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fak fret biosensor construct  (Addgene inc)


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    Structured Review

    Addgene inc fak fret biosensor construct
    ( A ) The <t>FAK</t> biosensor is composed of ECFP, SH2 domain, flexible linker, FAK substrate peptide, YPet, and FAT domain. ( B ) Schematics illustrating the <t>FRET</t> effect of the FAK biosensor upon the actions of FAK phosphorylation or dephosphorylation. Upon phosphorylation of Y397 in the biosensor FAK substrate peptide, the SH2 domain forms an intramolecular complex with the phosphotyrosine side chain, increasing the distance between the FRET pair to alter the FRET signal. Dephosphorylation reverses the FRET change. ATP, adenosine 5′-triphosphate. ( C ) C-terminal FAT domain recruits the biosensor to FAs. YPet intensity showing slight changes before and after FAK inhibition (FAKi; 10 μM PF-573228, 60 min). ( D ) ECFP/FRET signal before and after FAKi (10 μM PF-573228, 60 min) showing that the biosensor is specific and sensitive to FAK activity. ( E ) EFCP/FRET signal at individual FAs [ n = 195 FAs from seven cells across three independent experiments for FAKi (10 μM PF-573228, >60 min); n = 151 FAs from six cells across three independent experiments for DMSO control; means ± SD]. ( F ) Fluorescence lifetime image and quantification for fibroblasts expressing the FAK biosensor ( n = 23 FAs from six cells across three independent experiments). Scale bar, 20 μm. ( G ) FRET efficiency image and quantification for FAs and cytosol ( n = 19 FAs from five cells across three independent experiments). Scale bar, 20 μm. a.u., arbitrary units.
    Fak Fret Biosensor Construct, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fak fret biosensor construct/product/Addgene inc
    Average 93 stars, based on 3 article reviews
    fak fret biosensor construct - by Bioz Stars, 2026-04
    93/100 stars

    Images

    1) Product Images from "Mechanochemical waves in focal adhesions during cell migration"

    Article Title: Mechanochemical waves in focal adhesions during cell migration

    Journal: Science Advances

    doi: 10.1126/sciadv.adw6425

    ( A ) The FAK biosensor is composed of ECFP, SH2 domain, flexible linker, FAK substrate peptide, YPet, and FAT domain. ( B ) Schematics illustrating the FRET effect of the FAK biosensor upon the actions of FAK phosphorylation or dephosphorylation. Upon phosphorylation of Y397 in the biosensor FAK substrate peptide, the SH2 domain forms an intramolecular complex with the phosphotyrosine side chain, increasing the distance between the FRET pair to alter the FRET signal. Dephosphorylation reverses the FRET change. ATP, adenosine 5′-triphosphate. ( C ) C-terminal FAT domain recruits the biosensor to FAs. YPet intensity showing slight changes before and after FAK inhibition (FAKi; 10 μM PF-573228, 60 min). ( D ) ECFP/FRET signal before and after FAKi (10 μM PF-573228, 60 min) showing that the biosensor is specific and sensitive to FAK activity. ( E ) EFCP/FRET signal at individual FAs [ n = 195 FAs from seven cells across three independent experiments for FAKi (10 μM PF-573228, >60 min); n = 151 FAs from six cells across three independent experiments for DMSO control; means ± SD]. ( F ) Fluorescence lifetime image and quantification for fibroblasts expressing the FAK biosensor ( n = 23 FAs from six cells across three independent experiments). Scale bar, 20 μm. ( G ) FRET efficiency image and quantification for FAs and cytosol ( n = 19 FAs from five cells across three independent experiments). Scale bar, 20 μm. a.u., arbitrary units.
    Figure Legend Snippet: ( A ) The FAK biosensor is composed of ECFP, SH2 domain, flexible linker, FAK substrate peptide, YPet, and FAT domain. ( B ) Schematics illustrating the FRET effect of the FAK biosensor upon the actions of FAK phosphorylation or dephosphorylation. Upon phosphorylation of Y397 in the biosensor FAK substrate peptide, the SH2 domain forms an intramolecular complex with the phosphotyrosine side chain, increasing the distance between the FRET pair to alter the FRET signal. Dephosphorylation reverses the FRET change. ATP, adenosine 5′-triphosphate. ( C ) C-terminal FAT domain recruits the biosensor to FAs. YPet intensity showing slight changes before and after FAK inhibition (FAKi; 10 μM PF-573228, 60 min). ( D ) ECFP/FRET signal before and after FAKi (10 μM PF-573228, 60 min) showing that the biosensor is specific and sensitive to FAK activity. ( E ) EFCP/FRET signal at individual FAs [ n = 195 FAs from seven cells across three independent experiments for FAKi (10 μM PF-573228, >60 min); n = 151 FAs from six cells across three independent experiments for DMSO control; means ± SD]. ( F ) Fluorescence lifetime image and quantification for fibroblasts expressing the FAK biosensor ( n = 23 FAs from six cells across three independent experiments). Scale bar, 20 μm. ( G ) FRET efficiency image and quantification for FAs and cytosol ( n = 19 FAs from five cells across three independent experiments). Scale bar, 20 μm. a.u., arbitrary units.

