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lyn fak fret biosensor plasmid  (Addgene inc)


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    Structured Review

    Addgene inc lyn fak fret biosensor plasmid
    TCEP-induced mild reduction of the cell surface promotes early adhesion–associated FAK activation and focal adhesion assembly. (A) Schematic illustration of the experimental workflow for monitoring FAK activation using <t>a</t> <t>Lyn–FAK</t> <t>FRET</t> biosensor. This schematic was created using BioRender.com . (B) Representative time-lapse FRET ratio images showing ECFP/YPet FRET ratios during early adhesion (Scale bar = 20 μm). (C) Quantification of the time-dependent ECFP/YPet FRET ratio during early adhesion. Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 compared with the Ctrl group. (D) Representative immunofluorescence staining for F-actin (red) and pFAK (green) (Scale bar = 100 μm). (E-J) Quantitative image analysis of cell morphology and focal adhesion (FA) parameters (Scale bar = 50 μm). Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.
    Lyn Fak Fret Biosensor Plasmid, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/lyn+fak/Lyn+FAK+biosensor+(Plasmid+%2378299)/pmc12925200-151-1-7
    Average 93 stars, based on 9 article reviews
    lyn fak fret biosensor plasmid - by Bioz Stars, 2026-10
    93/100 stars

    Images

    1) Product Images from "Modulating cell surface chemistry through mild reduction reinforces extracellular-to-intracellular transmission forces and mechano-signaling"

    Article Title: Modulating cell surface chemistry through mild reduction reinforces extracellular-to-intracellular transmission forces and mechano-signaling

    Journal: Materials Today Bio

    doi: 10.1016/j.mtbio.2026.102908

    TCEP-induced mild reduction of the cell surface promotes early adhesion–associated FAK activation and focal adhesion assembly. (A) Schematic illustration of the experimental workflow for monitoring FAK activation using a Lyn–FAK FRET biosensor. This schematic was created using BioRender.com . (B) Representative time-lapse FRET ratio images showing ECFP/YPet FRET ratios during early adhesion (Scale bar = 20 μm). (C) Quantification of the time-dependent ECFP/YPet FRET ratio during early adhesion. Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 compared with the Ctrl group. (D) Representative immunofluorescence staining for F-actin (red) and pFAK (green) (Scale bar = 100 μm). (E-J) Quantitative image analysis of cell morphology and focal adhesion (FA) parameters (Scale bar = 50 μm). Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.
    Figure Legend Snippet: TCEP-induced mild reduction of the cell surface promotes early adhesion–associated FAK activation and focal adhesion assembly. (A) Schematic illustration of the experimental workflow for monitoring FAK activation using a Lyn–FAK FRET biosensor. This schematic was created using BioRender.com . (B) Representative time-lapse FRET ratio images showing ECFP/YPet FRET ratios during early adhesion (Scale bar = 20 μm). (C) Quantification of the time-dependent ECFP/YPet FRET ratio during early adhesion. Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 compared with the Ctrl group. (D) Representative immunofluorescence staining for F-actin (red) and pFAK (green) (Scale bar = 100 μm). (E-J) Quantitative image analysis of cell morphology and focal adhesion (FA) parameters (Scale bar = 50 μm). Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.

    Techniques Used: Activation Assay, Immunofluorescence, Staining

    Related Articles

    Plasmid Preparation:

    Article Title: A new biological enhancement therapy for anterior cruciate ligament reconstruction: the preclinical proof of anterior cruciate ligament reconstruction with tendon graft reseeded with autologous anterior cruciate ligament-derived cells.
    Article Snippet: .. The Talin-TS (plasmid #83376) and Lyn-FAK (plasmid #78299) biosensors, which utilize fluorescence resonance energy transfer (FRET, a technique that detects changes in distance between two fluorescent molecules to monitor molecular interactions or structural shifts) to identify biomolecules or monitor environmental changes, were obtained from Addgene. .. The Talin-TS (plasmid #83376) and Lyn-FAK (plasmid #78299) biosensors, which utilize fluorescence resonance energy transfer (FRET, a technique that detects changes in distance between two fluorescent molecules to monitor molecular interactions or structural shifts) to identify biomolecules or monitor environmental changes, were obtained from Addgene.

    Article Title: A new biological enhancement therapy for anterior cruciate ligament reconstruction: the preclinical proof of anterior cruciate ligament reconstruction with tendon graft reseeded with autologous anterior cruciate ligament-derived cells
    Article Snippet: .. The Talin-TS (plasmid #83376) and Lyn-FAK (plasmid #78299) biosensors, which utilize fluorescence resonance energy transfer (FRET, a technique that detects changes in distance between two fluorescent molecules to monitor molecular interactions or structural shifts) to identify biomolecules or monitor environmental changes, were obtained from Addgene. .. The Talin-TS (plasmid #83376) and Lyn-FAK (plasmid #78299) biosensors, which utilize fluorescence resonance energy transfer (FRET, a technique that detects changes in distance between two fluorescent molecules to monitor molecular interactions or structural shifts) to identify biomolecules or monitor environmental changes, were obtained from Addgene.

