fluorescence intensity acquisitions Search Results


99
Revvity fluorescence intensity acquisitions
( A ). Representative images of OE-19 xenograft bearing mice imaged at 4 and 6 h post NF-800 injection at IVIS Spectrum. ( B ) Mean <t>fluorescence</t> intensity values of Tumor, Kidney and Liver of animals bearing OE-19 xenografts and treated with NF-800. ( C ) Lifetime values obtained with tail fitting of the abovementioned tissues, compared to the probe dissolved in PBS (n = 7 animals). One way ANOVA Multiple comparison test (* = p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001; **** p ≤ 0.0001).
Fluorescence Intensity Acquisitions, supplied by Revvity, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Danaher Inc las x software
( A ). Representative images of OE-19 xenograft bearing mice imaged at 4 and 6 h post NF-800 injection at IVIS Spectrum. ( B ) Mean <t>fluorescence</t> intensity values of Tumor, Kidney and Liver of animals bearing OE-19 xenografts and treated with NF-800. ( C ) Lifetime values obtained with tail fitting of the abovementioned tissues, compared to the probe dissolved in PBS (n = 7 animals). One way ANOVA Multiple comparison test (* = p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001; **** p ≤ 0.0001).
Las X Software, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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MathWorks Inc matlab r2018b
Dependence of migration distance on protein molecular mass in three different gel compositions. A) Open microfluidic device for single-cell PAGE immunoassay. Single-cells are gravity settled into an array of microwells for subsequent cell lysis and protein solubilization, protein PAGE, and in-gel immobilization of separated proteins. Protein targets are immunoprobed with fluorophore-conjugated antibodies. B) (Left) Relationship between electromigration distance and the logarithm value (base 10) of molecular mass of nine different protein targets (GAPDH, 36 kDa; β-tubulin, 50 kDa; PTBP1, 57 kDa (above limit of detection in 6/9 gels tested); ER-α, 66 kDa; HSP90, 90 kDa; SFPQ, 95 kDa; α-Actinin, 103 kDa; Vinculin, 124 kDa; and mTOR, 289 kDa from lysed MCF-7 cells. Three different gel composition conditions (5%T, 6%T and 8%T) were used to analyze the differing electrophoretic migration distances. Boxplots represent aggregation of single-cell data points taken from 3 replicate devices with the number of individual cells assayed at the bottom of each plot. Dashed lines (---) represent linear fits including mTOR, while solid lines (—) indicate fits excluding mTOR. (Right) Representative false-color <t>fluorescence</t> micrographs and intensity plots as examples of protein electromigration in each gel condition. (See Figure S1 for additional targets)
Matlab R2018b, supplied by MathWorks Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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86
DiaSorin Biotechnology xmap 100 system
Dependence of migration distance on protein molecular mass in three different gel compositions. A) Open microfluidic device for single-cell PAGE immunoassay. Single-cells are gravity settled into an array of microwells for subsequent cell lysis and protein solubilization, protein PAGE, and in-gel immobilization of separated proteins. Protein targets are immunoprobed with fluorophore-conjugated antibodies. B) (Left) Relationship between electromigration distance and the logarithm value (base 10) of molecular mass of nine different protein targets (GAPDH, 36 kDa; β-tubulin, 50 kDa; PTBP1, 57 kDa (above limit of detection in 6/9 gels tested); ER-α, 66 kDa; HSP90, 90 kDa; SFPQ, 95 kDa; α-Actinin, 103 kDa; Vinculin, 124 kDa; and mTOR, 289 kDa from lysed MCF-7 cells. Three different gel composition conditions (5%T, 6%T and 8%T) were used to analyze the differing electrophoretic migration distances. Boxplots represent aggregation of single-cell data points taken from 3 replicate devices with the number of individual cells assayed at the bottom of each plot. Dashed lines (---) represent linear fits including mTOR, while solid lines (—) indicate fits excluding mTOR. (Right) Representative false-color <t>fluorescence</t> micrographs and intensity plots as examples of protein electromigration in each gel condition. (See Figure S1 for additional targets)
Xmap 100 System, supplied by DiaSorin Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Becton Dickinson lsrfortessa x-20 cell analyzer
Dependence of migration distance on protein molecular mass in three different gel compositions. A) Open microfluidic device for single-cell PAGE immunoassay. Single-cells are gravity settled into an array of microwells for subsequent cell lysis and protein solubilization, protein PAGE, and in-gel immobilization of separated proteins. Protein targets are immunoprobed with fluorophore-conjugated antibodies. B) (Left) Relationship between electromigration distance and the logarithm value (base 10) of molecular mass of nine different protein targets (GAPDH, 36 kDa; β-tubulin, 50 kDa; PTBP1, 57 kDa (above limit of detection in 6/9 gels tested); ER-α, 66 kDa; HSP90, 90 kDa; SFPQ, 95 kDa; α-Actinin, 103 kDa; Vinculin, 124 kDa; and mTOR, 289 kDa from lysed MCF-7 cells. Three different gel composition conditions (5%T, 6%T and 8%T) were used to analyze the differing electrophoretic migration distances. Boxplots represent aggregation of single-cell data points taken from 3 replicate devices with the number of individual cells assayed at the bottom of each plot. Dashed lines (---) represent linear fits including mTOR, while solid lines (—) indicate fits excluding mTOR. (Right) Representative false-color <t>fluorescence</t> micrographs and intensity plots as examples of protein electromigration in each gel condition. (See Figure S1 for additional targets)
