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time lapsed llsm image sequences  (Oxford Instruments)


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    Oxford Instruments time lapsed llsm image sequences
    Time Lapsed Llsm Image Sequences, supplied by Oxford Instruments, used in various techniques. Bioz Stars score: 99/100, based on 44196 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/time+lapse+image+sequences/Imaris/10__1091_slash_mbc__e21___11___0537-306-0-7
    Average 99 stars, based on 44196 article reviews
    time lapsed llsm image sequences - by Bioz Stars, 2026-09
    99/100 stars

    Images

    Related Articles

    Generated:

    Article Title: A protease-dependent mechanism for initiating T-dependent B cell responses to large particulate antigens
    Article Snippet: The maximum intensity z-projection time-lapse image sequences were generated with MetaMorph software (Molecular Devices). .. 3-D rotations and time-lapse image sequences were generated in Imaris 5.7.2 ×64 (Bitplane, St. Paul, MN). .. Semi-automated cell tracking in 3-D was verified manually with Imaris 5.7.2 ×64.

    Article Title: Interactions between programmed death-1 and programmed death ligand-1 promote tolerance by blocking the T cell receptor-induced stop signal
    Article Snippet: The maximum intensity z-projection time-lapse image sequences were generated with MetaMorph software (Molecular Devices). .. 3-D rotations and time-lapse image sequences were generated in Imaris 5.7.2 ×64 (Bitplane). ..

    Article Title: A protease-dependent mechanism for initiating T-dependent B cell responses to large particulate antigens.
    Article Snippet: The maximum intensity z-projection time-lapse image sequences were generated with MetaMorph software (Molecular Devices, Sunnyvale, CA). .. Three-dimensional rotations and time-lapse image sequences were generated in Imaris 5.7.2 x64 (Bitplane, St. Paul, MN). .. Semiautomated cell tracking in three dimensions was verified manually with Imaris 5.7.2 x64.

    Imaging:

    Article Title: CCL3 promotes germinal center B cells sampling by follicular regulatory T cells
    Article Snippet: Images were acquired by Leica Advanced Fluorescent Suite (Leica Microsystems). .. Analysis of the imaging data and generation of 3D rotations and time-lapse image sequences were performed using Imaris 7.6.5 × 64 (Bitplane). ..

    Article Title: CCL3 Promotes Germinal Center B Cells Sampling by Follicular Regulatory T Cells in Murine Lymph Nodes.
    Article Snippet: Each xy plane spanned 435 × 435μm and with z spacing ranging from 2 to 3μm detecting emission wavelengths of 430–450 nm (second harmonic emission of collagen), 465–500 nm (for CFP+ cells), 520–550 nm (for GFP+ cells), and >560 nm (for tdTomato+ cells), every 20– 25 s. Images were acquired by Leica Advanced Fluorescent Suite (Leica Microsystems). .. Analysis of the imaging data and generation of 3D rotations and time-lapse image sequences were performed using Imaris 7.6.5 × 64 (Bitplane). ..

    Article Title: CCL3 Promotes Germinal Center B Cells Sampling by Follicular Regulatory T Cells in Murine Lymph Nodes
    Article Snippet: Each xy plane spanned 435 × 435 μm and with z spacing ranging from 2 to 3 μm detecting emission wavelengths of 430–450 nm (second harmonic emission of collagen), 465–500 nm (for CFP + cells), 520–550 nm (for GFP + cells), and >560 nm (for tdTomato + cells), every 20–25 s. Images were acquired by Leica Advanced Fluorescent Suite (Leica Microsystems). .. Analysis of the imaging data and generation of 3D rotations and time-lapse image sequences were performed using Imaris 7.6.5 × 64 (Bitplane). ..

    Single-particle Tracking:

    Article Title: Loss of lamin A function increases chromatin dynamics in the nuclear interior
    Article Snippet: .. Quantitative SPT analysis of time-lapse image sequences was performed using the Imaris (Bitplane) image analysis software package for locating coordinates of labelled genomic loci. ..

    Software:

    Article Title: Loss of lamin A function increases chromatin dynamics in the nuclear interior
    Article Snippet: .. Quantitative SPT analysis of time-lapse image sequences was performed using the Imaris (Bitplane) image analysis software package for locating coordinates of labelled genomic loci. ..



