anti phospho egfr y1068  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho egfr y1068
    Anti Phospho Egfr Y1068, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phospho egfr y1068  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho egfr y1068
    Phospho Egfr Y1068, supplied by Cell Signaling Technology 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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    anti phospho egfr y1068  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho egfr y1068
    Anti Phospho Egfr Y1068, supplied by Cell Signaling Technology 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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    phospho egfr y1068  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho egfr y1068
    Phospho Egfr Y1068, supplied by Cell Signaling Technology 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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    phospho egfr y1068  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho egfr y1068
    Effect of genistein on expression and phosphorylation of EGFR during experimental CCl 4 -induced subacute liver damage. An increase in total protein and phosphorylation from livers with CCl 4 -induced subacute liver damage was observed. Genistein significantly increased total protein and pY845 and pY1068 EGFR. The analysis was determined by Western blot a semiquantitative analysis of the expression levels of p‑EGFR (Y845, Y992 and <t>Y1068),</t> β-actin was used as a loading control. Bars show the mean values ± standard deviations of the band density normalized to the total protein. n = 8, *p < 0.05 as compared to control group; #p < 0.05 as compared to liver damage group, respectively using an ANOVA and Tukey’s test
    Phospho Egfr Y1068, supplied by Cell Signaling Technology 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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    1) Product Images from "EGF-receptor phosphorylation and downstream signaling are activated by genistein during subacute liver damage"

    Article Title: EGF-receptor phosphorylation and downstream signaling are activated by genistein during subacute liver damage

    Journal: Journal of Molecular Histology

    doi: 10.1007/s10735-023-10127-8

    Effect of genistein on expression and phosphorylation of EGFR during experimental CCl 4 -induced subacute liver damage. An increase in total protein and phosphorylation from livers with CCl 4 -induced subacute liver damage was observed. Genistein significantly increased total protein and pY845 and pY1068 EGFR. The analysis was determined by Western blot a semiquantitative analysis of the expression levels of p‑EGFR (Y845, Y992 and Y1068), β-actin was used as a loading control. Bars show the mean values ± standard deviations of the band density normalized to the total protein. n = 8, *p < 0.05 as compared to control group; #p < 0.05 as compared to liver damage group, respectively using an ANOVA and Tukey’s test
    Figure Legend Snippet: Effect of genistein on expression and phosphorylation of EGFR during experimental CCl 4 -induced subacute liver damage. An increase in total protein and phosphorylation from livers with CCl 4 -induced subacute liver damage was observed. Genistein significantly increased total protein and pY845 and pY1068 EGFR. The analysis was determined by Western blot a semiquantitative analysis of the expression levels of p‑EGFR (Y845, Y992 and Y1068), β-actin was used as a loading control. Bars show the mean values ± standard deviations of the band density normalized to the total protein. n = 8, *p < 0.05 as compared to control group; #p < 0.05 as compared to liver damage group, respectively using an ANOVA and Tukey’s test