    Techniques Used: Phospho-proteomics, De-Phosphorylation Assay, Inhibition, Activity Assay, Control, Fluorescence, Expressing



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    fak fret biosensor construct  (Addgene inc)
    93
    Addgene inc fak fret biosensor construct
    ( A ) The <t>FAK</t> biosensor is composed of ECFP, SH2 domain, flexible linker, FAK substrate peptide, YPet, and FAT domain. ( B ) Schematics illustrating the <t>FRET</t> effect of the FAK biosensor upon the actions of FAK phosphorylation or dephosphorylation. Upon phosphorylation of Y397 in the biosensor FAK substrate peptide, the SH2 domain forms an intramolecular complex with the phosphotyrosine side chain, increasing the distance between the FRET pair to alter the FRET signal. Dephosphorylation reverses the FRET change. ATP, adenosine 5′-triphosphate. ( C ) C-terminal FAT domain recruits the biosensor to FAs. YPet intensity showing slight changes before and after FAK inhibition (FAKi; 10 μM PF-573228, 60 min). ( D ) ECFP/FRET signal before and after FAKi (10 μM PF-573228, 60 min) showing that the biosensor is specific and sensitive to FAK activity. ( E ) EFCP/FRET signal at individual FAs [ n = 195 FAs from seven cells across three independent experiments for FAKi (10 μM PF-573228, >60 min); n = 151 FAs from six cells across three independent experiments for DMSO control; means ± SD]. ( F ) Fluorescence lifetime image and quantification for fibroblasts expressing the FAK biosensor ( n = 23 FAs from six cells across three independent experiments). Scale bar, 20 μm. ( G ) FRET efficiency image and quantification for FAs and cytosol ( n = 19 FAs from five cells across three independent experiments). Scale bar, 20 μm. a.u., arbitrary units.
    Fak Fret Biosensor Construct, 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
    https://www.bioz.com/result/fak fret biosensor construct/product/Addgene inc
    Average 93 stars, based on 1 article reviews
    fak fret biosensor construct - by Bioz Stars, 2026-04
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    ( A ) The FAK biosensor is composed of ECFP, SH2 domain, flexible linker, FAK substrate peptide, YPet, and FAT domain. ( B ) Schematics illustrating the FRET effect of the FAK biosensor upon the actions of FAK phosphorylation or dephosphorylation. Upon phosphorylation of Y397 in the biosensor FAK substrate peptide, the SH2 domain forms an intramolecular complex with the phosphotyrosine side chain, increasing the distance between the FRET pair to alter the FRET signal. Dephosphorylation reverses the FRET change. ATP, adenosine 5′-triphosphate. ( C ) C-terminal FAT domain recruits the biosensor to FAs. YPet intensity showing slight changes before and after FAK inhibition (FAKi; 10 μM PF-573228, 60 min). ( D ) ECFP/FRET signal before and after FAKi (10 μM PF-573228, 60 min) showing that the biosensor is specific and sensitive to FAK activity. ( E ) EFCP/FRET signal at individual FAs [ n = 195 FAs from seven cells across three independent experiments for FAKi (10 μM PF-573228, >60 min); n = 151 FAs from six cells across three independent experiments for DMSO control; means ± SD]. ( F ) Fluorescence lifetime image and quantification for fibroblasts expressing the FAK biosensor ( n = 23 FAs from six cells across three independent experiments). Scale bar, 20 μm. ( G ) FRET efficiency image and quantification for FAs and cytosol ( n = 19 FAs from five cells across three independent experiments). Scale bar, 20 μm. a.u., arbitrary units.

    Journal: Science Advances

    Article Title: Mechanochemical waves in focal adhesions during cell migration

    doi: 10.1126/sciadv.adw6425

    Figure Lengend Snippet: ( A ) The FAK biosensor is composed of ECFP, SH2 domain, flexible linker, FAK substrate peptide, YPet, and FAT domain. ( B ) Schematics illustrating the FRET effect of the FAK biosensor upon the actions of FAK phosphorylation or dephosphorylation. Upon phosphorylation of Y397 in the biosensor FAK substrate peptide, the SH2 domain forms an intramolecular complex with the phosphotyrosine side chain, increasing the distance between the FRET pair to alter the FRET signal. Dephosphorylation reverses the FRET change. ATP, adenosine 5′-triphosphate. ( C ) C-terminal FAT domain recruits the biosensor to FAs. YPet intensity showing slight changes before and after FAK inhibition (FAKi; 10 μM PF-573228, 60 min). ( D ) ECFP/FRET signal before and after FAKi (10 μM PF-573228, 60 min) showing that the biosensor is specific and sensitive to FAK activity. ( E ) EFCP/FRET signal at individual FAs [ n = 195 FAs from seven cells across three independent experiments for FAKi (10 μM PF-573228, >60 min); n = 151 FAs from six cells across three independent experiments for DMSO control; means ± SD]. ( F ) Fluorescence lifetime image and quantification for fibroblasts expressing the FAK biosensor ( n = 23 FAs from six cells across three independent experiments). Scale bar, 20 μm. ( G ) FRET efficiency image and quantification for FAs and cytosol ( n = 19 FAs from five cells across three independent experiments). Scale bar, 20 μm. a.u., arbitrary units.

    Article Snippet: The FAK FRET biosensor construct is available from Addgene (plasmid no. 78303).

    Techniques: Phospho-proteomics, De-Phosphorylation Assay, Inhibition, Activity Assay, Control, Fluorescence, Expressing