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    time lapsed llsm image sequences  (Oxford Instruments)
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    time lapse tirfm imaging sequences  (Nikon)
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    A <t>TIRFM</t> visualization of actin filaments polymerizing on PEG-biotin-NeutrAvidin functionalized cover glass. Polymerization of 1 µM G-actin (20% TMR + 10% biotin labelled) was induced by KMEI (50 mM KCl, 1 mM MgCl 2 , 1 mM EGTA, 10 mM imidazole, pH 7.0) at t = 0 s, in the presence of 25 µM ATP. Representative time-lapses shown for: 1 µM G-actin (top), 1 µM G-actin + 1 µM M15(wt) (middle), and 1 µM G-actin + 1 µM mutant M15(jd) (bottom). B Quantification of actin filament density shows delayed nucleation activity of MYO15A in the presence of ATP. n = 3 independent determinations. C Kymographs of actin filament elongation. D Barbed-end elongation rates for G-actin + KMEI (red, n = 69 filaments), G-actin + M15(wt) (blue, n = 94), G-actin + M15(jd) (green, n = 80). E Elongation rate data (from D ) re-binned before nucleation, G-actin alone ( n = 69 filaments), G-actin + M15(wt) ( n = 54), G-actin + M15(jd) ( n = 40). F Elongation rate data (from D ) re-binned after nucleation, G-actin alone ( n = 69 filaments), G-actin + M15(wt) ( n = 40), G-actin + M15(jd) ( n = 40). The G-actin + KMEI control data set (from D ) is reproduced identically as a comparator in ( E , F ). G Time-lapse of actin filament polymerization induced by KMEI at t = 0 s, with no ATP in solution. G-actin (ATP) monomers were prepared by desalting into ATP-free G-buffer. H Actin filament density shows nucleation activity of MYO15A is accelerated in the absence of ATP. G-actin + KMEI ( n = 4 determinations), G-actin + M15(wt) ( n = 5), G-actin + M15(jd) ( n = 5). I Barbed-end filament rates in the absence of free ATP. Reaction deadtimes were typically 50 s and included in quantification. TIRFM images are shown as inverted grayscale. G-actin + KMEI ( n = 40 filaments), G-actin + M15(wt) ( n = 40), G-actin + M15(jd) ( n = 47). All data are plotted as mean ± SD. Statistics were computed using two-way ANOVA with Dunnett’s multiple comparisons test ( B , H ), and one-way ANOVA (Kruskal–Wallis) with Dunn’s multiple comparisons test ( D , E , F , I ). Statistical significance is denoted by ****, P < 0.0001, ***, P < 0.001, **, P < 0.01. Scale bars are 10 µm ( A , G ). Data are from 3 to 5 experimental determinations ( A – F ), and 4–5 experimental determinations ( G – I ), using 2 independent protein preparations.
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    time-lapse imaging sequences  (Mendeley Ltd)
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    A <t>TIRFM</t> visualization of actin filaments polymerizing on PEG-biotin-NeutrAvidin functionalized cover glass. Polymerization of 1 µM G-actin (20% TMR + 10% biotin labelled) was induced by KMEI (50 mM KCl, 1 mM MgCl 2 , 1 mM EGTA, 10 mM imidazole, pH 7.0) at t = 0 s, in the presence of 25 µM ATP. Representative time-lapses shown for: 1 µM G-actin (top), 1 µM G-actin + 1 µM M15(wt) (middle), and 1 µM G-actin + 1 µM mutant M15(jd) (bottom). B Quantification of actin filament density shows delayed nucleation activity of MYO15A in the presence of ATP. n = 3 independent determinations. C Kymographs of actin filament elongation. D Barbed-end elongation rates for G-actin + KMEI (red, n = 69 filaments), G-actin + M15(wt) (blue, n = 94), G-actin + M15(jd) (green, n = 80). E Elongation rate data (from D ) re-binned before nucleation, G-actin alone ( n = 69 filaments), G-actin + M15(wt) ( n = 54), G-actin + M15(jd) ( n = 40). F Elongation rate data (from D ) re-binned after nucleation, G-actin alone ( n = 69 filaments), G-actin + M15(wt) ( n = 40), G-actin + M15(jd) ( n = 40). The G-actin + KMEI control data set (from D ) is reproduced identically as a comparator in ( E , F ). G Time-lapse of actin filament polymerization induced by KMEI at t = 0 s, with no ATP in solution. G-actin (ATP) monomers were prepared by desalting into ATP-free G-buffer. H Actin filament density shows nucleation activity of MYO15A is accelerated in the absence of ATP. G-actin + KMEI ( n = 4 determinations), G-actin + M15(wt) ( n = 5), G-actin + M15(jd) ( n = 5). I Barbed-end filament rates in the absence of free ATP. Reaction deadtimes were typically 50 s and included in quantification. TIRFM images are shown as inverted grayscale. G-actin + KMEI ( n = 40 filaments), G-actin + M15(wt) ( n = 40), G-actin + M15(jd) ( n = 47). All data are plotted as mean ± SD. Statistics were computed using two-way ANOVA with Dunnett’s multiple comparisons test ( B , H ), and one-way ANOVA (Kruskal–Wallis) with Dunn’s multiple comparisons test ( D , E , F , I ). Statistical significance is denoted by ****, P < 0.0001, ***, P < 0.001, **, P < 0.01. Scale bars are 10 µm ( A , G ). Data are from 3 to 5 experimental determinations ( A – F ), and 4–5 experimental determinations ( G – I ), using 2 independent protein preparations.
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    time lapse image sequences  (Oxford Instruments)