    Techniques Used: Expressing, Western Blot

    anti phospho egfr y1068  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho egfr y1068
    Anti Phospho Egfr Y1068, supplied by Cell Signaling Technology 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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    anti phospho egfr y1068  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho egfr y1068
    Anti Phospho Egfr Y1068, supplied by Cell Signaling Technology 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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    antibodies anti phospho egfr y1068  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc antibodies anti phospho egfr y1068
    Antibodies Anti Phospho Egfr Y1068, supplied by Cell Signaling Technology 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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    anti phospho egfr y1068  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho egfr y1068
    Representative fluorescence micrographs of in cell EGF‐Alexa647 (0–320 ng/ml) dose–response imaging of EGFR phosphorylation in EmCit_MCF7 cells. Concentrations of EGF‐Alexa647 were increased at 1.5′ time interval and are shown as cumulative dose in ng/ml and corresponding relative receptor occupancies (α L ), obtained by normalizing the ratiometric fluorescence of EGF‐Alexa647/EGFR‐mCitrine to that at saturating EGF‐Alexa647 dose. First row: EGF‐Alexa647; Second row: EGFR‐mCitrine; Third row: phosphorylated EGFR‐mCitrine fraction (α p ); Scale bar: 10 μm. Left: Peak normalized photon intensity distribution histograms as a function of their time of arrival obtained from time‐correlated single photon counting measurements of EGFR‐mCitrine (with PTB‐mCherry as FRET‐acceptor; Fig ) at different cumulative EGF‐Alexa647 doses (A) (color code in inset). Right: Average fluorescence lifetime of mCitrine (τ avg, ns) obtained by integrating the area under individual normalized decay curves as a function of cumulative EGF‐Alexa647 dose. Left: fraction of EGF‐Alexa647 binding to EGFR‐mCitrine (receptor occupancy α L ) upon each administered dose (cumulative doses 2.5–640 ng/ml), middle: fraction of phosphorylated EGFR‐mCitrine (α p ) derived from FLIM measurments as a function of administered EGF‐Alexa647 dose, right: α p plotted against α L . Colored thin lines: individual cell profiles; Solid red line with shaded bounds: moving median with median absolute deviation. Same as (A) for RPTPγ‐KO EmCit_MCF7 cells. Same as (A) for p22 phox ‐KO EmCit_MCF7 cells. Top row: Left: Representative western blot showing EGFR (top) and corresponding phosphorylation response at <t>Y1068</t> (bottom) in lysates of MCF7 WT cells as a function of indicated EGF‐Alexa647 stimulus for 5′. Lysate from cells treated for 5′ with 0.33 mM of PTP‐inhibitor pervanadate (PV, last lane) was used as a positive control for EGFR‐phosphorylation. Middle: Same for Akt (top) and phosphorylation at pS473 (bottom). Right: Same for Erk (top) and phosphorylation at pT202 and pY204 (bottom). Bottom row: Quantification of phosphorylated Akt (pS473/Akt total ; left) and (pErk/Erk total ; right) as a function of the receptor occupancy α L (C) corresponding to the applied doses of EGF‐Alexa647. N = 4 biological replicates, mean (red symbols) ± SD and fit to the hill equation (solid black line). Inserts: Hill coefficient (HC) and EC50 of the fitted hill equation (95% confidence interval). Left: RPTPγ‐mTFP/EGFR‐mCitrine fluorescence ratio of individual EmCit_MCF7 RPTPγ‐KO cells with RPTPγ‐mTFP ectopic expression plotted against Hill coefficient (HC) obtained from fitting the hill equation to the corresponding in cell EGF‐dose response (compare Fig , N = 3 biological replicates, n = 23 cells) with colored lines encircling data points of the three clusters; Middle/Right: HC versus RPTPγ‐mTFP/EGFR‐mCitrine range of the three clusters; mean ± SD ( y ‐axis) and full range of values ( x ‐axis), P : unpaired two‐tailed t ‐test. Representative western blot showing RPTPγ (top row) and Na + /K + ATPase as a loading control (bottom row) in membrane protein extract lysates of WT MCF7 and MCF7‐RPTPγ‐KO cells stably expressing RPTPγ‐mCitrine. 17 (left and middle) and 28 (right) times more total protein was loaded for WT cells compared to MCF7‐RPTPγ‐KO cells expressing RPTPγ‐mCitrine to maintain band intensity within the dynamic range of the fluorescence detector of the scanner. Western blot showing endogenous TCPTP expression (top row) and GAPDH (loading control; bottom row) in cell lysates obtained from WT with (lane1) and without (lane2) ectopic TCPTP expression and different clones of MCF7 cells subjected to CRISPR‐Cas9 mediated TCPTP‐KO (3–7 lanes). Same as (A) for TCPTP‐KO EmCit_MCF7 cells. Same as (A) for TCPTP‐KO EmCit_MCF7 cells with TCPTP‐mTFP (fourth row) ectopic expression. Data information: All scale bars: 10 μm.
    Anti Phospho Egfr Y1068, supplied by Cell Signaling Technology 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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    Average 86 stars, based on 1 article reviews
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    anti phospho egfr y1068 - by Bioz Stars, 2023-09
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    Images

    1) Product Images from "The EGFR phosphatase RPTPγ is a redox‐regulated suppressor of promigratory signaling"

    Article Title: The EGFR phosphatase RPTPγ is a redox‐regulated suppressor of promigratory signaling

