic regions near the nuclear lamina. These methylation marks are specifically recognized by the m 6 A‐Tracer and could be detected by a GFP‐tagged DNA‐binding protein to visualize lamina‐associated domains. b) Representative confocal images of cells co‐transfected with m 6 A‐Tracer and Dam‐LMNB1, showing a reduction in LAD‐associated heterochromatin upon cyclic stretch. (Scale bar: 5 µm) c) Fluorescence intensity profiles of the m 6 A‐Tracer and DAPI along the nuclear axis. d) Representative transmission electron microscopy (TEM) images of nuclear periphery with (ST(+)) and without stretch (ST(−)). e) Quantification of heterochromatin area at the nuclear periphery based on TEM images, corresponding to LAD‐associated regions, with a schematic illustrating the measurement area. Heterochromatin loss was consistently observed across all analyzed cells. Quantification was performed within a 0.5 µm band from the nuclear edge, covering the entire nuclear periphery of each cell. Stretch‐induced loss of peripheral heterochromatin and increased nuclear wrinkling. (Scale bar: 2 µm; n = 15). f) Schematic depiction of the fluorescence resonance energy transfer (FRET)‐based <t>Nesprin‐2</t> tension sensor (TS), a critical element of the LINC complex. g,h) FRET analysis shows increased FRET efficiency in stretched cells, indicating reduced membrane tension. Scale bar: 5 µm. ( n = 9). i,j) Atomic force microscopy (AFM) force indentation experiments reveal softening of the nucleus in the ST(+) group compared to ST(−). ( n = 7). Statistical significance is denoted as * p < 0.5 and ** p < 0.01, determined by Student's t ‐test. All experiments were conducted right after 15 min of stretching.
    Plasmid Pcdna Nesprin Tension Sensor, supplied by Addgene 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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    Cyclic stretch disrupts perinuclear heterochromatin and reduces nuclear stiffness. a) Schematic illustrating the DNA adenine methyltransferase identification (DamID) technique for visualizing lamina‐associated domains (LADs). The Dam‐Lamin B1 fusion protein introduces N 6 ‐methyladenine (m 6 A) marks at GATC motifs in genomic regions near the nuclear lamina. These methylation marks are specifically recognized by the m 6 A‐Tracer and could be detected by a GFP‐tagged DNA‐binding protein to visualize lamina‐associated domains. b) Representative confocal images of cells co‐transfected with m 6 A‐Tracer and Dam‐LMNB1, showing a reduction in LAD‐associated heterochromatin upon cyclic stretch. (Scale bar: 5 µm) c) Fluorescence intensity profiles of the m 6 A‐Tracer and DAPI along the nuclear axis. d) Representative transmission electron microscopy (TEM) images of nuclear periphery with (ST(+)) and without stretch (ST(−)). e) Quantification of heterochromatin area at the nuclear periphery based on TEM images, corresponding to LAD‐associated regions, with a schematic illustrating the measurement area. Heterochromatin loss was consistently observed across all analyzed cells. Quantification was performed within a 0.5 µm band from the nuclear edge, covering the entire nuclear periphery of each cell. Stretch‐induced loss of peripheral heterochromatin and increased nuclear wrinkling. (Scale bar: 2 µm; n = 15). f) Schematic depiction of the fluorescence resonance energy transfer (FRET)‐based <t>Nesprin‐2</t> tension sensor (TS), a critical element of the LINC complex. g,h) FRET analysis shows increased FRET efficiency in stretched cells, indicating reduced membrane tension. Scale bar: 5 µm. ( n = 9). i,j) Atomic force microscopy (AFM) force indentation experiments reveal softening of the nucleus in the ST(+) group compared to ST(−). ( n = 7). Statistical significance is denoted as * p < 0.5 and ** p < 0.01, determined by Student's t ‐test. All experiments were conducted right after 15 min of stretching.
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    Cyclic stretch disrupts perinuclear heterochromatin and reduces nuclear stiffness. a) Schematic illustrating the DNA adenine methyltransferase identification (DamID) technique for visualizing lamina‐associated domains (LADs). The Dam‐Lamin B1 fusion protein introduces N 6 ‐methyladenine (m 6 A) marks at GATC motifs in genomic regions near the nuclear lamina. These methylation marks are specifically recognized by the m 6 A‐Tracer and could be detected by a GFP‐tagged DNA‐binding protein to visualize lamina‐associated domains. b) Representative confocal images of cells co‐transfected with m 6 A‐Tracer and Dam‐LMNB1, showing a reduction in LAD‐associated heterochromatin upon cyclic stretch. (Scale bar: 5 µm) c) Fluorescence intensity profiles of the m 6 A‐Tracer and DAPI along the nuclear axis. d) Representative transmission electron microscopy (TEM) images of nuclear periphery with (ST(+)) and without stretch (ST(−)). e) Quantification of heterochromatin area at the nuclear periphery based on TEM images, corresponding to LAD‐associated regions, with a schematic illustrating the measurement area. Heterochromatin loss was consistently observed across all analyzed cells. Quantification was performed within a 0.5 µm band from the nuclear edge, covering the entire nuclear periphery of each cell. Stretch‐induced loss of peripheral heterochromatin and increased nuclear wrinkling. (Scale bar: 2 µm; n = 15). f) Schematic depiction of the fluorescence resonance energy transfer (FRET)‐based <t>Nesprin‐2</t> tension sensor (TS), a critical element of the LINC complex. g,h) FRET analysis shows increased FRET efficiency in stretched cells, indicating reduced membrane tension. Scale bar: 5 µm. ( n = 9). i,j) Atomic force microscopy (AFM) force indentation experiments reveal softening of the nucleus in the ST(+) group compared to ST(−). ( n = 7). Statistical significance is denoted as * p < 0.5 and ** p < 0.01, determined by Student's t ‐test. All experiments were conducted right after 15 min of stretching.
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    Image Search Results