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    A <t>TIRFM</t> visualization of actin filaments polymerizing on PEG-biotin-NeutrAvidin functionalized cover glass. Polymerization of 1 µM G-actin (20% TMR + 10% biotin labelled) was induced by KMEI (50 mM KCl, 1 mM MgCl 2 , 1 mM EGTA, 10 mM imidazole, pH 7.0) at t = 0 s, in the presence of 25 µM ATP. Representative time-lapses shown for: 1 µM G-actin (top), 1 µM G-actin + 1 µM M15(wt) (middle), and 1 µM G-actin + 1 µM mutant M15(jd) (bottom). B Quantification of actin filament density shows delayed nucleation activity of MYO15A in the presence of ATP. n = 3 independent determinations. C Kymographs of actin filament elongation. D Barbed-end elongation rates for G-actin + KMEI (red, n = 69 filaments), G-actin + M15(wt) (blue, n = 94), G-actin + M15(jd) (green, n = 80). E Elongation rate data (from D ) re-binned before nucleation, G-actin alone ( n = 69 filaments), G-actin + M15(wt) ( n = 54), G-actin + M15(jd) ( n = 40). F Elongation rate data (from D ) re-binned after nucleation, G-actin alone ( n = 69 filaments), G-actin + M15(wt) ( n = 40), G-actin + M15(jd) ( n = 40). The G-actin + KMEI control data set (from D ) is reproduced identically as a comparator in ( E , F ). G Time-lapse of actin filament polymerization induced by KMEI at t = 0 s, with no ATP in solution. G-actin (ATP) monomers were prepared by desalting into ATP-free G-buffer. H Actin filament density shows nucleation activity of MYO15A is accelerated in the absence of ATP. G-actin + KMEI ( n = 4 determinations), G-actin + M15(wt) ( n = 5), G-actin + M15(jd) ( n = 5). I Barbed-end filament rates in the absence of free ATP. Reaction deadtimes were typically 50 s and included in quantification. TIRFM images are shown as inverted grayscale. G-actin + KMEI ( n = 40 filaments), G-actin + M15(wt) ( n = 40), G-actin + M15(jd) ( n = 47). All data are plotted as mean ± SD. Statistics were computed using two-way ANOVA with Dunnett’s multiple comparisons test ( B , H ), and one-way ANOVA (Kruskal–Wallis) with Dunn’s multiple comparisons test ( D , E , F , I ). Statistical significance is denoted by ****, P < 0.0001, ***, P < 0.001, **, P < 0.01. Scale bars are 10 µm ( A , G ). Data are from 3 to 5 experimental determinations ( A – F ), and 4–5 experimental determinations ( G – I ), using 2 independent protein preparations.
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    z stack time lapse image sequences  (Oxford Instruments)
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    Oxford Instruments z stack time lapse image sequences
    A <t>TIRFM</t> visualization of actin filaments polymerizing on PEG-biotin-NeutrAvidin functionalized cover glass. Polymerization of 1 µM G-actin (20% TMR + 10% biotin labelled) was induced by KMEI (50 mM KCl, 1 mM MgCl 2 , 1 mM EGTA, 10 mM imidazole, pH 7.0) at t = 0 s, in the presence of 25 µM ATP. Representative time-lapses shown for: 1 µM G-actin (top), 1 µM G-actin + 1 µM M15(wt) (middle), and 1 µM G-actin + 1 µM mutant M15(jd) (bottom). B Quantification of actin filament density shows delayed nucleation activity of MYO15A in the presence of ATP. n = 3 independent determinations. C Kymographs of actin filament elongation. D Barbed-end elongation rates for G-actin + KMEI (red, n = 69 filaments), G-actin + M15(wt) (blue, n = 94), G-actin + M15(jd) (green, n = 80). E Elongation rate data (from D ) re-binned before nucleation, G-actin alone ( n = 69 filaments), G-actin + M15(wt) ( n = 54), G-actin + M15(jd) ( n = 40). F Elongation rate data (from D ) re-binned after nucleation, G-actin alone ( n = 69 filaments), G-actin + M15(wt) ( n = 40), G-actin + M15(jd) ( n = 40). The G-actin + KMEI control data set (from D ) is reproduced identically as a comparator in ( E , F ). G Time-lapse of actin filament polymerization induced by KMEI at t = 0 s, with no ATP in solution. G-actin (ATP) monomers were prepared by desalting into ATP-free G-buffer. H Actin filament density shows nucleation activity of MYO15A is accelerated in the absence of ATP. G-actin + KMEI ( n = 4 determinations), G-actin + M15(wt) ( n = 5), G-actin + M15(jd) ( n = 5). I Barbed-end filament rates in the absence of free ATP. Reaction deadtimes were typically 50 s and included in quantification. TIRFM images are shown as inverted grayscale. G-actin + KMEI ( n = 40 filaments), G-actin + M15(wt) ( n = 40), G-actin + M15(jd) ( n = 47). All data are plotted as mean ± SD. Statistics were computed using two-way ANOVA with Dunnett’s multiple comparisons test ( B , H ), and one-way ANOVA (Kruskal–Wallis) with Dunn’s multiple comparisons test ( D , E , F , I ). Statistical significance is denoted by ****, P < 0.0001, ***, P < 0.001, **, P < 0.01. Scale bars are 10 µm ( A , G ). Data are from 3 to 5 experimental determinations ( A – F ), and 4–5 experimental determinations ( G – I ), using 2 independent protein preparations.
    Z Stack Time Lapse Image Sequences, supplied by Oxford Instruments, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/time+lapse+image+sequences/Imaris/pmc06400558-378-9-16
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    Image Search Results