    Journal: The EMBO Journal

    doi: 10.15252/embj.2022111806

    Representative fluorescence micrographs of in cell EGF‐Alexa647 (0–320 ng/ml) dose–response imaging of EGFR phosphorylation in EmCit_MCF7 cells. Concentrations of EGF‐Alexa647 were increased at 1.5′ time interval and are shown as cumulative dose in ng/ml and corresponding relative receptor occupancies (α L ), obtained by normalizing the ratiometric fluorescence of EGF‐Alexa647/EGFR‐mCitrine to that at saturating EGF‐Alexa647 dose. First row: EGF‐Alexa647; Second row: EGFR‐mCitrine; Third row: phosphorylated EGFR‐mCitrine fraction (α p ); Scale bar: 10 μm. Left: Peak normalized photon intensity distribution histograms as a function of their time of arrival obtained from time‐correlated single photon counting measurements of EGFR‐mCitrine (with PTB‐mCherry as FRET‐acceptor; Fig ) at different cumulative EGF‐Alexa647 doses (A) (color code in inset). Right: Average fluorescence lifetime of mCitrine (τ avg, ns) obtained by integrating the area under individual normalized decay curves as a function of cumulative EGF‐Alexa647 dose. Left: fraction of EGF‐Alexa647 binding to EGFR‐mCitrine (receptor occupancy α L ) upon each administered dose (cumulative doses 2.5–640 ng/ml), middle: fraction of phosphorylated EGFR‐mCitrine (α p ) derived from FLIM measurments as a function of administered EGF‐Alexa647 dose, right: α p plotted against α L . Colored thin lines: individual cell profiles; Solid red line with shaded bounds: moving median with median absolute deviation. Same as (A) for RPTPγ‐KO EmCit_MCF7 cells. Same as (A) for p22 phox ‐KO EmCit_MCF7 cells. Top row: Left: Representative western blot showing EGFR (top) and corresponding phosphorylation response at Y1068 (bottom) in lysates of MCF7 WT cells as a function of indicated EGF‐Alexa647 stimulus for 5′. Lysate from cells treated for 5′ with 0.33 mM of PTP‐inhibitor pervanadate (PV, last lane) was used as a positive control for EGFR‐phosphorylation. Middle: Same for Akt (top) and phosphorylation at pS473 (bottom). Right: Same for Erk (top) and phosphorylation at pT202 and pY204 (bottom). Bottom row: Quantification of phosphorylated Akt (pS473/Akt total ; left) and (pErk/Erk total ; right) as a function of the receptor occupancy α L (C) corresponding to the applied doses of EGF‐Alexa647. N = 4 biological replicates, mean (red symbols) ± SD and fit to the hill equation (solid black line). Inserts: Hill coefficient (HC) and EC50 of the fitted hill equation (95% confidence interval). Left: RPTPγ‐mTFP/EGFR‐mCitrine fluorescence ratio of individual EmCit_MCF7 RPTPγ‐KO cells with RPTPγ‐mTFP ectopic expression plotted against Hill coefficient (HC) obtained from fitting the hill equation to the corresponding in cell EGF‐dose response (compare Fig , N = 3 biological replicates, n = 23 cells) with colored lines encircling data points of the three clusters; Middle/Right: HC versus RPTPγ‐mTFP/EGFR‐mCitrine range of the three clusters; mean ± SD ( y ‐axis) and full range of values ( x ‐axis), P : unpaired two‐tailed t ‐test. Representative western blot showing RPTPγ (top row) and Na + /K + ATPase as a loading control (bottom row) in membrane protein extract lysates of WT MCF7 and MCF7‐RPTPγ‐KO cells stably expressing RPTPγ‐mCitrine. 17 (left and middle) and 28 (right) times more total protein was loaded for WT cells compared to MCF7‐RPTPγ‐KO cells expressing RPTPγ‐mCitrine to maintain band intensity within the dynamic range of the fluorescence detector of the scanner. Western blot showing endogenous TCPTP expression (top row) and GAPDH (loading control; bottom row) in cell lysates obtained from WT with (lane1) and without (lane2) ectopic TCPTP expression and different clones of MCF7 cells subjected to CRISPR‐Cas9 mediated TCPTP‐KO (3–7 lanes). Same as (A) for TCPTP‐KO EmCit_MCF7 cells. Same as (A) for TCPTP‐KO EmCit_MCF7 cells with TCPTP‐mTFP (fourth row) ectopic expression. Data information: All scale bars: 10 μm.
