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lifetime fluorescence imaging attachment  (Lambert Instruments BV)


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    Lambert Instruments BV lifetime fluorescence imaging attachment
    Lifetime Fluorescence Imaging Attachment, supplied by Lambert Instruments BV, 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/product/lifetime+fluorescence+imaging+attachment/us12251383-1101-7-11?v=Lambert+Instruments+BV
    Average 90 stars, based on 1 article reviews
    lifetime fluorescence imaging attachment - by Bioz Stars, 2026-08
    90/100 stars

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    Lambert Instruments BV lifetime fluorescence imaging attachment
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    Lambert Instruments BV fluorescence lifetime imaging attachment
    a Effect of L5UR expression (24 h) on Gal1/C-RBD FRET (donor:acceptor plasmid ratio = 1:3); n = 3. b Effect of L5UR expression (24 h) on Gal1-augmented H-RasG12V nanoclustering-FRET (donor:acceptor plasmid ratio = 1:3); n = 3. c Immunoblot data from pull-down assay with biotinylated L5UR and purified Gal1, GST-B-RBD or GST-only control with example blots (left) and quantification of repeat data (right); n = 3. d Binding of 10 nM F-L5UR to GST-B-RBD detected in a <t>fluorescence</t> polarization assay; n = 3. e Displacement of F-L5UR (10 nM) from GST-B-RBD (15 µM) by L5UR-derived peptides; n = 3. f Sequences of L5UR-derived peptides as used for in vitro and in cellulo assays. The stretch of the core peptide is highlighted in blue, mutations are in red.
    Fluorescence Lifetime Imaging Attachment, supplied by Lambert Instruments BV, 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/product/lifetime+fluorescence+imaging+attachment/pmc11233548-340-9-13?v=Lambert+Instruments+BV
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    Lambert Instruments BV lifetime fluorescence imaging attachment lambert instruments
    FLIM-FRET analysis demonstrating obscurin regulation of ankyrin complex formation in cells. Pseudocolored images showing average CFP lifetime (τav) of (A) obscurin-CFP alone (negative control) or sarcolipin-CFP-YFP (positive control), (B) obscurin-CFP (donor) with acceptors sAnk1.5-YFP or AnkG107-YFP, and (C) sAnk1.5-CFP (donor) with acceptor AnkG107-YFP alone or with wild-type (WT) or mutant (ΔABD1&2) obscurin-HA. Scale bar represents 20 μm. (D) HA and GFP immunoblots demonstrate similar expression of donor, acceptor, and obscurin constructs between WT and mutant (ΔABDs) obscurin conditions. (E) The graph shows mean <t>fluorescence</t> lifetime of CFP (n ≥ 70 per condition per experiment from three independent experiments (biological replicates, n = 3)). Error bars represent standard error of the mean. Using ordinary one-way ANOVA and Tukey’s multiple comparison post hoc test, statistical analysis was performed separately (denoted by dotted line) on measurements from A and B, then C (**** represents p-values of <0.0001).
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    Nikon fluorescence lifetime imaging microscopy (flim) attachment
    Phasor plots: ( A ) the <t>fluorescence</t> <t>lifetime</t> <t>imaging</t> microscopy phasor plot of rhodamine 6G 5 μM and ( B ) sample No 1 with rhodamine 6G 5 μM as a reference.
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    Average 90 stars, based on 1 article reviews
    fluorescence lifetime imaging microscopy (flim) attachment - by Bioz Stars, 2026-08
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    a Effect of L5UR expression (24 h) on Gal1/C-RBD FRET (donor:acceptor plasmid ratio = 1:3); n = 3. b Effect of L5UR expression (24 h) on Gal1-augmented H-RasG12V nanoclustering-FRET (donor:acceptor plasmid ratio = 1:3); n = 3. c Immunoblot data from pull-down assay with biotinylated L5UR and purified Gal1, GST-B-RBD or GST-only control with example blots (left) and quantification of repeat data (right); n = 3. d Binding of 10 nM F-L5UR to GST-B-RBD detected in a fluorescence polarization assay; n = 3. e Displacement of F-L5UR (10 nM) from GST-B-RBD (15 µM) by L5UR-derived peptides; n = 3. f Sequences of L5UR-derived peptides as used for in vitro and in cellulo assays. The stretch of the core peptide is highlighted in blue, mutations are in red.

    Journal: Communications Biology

    Article Title: Identification of an H-Ras nanocluster disrupting peptide

    doi: 10.1038/s42003-024-06523-9

    Figure Lengend Snippet: a Effect of L5UR expression (24 h) on Gal1/C-RBD FRET (donor:acceptor plasmid ratio = 1:3); n = 3. b Effect of L5UR expression (24 h) on Gal1-augmented H-RasG12V nanoclustering-FRET (donor:acceptor plasmid ratio = 1:3); n = 3. c Immunoblot data from pull-down assay with biotinylated L5UR and purified Gal1, GST-B-RBD or GST-only control with example blots (left) and quantification of repeat data (right); n = 3. d Binding of 10 nM F-L5UR to GST-B-RBD detected in a fluorescence polarization assay; n = 3. e Displacement of F-L5UR (10 nM) from GST-B-RBD (15 µM) by L5UR-derived peptides; n = 3. f Sequences of L5UR-derived peptides as used for in vitro and in cellulo assays. The stretch of the core peptide is highlighted in blue, mutations are in red.