    A TIRFM visualization of actin filaments polymerizing on PEG-biotin-NeutrAvidin functionalized cover glass. Polymerization of 1 µM G-actin (20% TMR + 10% biotin labelled) was induced by KMEI (50 mM KCl, 1 mM MgCl 2 , 1 mM EGTA, 10 mM imidazole, pH 7.0) at t = 0 s, in the presence of 25 µM ATP. Representative time-lapses shown for: 1 µM G-actin (top), 1 µM G-actin + 1 µM M15(wt) (middle), and 1 µM G-actin + 1 µM mutant M15(jd) (bottom). B Quantification of actin filament density shows delayed nucleation activity of MYO15A in the presence of ATP. n = 3 independent determinations. C Kymographs of actin filament elongation. D Barbed-end elongation rates for G-actin + KMEI (red, n = 69 filaments), G-actin + M15(wt) (blue, n = 94), G-actin + M15(jd) (green, n = 80). E Elongation rate data (from D ) re-binned before nucleation, G-actin alone ( n = 69 filaments), G-actin + M15(wt) ( n = 54), G-actin + M15(jd) ( n = 40). F Elongation rate data (from D ) re-binned after nucleation, G-actin alone ( n = 69 filaments), G-actin + M15(wt) ( n = 40), G-actin + M15(jd) ( n = 40). The G-actin + KMEI control data set (from D ) is reproduced identically as a comparator in ( E , F ). G Time-lapse of actin filament polymerization induced by KMEI at t = 0 s, with no ATP in solution. G-actin (ATP) monomers were prepared by desalting into ATP-free G-buffer. H Actin filament density shows nucleation activity of MYO15A is accelerated in the absence of ATP. G-actin + KMEI ( n = 4 determinations), G-actin + M15(wt) ( n = 5), G-actin + M15(jd) ( n = 5). I Barbed-end filament rates in the absence of free ATP. Reaction deadtimes were typically 50 s and included in quantification. TIRFM images are shown as inverted grayscale. G-actin + KMEI ( n = 40 filaments), G-actin + M15(wt) ( n = 40), G-actin + M15(jd) ( n = 47). All data are plotted as mean ± SD. Statistics were computed using two-way ANOVA with Dunnett’s multiple comparisons test ( B , H ), and one-way ANOVA (Kruskal–Wallis) with Dunn’s multiple comparisons test ( D , E , F , I ). Statistical significance is denoted by ****, P < 0.0001, ***, P < 0.001, **, P < 0.01. Scale bars are 10 µm ( A , G ). Data are from 3 to 5 experimental determinations ( A – F ), and 4–5 experimental determinations ( G – I ), using 2 independent protein preparations.