    Figure Legend Snippet: Representative fluorescence micrographs of in cell EGF‐Alexa647 (0–320 ng/ml) dose–response imaging of EGFR phosphorylation in EmCit_MCF7 cells. Concentrations of EGF‐Alexa647 were increased at 1.5′ time interval and are shown as cumulative dose in ng/ml and corresponding relative receptor occupancies (α L ), obtained by normalizing the ratiometric fluorescence of EGF‐Alexa647/EGFR‐mCitrine to that at saturating EGF‐Alexa647 dose. First row: EGF‐Alexa647; Second row: EGFR‐mCitrine; Third row: phosphorylated EGFR‐mCitrine fraction (α p ); Scale bar: 10 μm. Left: Peak normalized photon intensity distribution histograms as a function of their time of arrival obtained from time‐correlated single photon counting measurements of EGFR‐mCitrine (with PTB‐mCherry as FRET‐acceptor; Fig ) at different cumulative EGF‐Alexa647 doses (A) (color code in inset). Right: Average fluorescence lifetime of mCitrine (τ avg, ns) obtained by integrating the area under individual normalized decay curves as a function of cumulative EGF‐Alexa647 dose. Left: fraction of EGF‐Alexa647 binding to EGFR‐mCitrine (receptor occupancy α L ) upon each administered dose (cumulative doses 2.5–640 ng/ml), middle: fraction of phosphorylated EGFR‐mCitrine (α p ) derived from FLIM measurments as a function of administered EGF‐Alexa647 dose, right: α p plotted against α L . Colored thin lines: individual cell profiles; Solid red line with shaded bounds: moving median with median absolute deviation. Same as (A) for RPTPγ‐KO EmCit_MCF7 cells. Same as (A) for p22 phox ‐KO EmCit_MCF7 cells. Top row: Left: Representative western blot showing EGFR (top) and corresponding phosphorylation response at Y1068 (bottom) in lysates of MCF7 WT cells as a function of indicated EGF‐Alexa647 stimulus for 5′. Lysate from cells treated for 5′ with 0.33 mM of PTP‐inhibitor pervanadate (PV, last lane) was used as a positive control for EGFR‐phosphorylation. Middle: Same for Akt (top) and phosphorylation at pS473 (bottom). Right: Same for Erk (top) and phosphorylation at pT202 and pY204 (bottom). Bottom row: Quantification of phosphorylated Akt (pS473/Akt total ; left) and (pErk/Erk total ; right) as a function of the receptor occupancy α L (C) corresponding to the applied doses of EGF‐Alexa647. N = 4 biological replicates, mean (red symbols) ± SD and fit to the hill equation (solid black line). Inserts: Hill coefficient (HC) and EC50 of the fitted hill equation (95% confidence interval). Left: RPTPγ‐mTFP/EGFR‐mCitrine fluorescence ratio of individual EmCit_MCF7 RPTPγ‐KO cells with RPTPγ‐mTFP ectopic expression plotted against Hill coefficient (HC) obtained from fitting the hill equation to the corresponding in cell EGF‐dose response (compare Fig , N = 3 biological replicates, n = 23 cells) with colored lines encircling data points of the three clusters; Middle/Right: HC versus RPTPγ‐mTFP/EGFR‐mCitrine range of the three clusters; mean ± SD ( y ‐axis) and full range of values ( x ‐axis), P : unpaired two‐tailed t ‐test. Representative western blot showing RPTPγ (top row) and Na + /K + ATPase as a loading control (bottom row) in membrane protein extract lysates of WT MCF7 and MCF7‐RPTPγ‐KO cells stably expressing RPTPγ‐mCitrine. 17 (left and middle) and 28 (right) times more total protein was loaded for WT cells compared to MCF7‐RPTPγ‐KO cells expressing RPTPγ‐mCitrine to maintain band intensity within the dynamic range of the fluorescence detector of the scanner. Western blot showing endogenous TCPTP expression (top row) and GAPDH (loading control; bottom row) in cell lysates obtained from WT with (lane1) and without (lane2) ectopic TCPTP expression and different clones of MCF7 cells subjected to CRISPR‐Cas9 mediated TCPTP‐KO (3–7 lanes). Same as (A) for TCPTP‐KO EmCit_MCF7 cells. Same as (A) for TCPTP‐KO EmCit_MCF7 cells with TCPTP‐mTFP (fourth row) ectopic expression. Data information: All scale bars: 10 μm.