    Article Title: Deciphering cell signaling networks with massively multiplexed biosensor barcoding
    Article Snippet: Cyto-FAK , , Addgene plasmid #78300. .. Lyn-FAK , , Addgene plasmid #78299. .. Src , , Addgene plasmid #78302.

    Fluorescence:

    Article Title: A new biological enhancement therapy for anterior cruciate ligament reconstruction: the preclinical proof of anterior cruciate ligament reconstruction with tendon graft reseeded with autologous anterior cruciate ligament-derived cells.
    Article Snippet: .. The Talin-TS (plasmid #83376) and Lyn-FAK (plasmid #78299) biosensors, which utilize fluorescence resonance energy transfer (FRET, a technique that detects changes in distance between two fluorescent molecules to monitor molecular interactions or structural shifts) to identify biomolecules or monitor environmental changes, were obtained from Addgene. .. The Talin-TS (plasmid #83376) and Lyn-FAK (plasmid #78299) biosensors, which utilize fluorescence resonance energy transfer (FRET, a technique that detects changes in distance between two fluorescent molecules to monitor molecular interactions or structural shifts) to identify biomolecules or monitor environmental changes, were obtained from Addgene.

    Article Title: A new biological enhancement therapy for anterior cruciate ligament reconstruction: the preclinical proof of anterior cruciate ligament reconstruction with tendon graft reseeded with autologous anterior cruciate ligament-derived cells
    Article Snippet: .. The Talin-TS (plasmid #83376) and Lyn-FAK (plasmid #78299) biosensors, which utilize fluorescence resonance energy transfer (FRET, a technique that detects changes in distance between two fluorescent molecules to monitor molecular interactions or structural shifts) to identify biomolecules or monitor environmental changes, were obtained from Addgene. .. The Talin-TS (plasmid #83376) and Lyn-FAK (plasmid #78299) biosensors, which utilize fluorescence resonance energy transfer (FRET, a technique that detects changes in distance between two fluorescent molecules to monitor molecular interactions or structural shifts) to identify biomolecules or monitor environmental changes, were obtained from Addgene.

    Förster Resonance Energy Transfer:

    Article Title: A new biological enhancement therapy for anterior cruciate ligament reconstruction: the preclinical proof of anterior cruciate ligament reconstruction with tendon graft reseeded with autologous anterior cruciate ligament-derived cells.
    Article Snippet: .. The Talin-TS (plasmid #83376) and Lyn-FAK (plasmid #78299) biosensors, which utilize fluorescence resonance energy transfer (FRET, a technique that detects changes in distance between two fluorescent molecules to monitor molecular interactions or structural shifts) to identify biomolecules or monitor environmental changes, were obtained from Addgene. .. The Talin-TS (plasmid #83376) and Lyn-FAK (plasmid #78299) biosensors, which utilize fluorescence resonance energy transfer (FRET, a technique that detects changes in distance between two fluorescent molecules to monitor molecular interactions or structural shifts) to identify biomolecules or monitor environmental changes, were obtained from Addgene.

    Article Title: A new biological enhancement therapy for anterior cruciate ligament reconstruction: the preclinical proof of anterior cruciate ligament reconstruction with tendon graft reseeded with autologous anterior cruciate ligament-derived cells
    Article Snippet: .. The Talin-TS (plasmid #83376) and Lyn-FAK (plasmid #78299) biosensors, which utilize fluorescence resonance energy transfer (FRET, a technique that detects changes in distance between two fluorescent molecules to monitor molecular interactions or structural shifts) to identify biomolecules or monitor environmental changes, were obtained from Addgene. .. The Talin-TS (plasmid #83376) and Lyn-FAK (plasmid #78299) biosensors, which utilize fluorescence resonance energy transfer (FRET, a technique that detects changes in distance between two fluorescent molecules to monitor molecular interactions or structural shifts) to identify biomolecules or monitor environmental changes, were obtained from Addgene.

    other:

    Article Title: Imaging and analysis for simultaneous tracking of fluorescent biosensors in barcoded cells
    Article Snippet: Lyn-FAK , ( ) , Addgene #78299.