    Journal: Nature Communications

    Article Title: Myosin-based nucleation of actin filaments contributes to stereocilia development critical for hearing

    doi: 10.1038/s41467-025-55898-8

    Figure Lengend Snippet: A TIRFM visualization of actin filaments polymerizing on PEG-biotin-NeutrAvidin functionalized cover glass. Polymerization of 1 µM G-actin (20% TMR + 10% biotin labelled) was induced by KMEI (50 mM KCl, 1 mM MgCl 2 , 1 mM EGTA, 10 mM imidazole, pH 7.0) at t = 0 s, in the presence of 25 µM ATP. Representative time-lapses shown for: 1 µM G-actin (top), 1 µM G-actin + 1 µM M15(wt) (middle), and 1 µM G-actin + 1 µM mutant M15(jd) (bottom). B Quantification of actin filament density shows delayed nucleation activity of MYO15A in the presence of ATP. n = 3 independent determinations. C Kymographs of actin filament elongation. D Barbed-end elongation rates for G-actin + KMEI (red, n = 69 filaments), G-actin + M15(wt) (blue, n = 94), G-actin + M15(jd) (green, n = 80). E Elongation rate data (from D ) re-binned before nucleation, G-actin alone ( n = 69 filaments), G-actin + M15(wt) ( n = 54), G-actin + M15(jd) ( n = 40). F Elongation rate data (from D ) re-binned after nucleation, G-actin alone ( n = 69 filaments), G-actin + M15(wt) ( n = 40), G-actin + M15(jd) ( n = 40). The G-actin + KMEI control data set (from D ) is reproduced identically as a comparator in ( E , F ). G Time-lapse of actin filament polymerization induced by KMEI at t = 0 s, with no ATP in solution. G-actin (ATP) monomers were prepared by desalting into ATP-free G-buffer. H Actin filament density shows nucleation activity of MYO15A is accelerated in the absence of ATP. G-actin + KMEI ( n = 4 determinations), G-actin + M15(wt) ( n = 5), G-actin + M15(jd) ( n = 5). I Barbed-end filament rates in the absence of free ATP. Reaction deadtimes were typically 50 s and included in quantification. TIRFM images are shown as inverted grayscale. G-actin + KMEI ( n = 40 filaments), G-actin + M15(wt) ( n = 40), G-actin + M15(jd) ( n = 47). All data are plotted as mean ± SD. Statistics were computed using two-way ANOVA with Dunnett’s multiple comparisons test ( B , H ), and one-way ANOVA (Kruskal–Wallis) with Dunn’s multiple comparisons test ( D , E , F , I ). Statistical significance is denoted by ****, P < 0.0001, ***, P < 0.001, **, P < 0.01. Scale bars are 10 µm ( A , G ). Data are from 3 to 5 experimental determinations ( A – F ), and 4–5 experimental determinations ( G – I ), using 2 independent protein preparations.

    Article Snippet: Filament elongation rates were calculated from time-lapse TIRFM imaging sequences using kymographs generated in NIS-Elements Software (version 5.2, Nikon).

    Techniques: Mutagenesis, Activity Assay, Control