    Techniques Used: Fluorescence, Imaging, Binding Assay, Derivative Assay, Western Blot, Positive Control, Expressing, Two Tailed Test, Stable Transfection, Clone Assay, CRISPR

    anti phospho egfr y1068  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho egfr y1068
    Representative fluorescence micrographs of in cell EGF‐Alexa647 (0–320 ng/ml) dose–response imaging of EGFR phosphorylation in EmCit_MCF7 cells. Concentrations of EGF‐Alexa647 were increased at 1.5′ time interval and are shown as cumulative dose in ng/ml and corresponding relative receptor occupancies (α L ), obtained by normalizing the ratiometric fluorescence of EGF‐Alexa647/EGFR‐mCitrine to that at saturating EGF‐Alexa647 dose. First row: EGF‐Alexa647; Second row: EGFR‐mCitrine; Third row: phosphorylated EGFR‐mCitrine fraction (α p ); Scale bar: 10 μm. Left: Peak normalized photon intensity distribution histograms as a function of their time of arrival obtained from time‐correlated single photon counting measurements of EGFR‐mCitrine (with PTB‐mCherry as FRET‐acceptor; Fig ) at different cumulative EGF‐Alexa647 doses (A) (color code in inset). Right: Average fluorescence lifetime of mCitrine (τ avg, ns) obtained by integrating the area under individual normalized decay curves as a function of cumulative EGF‐Alexa647 dose. Left: fraction of EGF‐Alexa647 binding to EGFR‐mCitrine (receptor occupancy α L ) upon each administered dose (cumulative doses 2.5–640 ng/ml), middle: fraction of phosphorylated EGFR‐mCitrine (α p ) derived from FLIM measurments as a function of administered EGF‐Alexa647 dose, right: α p plotted against α L . Colored thin lines: individual cell profiles; Solid red line with shaded bounds: moving median with median absolute deviation. Same as (A) for RPTPγ‐KO EmCit_MCF7 cells. Same as (A) for p22 phox ‐KO EmCit_MCF7 cells. Top row: Left: Representative western blot showing EGFR (top) and corresponding phosphorylation response at <t>Y1068</t> (bottom) in lysates of MCF7 WT cells as a function of indicated EGF‐Alexa647 stimulus for 5′. Lysate from cells treated for 5′ with 0.33 mM of PTP‐inhibitor pervanadate (PV, last lane) was used as a positive control for EGFR‐phosphorylation. Middle: Same for Akt (top) and phosphorylation at pS473 (bottom). Right: Same for Erk (top) and phosphorylation at pT202 and pY204 (bottom). Bottom row: Quantification of phosphorylated Akt (pS473/Akt total ; left) and (pErk/Erk total ; right) as a function of the receptor occupancy α L (C) corresponding to the applied doses of EGF‐Alexa647. N = 4 biological replicates, mean (red symbols) ± SD and fit to the hill equation (solid black line). Inserts: Hill coefficient (HC) and EC50 of the fitted hill equation (95% confidence interval). Left: RPTPγ‐mTFP/EGFR‐mCitrine fluorescence ratio of individual EmCit_MCF7 RPTPγ‐KO cells with RPTPγ‐mTFP ectopic expression plotted against Hill coefficient (HC) obtained from fitting the hill equation to the corresponding in cell EGF‐dose response (compare Fig , N = 3 biological replicates, n = 23 cells) with colored lines encircling data points of the three clusters; Middle/Right: HC versus RPTPγ‐mTFP/EGFR‐mCitrine range of the three clusters; mean ± SD ( y ‐axis) and full range of values ( x ‐axis), P : unpaired two‐tailed t ‐test. Representative western blot showing RPTPγ (top row) and Na + /K + ATPase as a loading control (bottom row) in membrane protein extract lysates of WT MCF7 and MCF7‐RPTPγ‐KO cells stably expressing RPTPγ‐mCitrine. 17 (left and middle) and 28 (right) times more total protein was loaded for WT cells compared to MCF7‐RPTPγ‐KO cells expressing RPTPγ‐mCitrine to maintain band intensity within the dynamic range of the fluorescence detector of the scanner. Western blot showing endogenous TCPTP expression (top row) and GAPDH (loading control; bottom row) in cell lysates obtained from WT with (lane1) and without (lane2) ectopic TCPTP expression and different clones of MCF7 cells subjected to CRISPR‐Cas9 mediated TCPTP‐KO (3–7 lanes). Same as (A) for TCPTP‐KO EmCit_MCF7 cells. Same as (A) for TCPTP‐KO EmCit_MCF7 cells with TCPTP‐mTFP (fourth row) ectopic expression. Data information: All scale bars: 10 μm.
    Anti Phospho Egfr Y1068, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho egfr y1068/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti phospho egfr y1068 - by Bioz Stars, 2023-09
    86/100 stars