Lsrfortessa X 20 Cell Analyzer, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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universal imaging inc metafluor
Dependence of migration distance on protein molecular mass in three different gel compositions. A) Open microfluidic device for single-cell PAGE immunoassay. Single-cells are gravity settled into an array of microwells for subsequent cell lysis and protein solubilization, protein PAGE, and in-gel immobilization of separated proteins. Protein targets are immunoprobed with fluorophore-conjugated antibodies. B) (Left) Relationship between electromigration distance and the logarithm value (base 10) of molecular mass of nine different protein targets (GAPDH, 36 kDa; β-tubulin, 50 kDa; PTBP1, 57 kDa (above limit of detection in 6/9 gels tested); ER-α, 66 kDa; HSP90, 90 kDa; SFPQ, 95 kDa; α-Actinin, 103 kDa; Vinculin, 124 kDa; and mTOR, 289 kDa from lysed MCF-7 cells. Three different gel composition conditions (5%T, 6%T and 8%T) were used to analyze the differing electrophoretic migration distances. Boxplots represent aggregation of single-cell data points taken from 3 replicate devices with the number of individual cells assayed at the bottom of each plot. Dashed lines (---) represent linear fits including mTOR, while solid lines (—) indicate fits excluding mTOR. (Right) Representative false-color <t>fluorescence</t> micrographs and intensity plots as examples of protein electromigration in each gel condition. (See Figure S1 for additional targets)
Metafluor, supplied by universal imaging inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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universal imaging inc metafluor computer software
Dependence of migration distance on protein molecular mass in three different gel compositions. A) Open microfluidic device for single-cell PAGE immunoassay. Single-cells are gravity settled into an array of microwells for subsequent cell lysis and protein solubilization, protein PAGE, and in-gel immobilization of separated proteins. Protein targets are immunoprobed with fluorophore-conjugated antibodies. B) (Left) Relationship between electromigration distance and the logarithm value (base 10) of molecular mass of nine different protein targets (GAPDH, 36 kDa; β-tubulin, 50 kDa; PTBP1, 57 kDa (above limit of detection in 6/9 gels tested); ER-α, 66 kDa; HSP90, 90 kDa; SFPQ, 95 kDa; α-Actinin, 103 kDa; Vinculin, 124 kDa; and mTOR, 289 kDa from lysed MCF-7 cells. Three different gel composition conditions (5%T, 6%T and 8%T) were used to analyze the differing electrophoretic migration distances. Boxplots represent aggregation of single-cell data points taken from 3 replicate devices with the number of individual cells assayed at the bottom of each plot. Dashed lines (---) represent linear fits including mTOR, while solid lines (—) indicate fits excluding mTOR. (Right) Representative false-color <t>fluorescence</t> micrographs and intensity plots as examples of protein electromigration in each gel condition. (See Figure S1 for additional targets)
Metafluor Computer Software, supplied by universal imaging inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Evident Corporation fv1000 confocal
Dependence of migration distance on protein molecular mass in three different gel compositions. A) Open microfluidic device for single-cell PAGE immunoassay. Single-cells are gravity settled into an array of microwells for subsequent cell lysis and protein solubilization, protein PAGE, and in-gel immobilization of separated proteins. Protein targets are immunoprobed with fluorophore-conjugated antibodies. B) (Left) Relationship between electromigration distance and the logarithm value (base 10) of molecular mass of nine different protein targets (GAPDH, 36 kDa; β-tubulin, 50 kDa; PTBP1, 57 kDa (above limit of detection in 6/9 gels tested); ER-α, 66 kDa; HSP90, 90 kDa; SFPQ, 95 kDa; α-Actinin, 103 kDa; Vinculin, 124 kDa; and mTOR, 289 kDa from lysed MCF-7 cells. Three different gel composition conditions (5%T, 6%T and 8%T) were used to analyze the differing electrophoretic migration distances. Boxplots represent aggregation of single-cell data points taken from 3 replicate devices with the number of individual cells assayed at the bottom of each plot. Dashed lines (---) represent linear fits including mTOR, while solid lines (—) indicate fits excluding mTOR. (Right) Representative false-color <t>fluorescence</t> micrographs and intensity plots as examples of protein electromigration in each gel condition. (See Figure S1 for additional targets)
Fv1000 Confocal, supplied by Evident Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Carl Zeiss lsm510 software 3.2 sp2