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    lyn fak fret biosensor plasmid  (Addgene inc)
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    Addgene inc lyn fak fret biosensor plasmid
    TCEP-induced mild reduction of the cell surface promotes early adhesion–associated FAK activation and focal adhesion assembly. (A) Schematic illustration of the experimental workflow for monitoring FAK activation using <t>a</t> <t>Lyn–FAK</t> <t>FRET</t> biosensor. This schematic was created using BioRender.com . (B) Representative time-lapse FRET ratio images showing ECFP/YPet FRET ratios during early adhesion (Scale bar = 20 μm). (C) Quantification of the time-dependent ECFP/YPet FRET ratio during early adhesion. Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 compared with the Ctrl group. (D) Representative immunofluorescence staining for F-actin (red) and pFAK (green) (Scale bar = 100 μm). (E-J) Quantitative image analysis of cell morphology and focal adhesion (FA) parameters (Scale bar = 50 μm). Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.
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    TCEP-induced mild reduction of the cell surface promotes early adhesion–associated FAK activation and focal adhesion assembly. (A) Schematic illustration of the experimental workflow for monitoring FAK activation using <t>a</t> <t>Lyn–FAK</t> <t>FRET</t> biosensor. This schematic was created using BioRender.com . (B) Representative time-lapse FRET ratio images showing ECFP/YPet FRET ratios during early adhesion (Scale bar = 20 μm). (C) Quantification of the time-dependent ECFP/YPet FRET ratio during early adhesion. Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 compared with the Ctrl group. (D) Representative immunofluorescence staining for F-actin (red) and pFAK (green) (Scale bar = 100 μm). (E-J) Quantitative image analysis of cell morphology and focal adhesion (FA) parameters (Scale bar = 50 μm). Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.
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    TCEP-induced mild reduction of the cell surface promotes early adhesion–associated FAK activation and focal adhesion assembly. (A) Schematic illustration of the experimental workflow for monitoring FAK activation using <t>a</t> <t>Lyn–FAK</t> <t>FRET</t> biosensor. This schematic was created using BioRender.com . (B) Representative time-lapse FRET ratio images showing ECFP/YPet FRET ratios during early adhesion (Scale bar = 20 μm). (C) Quantification of the time-dependent ECFP/YPet FRET ratio during early adhesion. Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 compared with the Ctrl group. (D) Representative immunofluorescence staining for F-actin (red) and pFAK (green) (Scale bar = 100 μm). (E-J) Quantitative image analysis of cell morphology and focal adhesion (FA) parameters (Scale bar = 50 μm). Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.
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    TCEP-induced mild reduction of the cell surface promotes early adhesion–associated FAK activation and focal adhesion assembly. (A) Schematic illustration of the experimental workflow for monitoring FAK activation using <t>a</t> <t>Lyn–FAK</t> <t>FRET</t> biosensor. This schematic was created using BioRender.com . (B) Representative time-lapse FRET ratio images showing ECFP/YPet FRET ratios during early adhesion (Scale bar = 20 μm). (C) Quantification of the time-dependent ECFP/YPet FRET ratio during early adhesion. Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 compared with the Ctrl group. (D) Representative immunofluorescence staining for F-actin (red) and pFAK (green) (Scale bar = 100 μm). (E-J) Quantitative image analysis of cell morphology and focal adhesion (FA) parameters (Scale bar = 50 μm). Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.
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    Image Search Results


    TCEP-induced mild reduction of the cell surface promotes early adhesion–associated FAK activation and focal adhesion assembly. (A) Schematic illustration of the experimental workflow for monitoring FAK activation using a Lyn–FAK FRET biosensor. This schematic was created using BioRender.com . (B) Representative time-lapse FRET ratio images showing ECFP/YPet FRET ratios during early adhesion (Scale bar = 20 μm). (C) Quantification of the time-dependent ECFP/YPet FRET ratio during early adhesion. Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 compared with the Ctrl group. (D) Representative immunofluorescence staining for F-actin (red) and pFAK (green) (Scale bar = 100 μm). (E-J) Quantitative image analysis of cell morphology and focal adhesion (FA) parameters (Scale bar = 50 μm). Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.

    Journal: Materials Today Bio

    Article Title: Modulating cell surface chemistry through mild reduction reinforces extracellular-to-intracellular transmission forces and mechano-signaling

    doi: 10.1016/j.mtbio.2026.102908

    Figure Lengend Snippet: TCEP-induced mild reduction of the cell surface promotes early adhesion–associated FAK activation and focal adhesion assembly. (A) Schematic illustration of the experimental workflow for monitoring FAK activation using a Lyn–FAK FRET biosensor. This schematic was created using BioRender.com . (B) Representative time-lapse FRET ratio images showing ECFP/YPet FRET ratios during early adhesion (Scale bar = 20 μm). (C) Quantification of the time-dependent ECFP/YPet FRET ratio during early adhesion. Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 compared with the Ctrl group. (D) Representative immunofluorescence staining for F-actin (red) and pFAK (green) (Scale bar = 100 μm). (E-J) Quantitative image analysis of cell morphology and focal adhesion (FA) parameters (Scale bar = 50 μm). Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.

    Article Snippet: The Lyn–FAK FRET biosensor plasmid (Plasmid #78299, Addgene, Watertown, MA, USA) was inserted into the pAd/CMV/V5-DESTTM GatewayTM vector (V49320, Thermo Fisher Scientific, Waltham, MA, USA) according to the manufacturer's instructions to generate an adenoviral expression construct.

    Techniques: Activation Assay, Immunofluorescence, Staining