    Images

    1) Product Images from "The EGFR phosphatase RPTPγ is a redox‐regulated suppressor of promigratory signaling"

    Article Title: The EGFR phosphatase RPTPγ is a redox‐regulated suppressor of promigratory signaling

    Journal: The EMBO Journal

    doi: 10.15252/embj.2022111806

    Representative fluorescence micrographs of in cell EGF‐Alexa647 (0–320 ng/ml) dose–response imaging of EGFR phosphorylation in EmCit_MCF7 cells. Concentrations of EGF‐Alexa647 were increased at 1.5′ time interval and are shown as cumulative dose in ng/ml and corresponding relative receptor occupancies (α L ), obtained by normalizing the ratiometric fluorescence of EGF‐Alexa647/EGFR‐mCitrine to that at saturating EGF‐Alexa647 dose. First row: EGF‐Alexa647; Second row: EGFR‐mCitrine; Third row: phosphorylated EGFR‐mCitrine fraction (α p ); Scale bar: 10 μm. Left: Peak normalized photon intensity distribution histograms as a function of their time of arrival obtained from time‐correlated single photon counting measurements of EGFR‐mCitrine (with PTB‐mCherry as FRET‐acceptor; Fig ) at different cumulative EGF‐Alexa647 doses (A) (color code in inset). Right: Average fluorescence lifetime of mCitrine (τ avg, ns) obtained by integrating the area under individual normalized decay curves as a function of cumulative EGF‐Alexa647 dose. Left: fraction of EGF‐Alexa647 binding to EGFR‐mCitrine (receptor occupancy α L ) upon each administered dose (cumulative doses 2.5–640 ng/ml), middle: fraction of phosphorylated EGFR‐mCitrine (α p ) derived from FLIM measurments as a function of administered EGF‐Alexa647 dose, right: α p plotted against α L . Colored thin lines: individual cell profiles; Solid red line with shaded bounds: moving median with median absolute deviation. Same as (A) for RPTPγ‐KO EmCit_MCF7 cells. Same as (A) for p22 phox ‐KO EmCit_MCF7 cells. Top row: Left: Representative western blot showing EGFR (top) and corresponding phosphorylation response at Y1068 (bottom) in lysates of MCF7 WT cells as a function of indicated EGF‐Alexa647 stimulus for 5′. Lysate from cells treated for 5′ with 0.33 mM of PTP‐inhibitor pervanadate (PV, last lane) was used as a positive control for EGFR‐phosphorylation. Middle: Same for Akt (top) and phosphorylation at pS473 (bottom). Right: Same for Erk (top) and phosphorylation at pT202 and pY204 (bottom). Bottom row: Quantification of phosphorylated Akt (pS473/Akt total ; left) and (pErk/Erk total ; right) as a function of the receptor occupancy α L (C) corresponding to the applied doses of EGF‐Alexa647. N = 4 biological replicates, mean (red symbols) ± SD and fit to the hill equation (solid black line). Inserts: Hill coefficient (HC) and EC50 of the fitted hill equation (95% confidence interval). Left: RPTPγ‐mTFP/EGFR‐mCitrine fluorescence ratio of individual EmCit_MCF7 RPTPγ‐KO cells with RPTPγ‐mTFP ectopic expression plotted against Hill coefficient (HC) obtained from fitting the hill equation to the corresponding in cell EGF‐dose response (compare Fig , N = 3 biological replicates, n = 23 cells) with colored lines encircling data points of the three clusters; Middle/Right: HC versus RPTPγ‐mTFP/EGFR‐mCitrine range of the three clusters; mean ± SD ( y ‐axis) and full range of values ( x ‐axis), P : unpaired two‐tailed t ‐test. Representative western blot showing RPTPγ (top row) and Na + /K + ATPase as a loading control (bottom row) in membrane protein extract lysates of WT MCF7 and MCF7‐RPTPγ‐KO cells stably expressing RPTPγ‐mCitrine. 