    Cyclic stretch disrupts perinuclear heterochromatin and reduces nuclear stiffness. a) Schematic illustrating the DNA adenine methyltransferase identification (DamID) technique for visualizing lamina‐associated domains (LADs). The Dam‐Lamin B1 fusion protein introduces N 6 ‐methyladenine (m 6 A) marks at GATC motifs in genomic regions near the nuclear lamina. These methylation marks are specifically recognized by the m 6 A‐Tracer and could be detected by a GFP‐tagged DNA‐binding protein to visualize lamina‐associated domains. b) Representative confocal images of cells co‐transfected with m 6 A‐Tracer and Dam‐LMNB1, showing a reduction in LAD‐associated heterochromatin upon cyclic stretch. (Scale bar: 5 µm) c) Fluorescence intensity profiles of the m 6 A‐Tracer and DAPI along the nuclear axis. d) Representative transmission electron microscopy (TEM) images of nuclear periphery with (ST(+)) and without stretch (ST(−)). e) Quantification of heterochromatin area at the nuclear periphery based on TEM images, corresponding to LAD‐associated regions, with a schematic illustrating the measurement area. Heterochromatin loss was consistently observed across all analyzed cells. Quantification was performed within a 0.5 µm band from the nuclear edge, covering the entire nuclear periphery of each cell. Stretch‐induced loss of peripheral heterochromatin and increased nuclear wrinkling. (Scale bar: 2 µm; n = 15). f) Schematic depiction of the fluorescence resonance energy transfer (FRET)‐based Nesprin‐2 tension sensor (TS), a critical element of the LINC complex. g,h) FRET analysis shows increased FRET efficiency in stretched cells, indicating reduced membrane tension. Scale bar: 5 µm. ( n = 9). i,j) Atomic force microscopy (AFM) force indentation experiments reveal softening of the nucleus in the ST(+) group compared to ST(−). ( n = 7). Statistical significance is denoted as * p < 0.5 and ** p < 0.01, determined by Student's t ‐test. All experiments were conducted right after 15 min of stretching.

    Journal: Advanced Science

    Article Title: Temporal Stretch‐Induced Nuclear Mechanosensing Coordinates Early Chromatin Accessibility and Genome Protection

    doi: 10.1002/advs.202510554

    Figure Lengend Snippet: Cyclic stretch disrupts perinuclear heterochromatin and reduces nuclear stiffness. a) Schematic illustrating the DNA adenine methyltransferase identification (DamID) technique for visualizing lamina‐associated domains (LADs). The Dam‐Lamin B1 fusion protein introduces N 6 ‐methyladenine (m 6 A) marks at GATC motifs in genomic regions near the nuclear lamina. These methylation marks are specifically recognized by the m 6 A‐Tracer and could be detected by a GFP‐tagged DNA‐binding protein to visualize lamina‐associated domains. b) Representative confocal images of cells co‐transfected with m 6 A‐Tracer and Dam‐LMNB1, showing a reduction in LAD‐associated heterochromatin upon cyclic stretch. (Scale bar: 5 µm) c) Fluorescence intensity profiles of the m 6 A‐Tracer and DAPI along the nuclear axis. d) Representative transmission electron microscopy (TEM) images of nuclear periphery with (ST(+)) and without stretch (ST(−)). e) Quantification of heterochromatin area at the nuclear periphery based on TEM images, corresponding to LAD‐associated regions, with a schematic illustrating the measurement area. Heterochromatin loss was consistently observed across all analyzed cells. Quantification was performed within a 0.5 µm band from the nuclear edge, covering the entire nuclear periphery of each cell. Stretch‐induced loss of peripheral heterochromatin and increased nuclear wrinkling. (Scale bar: 2 µm; n = 15). f) Schematic depiction of the fluorescence resonance energy transfer (FRET)‐based Nesprin‐2 tension sensor (TS), a critical element of the LINC complex. g,h) FRET analysis shows increased FRET efficiency in stretched cells, indicating reduced membrane tension. Scale bar: 5 µm. ( n = 9). i,j) Atomic force microscopy (AFM) force indentation experiments reveal softening of the nucleus in the ST(+) group compared to ST(−). ( n = 7). Statistical significance is denoted as * p < 0.5 and ** p < 0.01, determined by Student's t ‐test. All experiments were conducted right after 15 min of stretching.

    Article Snippet: To assess cell membrane tension, the plasmid pcDNA Nesprin tension sensor (TS, Addgene, #68127) was employed, harboring TFP, an elastin linker, and Venus.

    Techniques: Methylation, Binding Assay, Transfection, Fluorescence, Transmission Assay, Electron Microscopy, Förster Resonance Energy Transfer, Membrane, Microscopy