Dependence of migration distance on protein molecular mass in three different gel compositions. A) Open microfluidic device for single-cell PAGE immunoassay. Single-cells are gravity settled into an array of microwells for subsequent cell lysis and protein solubilization, protein PAGE, and in-gel immobilization of separated proteins. Protein targets are immunoprobed with fluorophore-conjugated antibodies. B) (Left) Relationship between electromigration distance and the logarithm value (base 10) of molecular mass of nine different protein targets (GAPDH, 36 kDa; β-tubulin, 50 kDa; PTBP1, 57 kDa (above limit of detection in 6/9 gels tested); ER-α, 66 kDa; HSP90, 90 kDa; SFPQ, 95 kDa; α-Actinin, 103 kDa; Vinculin, 124 kDa; and mTOR, 289 kDa from lysed MCF-7 cells. Three different gel composition conditions (5%T, 6%T and 8%T) were used to analyze the differing electrophoretic migration distances. Boxplots represent aggregation of single-cell data points taken from 3 replicate devices with the number of individual cells assayed at the bottom of each plot. Dashed lines (---) represent linear fits including mTOR, while solid lines (—) indicate fits excluding mTOR. (Right) Representative false-color <t>fluorescence</t> micrographs and intensity plots as examples of protein electromigration in each gel condition. (See Figure S1 for additional targets)
Lsm510 Software 3.2 Sp2, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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MathWorks Inc matlab-based image analysis pipeline supersegger
Dependence of migration distance on protein molecular mass in three different gel compositions. A) Open microfluidic device for single-cell PAGE immunoassay. Single-cells are gravity settled into an array of microwells for subsequent cell lysis and protein solubilization, protein PAGE, and in-gel immobilization of separated proteins. Protein targets are immunoprobed with fluorophore-conjugated antibodies. B) (Left) Relationship between electromigration distance and the logarithm value (base 10) of molecular mass of nine different protein targets (GAPDH, 36 kDa; β-tubulin, 50 kDa; PTBP1, 57 kDa (above limit of detection in 6/9 gels tested); ER-α, 66 kDa; HSP90, 90 kDa; SFPQ, 95 kDa; α-Actinin, 103 kDa; Vinculin, 124 kDa; and mTOR, 289 kDa from lysed MCF-7 cells. Three different gel composition conditions (5%T, 6%T and 8%T) were used to analyze the differing electrophoretic migration distances. Boxplots represent aggregation of single-cell data points taken from 3 replicate devices with the number of individual cells assayed at the bottom of each plot. Dashed lines (---) represent linear fits including mTOR, while solid lines (—) indicate fits excluding mTOR. (Right) Representative false-color <t>fluorescence</t> micrographs and intensity plots as examples of protein electromigration in each gel condition. (See Figure S1 for additional targets)
Matlab Based Image Analysis Pipeline Supersegger, supplied by MathWorks Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Carl Zeiss acquisition software zen 2.6
Dependence of migration distance on protein molecular mass in three different gel compositions. A) Open microfluidic device for single-cell PAGE immunoassay. Single-cells are gravity settled into an array of microwells for subsequent cell lysis and protein solubilization, protein PAGE, and in-gel immobilization of separated proteins. Protein targets are immunoprobed with fluorophore-conjugated antibodies. B) (Left) Relationship between electromigration distance and the logarithm value (base 10) of molecular mass of nine different protein targets (GAPDH, 36 kDa; β-tubulin, 50 kDa; PTBP1, 57 kDa (above limit of detection in 6/9 gels tested); ER-α, 66 kDa; HSP90, 90 kDa; SFPQ, 95 kDa; α-Actinin, 103 kDa; Vinculin, 124 kDa; and mTOR, 289 kDa from lysed MCF-7 cells. Three different gel composition conditions (5%T, 6%T and 8%T) were used to analyze the differing electrophoretic migration distances. Boxplots represent aggregation of single-cell data points taken from 3 replicate devices with the number of individual cells assayed at the bottom of each plot. Dashed lines (---) represent linear fits including mTOR, while solid lines (—) indicate fits excluding mTOR. (Right) Representative false-color <t>fluorescence</t> micrographs and intensity plots as examples of protein electromigration in each gel condition. (See Figure S1 for additional targets)
Acquisition Software Zen 2.6, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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MathWorks Inc custom-written matlab scripts
Dependence of migration distance on protein molecular mass in three different gel compositions. A) Open microfluidic device for single-cell PAGE immunoassay. Single-cells are gravity settled into an array of microwells for subsequent cell lysis and protein solubilization, protein PAGE, and in-gel immobilization of separated proteins. Protein targets are immunoprobed with fluorophore-conjugated antibodies. B) (Left) Relationship between electromigration distance and the logarithm value (base 10) of molecular mass of nine different protein targets (GAPDH, 36 kDa; β-tubulin, 50 kDa; PTBP1, 57 kDa (above limit of detection in 6/9 gels tested); ER-α, 66 kDa; HSP90, 90 kDa; SFPQ, 95 kDa; α-Actinin, 103 kDa; Vinculin, 124 kDa; and mTOR, 289 kDa from lysed MCF-7 cells. Three different gel composition conditions (5%T, 6%T and 8%T) were used to analyze the differing electrophoretic migration distances. Boxplots represent aggregation of single-cell data points taken from 3 replicate devices with the number of individual cells assayed at the bottom of each plot. Dashed lines (---) represent linear fits including mTOR, while solid lines (—) indicate fits excluding mTOR. (Right) Representative false-color <t>fluorescence</t> micrographs and intensity plots as examples of protein electromigration in each gel condition. (See Figure S1 for additional targets)
Custom Written Matlab Scripts, supplied by MathWorks Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


