Review





Similar Products

time lapsed llsm image sequences  (Oxford Instruments)
99
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 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/time lapsed llsm image sequences/product/Oxford Instruments
Average 99 stars, based on 1 article reviews
time lapsed llsm image sequences - by Bioz Stars, 2026-04
99/100 stars
  Buy from Supplier
time lapse image sequences  (Nikon)
99
Nikon time lapse image sequences
Time Lapse Image Sequences, supplied by Nikon, 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/result/time lapse image sequences/product/Nikon
Average 99 stars, based on 1 article reviews
time lapse image sequences - by Bioz Stars, 2026-04
99/100 stars
  Buy from Supplier
time lapse tirfm imaging sequences  (Nikon)
99
Nikon time lapse tirfm imaging 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.
Time Lapse Tirfm Imaging Sequences, supplied by Nikon, 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/result/time lapse tirfm imaging sequences/product/Nikon
Average 99 stars, based on 1 article reviews
time lapse tirfm imaging sequences - by Bioz Stars, 2026-04
99/100 stars
  Buy from Supplier
a1 eclipse ti2 e time lapse sequence images  (Nikon)
99
Nikon a1 eclipse ti2 e time lapse sequence images
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.
A1 Eclipse Ti2 E Time Lapse Sequence Images, supplied by Nikon, 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/result/a1 eclipse ti2 e time lapse sequence images/product/Nikon
Average 99 stars, based on 1 article reviews
a1 eclipse ti2 e time lapse sequence images - by Bioz Stars, 2026-04
99/100 stars
  Buy from Supplier
time-lapse imaging sequences  (Mendeley Ltd)
90
Mendeley Ltd time-lapse imaging 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.
Time Lapse Imaging Sequences, supplied by Mendeley Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/time-lapse imaging sequences/product/Mendeley Ltd
Average 90 stars, based on 1 article reviews
time-lapse imaging sequences - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
time lapse image sequences  (Oxford Instruments)
99
Oxford Instruments 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.
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/result/time lapse image sequences/product/Oxford Instruments
Average 99 stars, based on 1 article reviews
time lapse image sequences - by Bioz Stars, 2026-04
99/100 stars
  Buy from Supplier
z stack time lapse image sequences  (Oxford Instruments)
99
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/result/z stack time lapse image sequences/product/Oxford Instruments
Average 99 stars, based on 1 article reviews
z stack time lapse image sequences - by Bioz Stars, 2026-04
99/100 stars
  Buy from Supplier

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