    Article Snippet: An inverted microscope (Zeiss AXIO Observer D1) with a fluorescence lifetime imaging attachment (Lambert Instruments) was used to measure fluorescence lifetimes of mGFP.

    Techniques: Expressing, Plasmid Preparation, Western Blot, Pull Down Assay, Purification, Control, Binding Assay, Fluorescence, Derivative Assay, In Vitro

    FLIM-FRET analysis demonstrating obscurin regulation of ankyrin complex formation in cells. Pseudocolored images showing average CFP lifetime (τav) of (A) obscurin-CFP alone (negative control) or sarcolipin-CFP-YFP (positive control), (B) obscurin-CFP (donor) with acceptors sAnk1.5-YFP or AnkG107-YFP, and (C) sAnk1.5-CFP (donor) with acceptor AnkG107-YFP alone or with wild-type (WT) or mutant (ΔABD1&2) obscurin-HA. Scale bar represents 20 μm. (D) HA and GFP immunoblots demonstrate similar expression of donor, acceptor, and obscurin constructs between WT and mutant (ΔABDs) obscurin conditions. (E) The graph shows mean fluorescence lifetime of CFP (n ≥ 70 per condition per experiment from three independent experiments (biological replicates, n = 3)). Error bars represent standard error of the mean. Using ordinary one-way ANOVA and Tukey’s multiple comparison post hoc test, statistical analysis was performed separately (denoted by dotted line) on measurements from A and B, then C (**** represents p-values of <0.0001).

    Journal: Journal of molecular and cellular cardiology

    Article Title: Obscurin regulates ankyrin macromolecular complex formation

    doi: 10.1016/j.yjmcc.2022.04.008

    Figure Lengend Snippet: FLIM-FRET analysis demonstrating obscurin regulation of ankyrin complex formation in cells. Pseudocolored images showing average CFP lifetime (τav) of (A) obscurin-CFP alone (negative control) or sarcolipin-CFP-YFP (positive control), (B) obscurin-CFP (donor) with acceptors sAnk1.5-YFP or AnkG107-YFP, and (C) sAnk1.5-CFP (donor) with acceptor AnkG107-YFP alone or with wild-type (WT) or mutant (ΔABD1&2) obscurin-HA. Scale bar represents 20 μm. (D) HA and GFP immunoblots demonstrate similar expression of donor, acceptor, and obscurin constructs between WT and mutant (ΔABDs) obscurin conditions. (E) The graph shows mean fluorescence lifetime of CFP (n ≥ 70 per condition per experiment from three independent experiments (biological replicates, n = 3)). Error bars represent standard error of the mean. Using ordinary one-way ANOVA and Tukey’s multiple comparison post hoc test, statistical analysis was performed separately (denoted by dotted line) on measurements from A and B, then C (**** represents p-values of <0.0001).

    Article Snippet: FLIM-FRET analysis FLIM-FRET experiments were performed with a lifetime fluorescence imaging attachment (Lambert Instruments, Leutingewolde, The Netherlands) on an inverted microscope (Nikon).

    Techniques: Negative Control, Positive Control, Mutagenesis, Western Blot, Expressing, Construct, Fluorescence, Comparison

    Phasor plots: ( A ) the fluorescence lifetime imaging microscopy phasor plot of rhodamine 6G 5 μM and ( B ) sample No 1 with rhodamine 6G 5 μM as a reference.

    Journal: International Journal of Nanomedicine

    Article Title: Ultra-pure, water-dispersed Au nanoparticles produced by femtosecond laser ablation and fragmentation

    doi: 10.2147/IJN.S44163

    Figure Lengend Snippet: Phasor plots: ( A ) the fluorescence lifetime imaging microscopy phasor plot of rhodamine 6G 5 μM and ( B ) sample No 1 with rhodamine 6G 5 μM as a reference.

    Article Snippet: The Nikon Eclipse Ti microscope with a Lambert fluorescence lifetime imaging microscopy (FLIM) attachment was used to carry out experiments on the quenching of the rhodamine 6G (Rh6G) dye lifetime in the presence of gold nanoparticles.

    Techniques: Fluorescence, Imaging, Microscopy

    Determination of the fluorescence lifetime, τ = A/(Bω), from a phasor plot, where ω is the modulation frequency; see text for details.

    Journal: International Journal of Nanomedicine

    Article Title: Ultra-pure, water-dispersed Au nanoparticles produced by femtosecond laser ablation and fragmentation

    doi: 10.2147/IJN.S44163

    Figure Lengend Snippet: Determination of the fluorescence lifetime, τ = A/(Bω), from a phasor plot, where ω is the modulation frequency; see text for details.

    Article Snippet: The Nikon Eclipse Ti microscope with a Lambert fluorescence lifetime imaging microscopy (FLIM) attachment was used to carry out experiments on the quenching of the rhodamine 6G (Rh6G) dye lifetime in the presence of gold nanoparticles.

    Techniques: Fluorescence