( A ). Representative images of OE-19 xenograft bearing mice imaged at 4 and 6 h post NF-800 injection at IVIS Spectrum. ( B ) Mean fluorescence intensity values of Tumor, Kidney and Liver of animals bearing OE-19 xenografts and treated with NF-800. ( C ) Lifetime values obtained with tail fitting of the abovementioned tissues, compared to the probe dissolved in PBS (n = 7 animals). One way ANOVA Multiple comparison test (* = p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001; **** p ≤ 0.0001).

Journal: Scientific Reports

Article Title: Investigating probe-receptor interactions and enhancing fluorescence guided surgery with fluorescence lifetime imaging and NF-800 in HER-2 positive esophageal adenocarcinoma

doi: 10.1038/s41598-025-31872-8

Figure Lengend Snippet: ( A ). Representative images of OE-19 xenograft bearing mice imaged at 4 and 6 h post NF-800 injection at IVIS Spectrum. ( B ) Mean fluorescence intensity values of Tumor, Kidney and Liver of animals bearing OE-19 xenografts and treated with NF-800. ( C ) Lifetime values obtained with tail fitting of the abovementioned tissues, compared to the probe dissolved in PBS (n = 7 animals). One way ANOVA Multiple comparison test (* = p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001; **** p ≤ 0.0001).

Article Snippet: Fluorescence intensity acquisitions were performed at IVIS Spectrum (Perkin Elmer Italia S.p.A.) equipped with an excitation filter at 745 nm and emission filter at 800 nm with 30 nm and 20 nm bandwidth, respectively.

Techniques: Injection, Fluorescence, Comparison

( A ) Fluorescence intensity values (counts) and respective lifetimes (ns) of ex vivo tumor and kidneys 6 h after administration of NF-800. ( B ) Fluorescence intensity values and respective lifetimes (ns) of ex vivo tumor and liver after administration of Tz-800. (One way ANOVA Multiple comparison test was performed between all the groups (e.g. tumor vs kidney; tumor vs PBS; kidney vs PBS) (* = p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001; **** p ≤ 0.0001).

Journal: Scientific Reports

Article Title: Investigating probe-receptor interactions and enhancing fluorescence guided surgery with fluorescence lifetime imaging and NF-800 in HER-2 positive esophageal adenocarcinoma

doi: 10.1038/s41598-025-31872-8

Figure Lengend Snippet: ( A ) Fluorescence intensity values (counts) and respective lifetimes (ns) of ex vivo tumor and kidneys 6 h after administration of NF-800. ( B ) Fluorescence intensity values and respective lifetimes (ns) of ex vivo tumor and liver after administration of Tz-800. (One way ANOVA Multiple comparison test was performed between all the groups (e.g. tumor vs kidney; tumor vs PBS; kidney vs PBS) (* = p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001; **** p ≤ 0.0001).

Article Snippet: Fluorescence intensity acquisitions were performed at IVIS Spectrum (Perkin Elmer Italia S.p.A.) equipped with an excitation filter at 745 nm and emission filter at 800 nm with 30 nm and 20 nm bandwidth, respectively.

Techniques: Fluorescence, Ex Vivo, Comparison

Representative Fluorescence Intensity (AU) and FLT parametric map (ns) of a tumor treated with NF-800. ROIs indicate tumors, which appears to have spread throughout the stomach. Histogram represents distribution of lifetimes across pixels, as fitted to obtain the parametric map.

Journal: Scientific Reports

Article Title: Investigating probe-receptor interactions and enhancing fluorescence guided surgery with fluorescence lifetime imaging and NF-800 in HER-2 positive esophageal adenocarcinoma

doi: 10.1038/s41598-025-31872-8

Figure Lengend Snippet: Representative Fluorescence Intensity (AU) and FLT parametric map (ns) of a tumor treated with NF-800. ROIs indicate tumors, which appears to have spread throughout the stomach. Histogram represents distribution of lifetimes across pixels, as fitted to obtain the parametric map.

Article Snippet: Fluorescence intensity acquisitions were performed at IVIS Spectrum (Perkin Elmer Italia S.p.A.) equipped with an excitation filter at 745 nm and emission filter at 800 nm with 30 nm and 20 nm bandwidth, respectively.

Techniques: Fluorescence

Dependence of migration distance on protein molecular mass in three different gel compositions. A) Open microfluidic device for single-cell PAGE immunoassay. Single-cells are gravity settled into an array of microwells for subsequent cell lysis and protein solubilization, protein PAGE, and in-gel immobilization of separated proteins. Protein targets are immunoprobed with fluorophore-conjugated antibodies. B) (Left) Relationship between electromigration distance and the logarithm value (base 10) of molecular mass of nine different protein targets (GAPDH, 36 kDa; β-tubulin, 50 kDa; PTBP1, 57 kDa (above limit of detection in 6/9 gels tested); ER-α, 66 kDa; HSP90, 90 kDa; SFPQ, 95 kDa; α-Actinin, 103 kDa; Vinculin, 124 kDa; and mTOR, 289 kDa from lysed MCF-7 cells. Three different gel composition conditions (5%T, 6%T and 8%T) were used to analyze the differing electrophoretic migration distances. Boxplots represent aggregation of single-cell data points taken from 3 replicate devices with the number of individual cells assayed at the bottom of each plot. Dashed lines (---) represent linear fits including mTOR, while solid lines (—) indicate fits excluding mTOR. (Right) Representative false-color fluorescence micrographs and intensity plots as examples of protein electromigration in each gel condition. (See Figure S1 for additional targets)

Journal: The Analyst

Article Title: Ferguson analysis of protein electromigration during single-cell electrophoresis in an open microfluidic device

doi: 10.1039/c9an02553g

Figure Lengend Snippet: Dependence of migration distance on protein molecular mass in three different gel compositions. A) Open microfluidic device for single-cell PAGE immunoassay. Single-cells are gravity settled into an array of microwells for subsequent cell lysis and protein solubilization, protein PAGE, and in-gel immobilization of separated proteins. Protein targets are immunoprobed with fluorophore-conjugated antibodies. B) (Left) Relationship between electromigration distance and the logarithm value (base 10) of molecular mass of nine different protein targets (GAPDH, 36 kDa; β-tubulin, 50 kDa; PTBP1, 57 kDa (above limit of detection in 6/9 gels tested); ER-α, 66 kDa; HSP90, 90 kDa; SFPQ, 95 kDa; α-Actinin, 103 kDa; Vinculin, 124 kDa; and mTOR, 289 kDa from lysed MCF-7 cells. Three different gel composition conditions (5%T, 6%T and 8%T) were used to analyze the differing electrophoretic migration distances. Boxplots represent aggregation of single-cell data points taken from 3 replicate devices with the number of individual cells assayed at the bottom of each plot. Dashed lines (---) represent linear fits including mTOR, while solid lines (—) indicate fits excluding mTOR. (Right) Representative false-color fluorescence micrographs and intensity plots as examples of protein electromigration in each gel condition. (See Figure S1 for additional targets)

Article Snippet: Gaussian curves were fit to fluorescence intensity profiles in MATLAB (R2018b, Curve Fitting Toolbox) in order to obtain the mean μ (used to describe the protein migration distance) and the variance σ 2 (used to calculate peak width as 4σ).

Techniques: Migration, Lysis, Fluorescence