17 (left and middle) and 28 (right) times more total protein was loaded for WT cells compared to MCF7‐RPTPγ‐KO cells expressing RPTPγ‐mCitrine to maintain band intensity within the dynamic range of the fluorescence detector of the scanner. Western blot showing endogenous TCPTP expression (top row) and GAPDH (loading control; bottom row) in cell lysates obtained from WT with (lane1) and without (lane2) ectopic TCPTP expression and different clones of MCF7 cells subjected to CRISPR‐Cas9 mediated TCPTP‐KO (3–7 lanes). Same as (A) for TCPTP‐KO EmCit_MCF7 cells. Same as (A) for TCPTP‐KO EmCit_MCF7 cells with TCPTP‐mTFP (fourth row) ectopic expression. Data information: All scale bars: 10 μm.
    Figure Legend Snippet: Representative fluorescence micrographs of in cell EGF‐Alexa647 (0–320 ng/ml) dose–response imaging of EGFR phosphorylation in EmCit_MCF7 cells. Concentrations of EGF‐Alexa647 were increased at 1.5′ time interval and are shown as cumulative dose in ng/ml and corresponding relative receptor occupancies (α L ), obtained by normalizing the ratiometric fluorescence of EGF‐Alexa647/EGFR‐mCitrine to that at saturating EGF‐Alexa647 dose. First row: EGF‐Alexa647; Second row: EGFR‐mCitrine; Third row: phosphorylated EGFR‐mCitrine fraction (α p ); Scale bar: 10 μm. Left: Peak normalized photon intensity distribution histograms as a function of their time of arrival obtained from time‐correlated single photon counting measurements of EGFR‐mCitrine (with PTB‐mCherry as FRET‐acceptor; Fig ) at different cumulative EGF‐Alexa647 doses (A) (color code in inset). Right: Average fluorescence lifetime of mCitrine (τ avg, ns) obtained by integrating the area under individual normalized decay curves as a function of cumulative EGF‐Alexa647 dose. Left: fraction of EGF‐Alexa647 binding to EGFR‐mCitrine (receptor occupancy α L ) upon each administered dose (cumulative doses 2.5–640 ng/ml), middle: fraction of phosphorylated EGFR‐mCitrine (α p ) derived from FLIM measurments as a function of administered EGF‐Alexa647 dose, right: α p plotted against α L . Colored thin lines: individual cell profiles; Solid red line with shaded bounds: moving median with median absolute deviation. Same as (A) for RPTPγ‐KO EmCit_MCF7 cells. Same as (A) for p22 phox ‐KO EmCit_MCF7 cells. Top row: Left: Representative western blot showing EGFR (top) and corresponding phosphorylation response at Y1068 (bottom) in lysates of MCF7 WT cells as a function of indicated EGF‐Alexa647 stimulus for 5′. Lysate from cells treated for 5′ with 0.33 mM of PTP‐inhibitor pervanadate (PV, last lane) was used as a positive control for EGFR‐phosphorylation. Middle: Same for Akt (top) and phosphorylation at pS473 (bottom). Right: Same for Erk (top) and phosphorylation at pT202 and pY204 (bottom). Bottom row: Quantification of phosphorylated Akt (pS473/Akt total ; left) and (pErk/Erk total ; right) as a function of the receptor occupancy α L (C) corresponding to the applied doses of EGF‐Alexa647. N = 4 biological replicates, mean (red symbols) ± SD and fit to the hill equation (solid black line). Inserts: Hill coefficient (HC) and EC50 of the fitted hill equation (95% confidence interval). Left: RPTPγ‐mTFP/EGFR‐mCitrine fluorescence ratio of individual EmCit_MCF7 RPTPγ‐KO cells with RPTPγ‐mTFP ectopic expression plotted against Hill coefficient (HC) obtained from fitting the hill equation to the corresponding in cell EGF‐dose response (compare Fig , N = 3 biological replicates, n = 23 cells) with colored lines encircling data points of the three clusters; Middle/Right: HC versus RPTPγ‐mTFP/EGFR‐mCitrine range of the three clusters; mean ± SD ( y ‐axis) and full range of values ( x ‐axis), P : unpaired two‐tailed t ‐test. Representative western blot showing RPTPγ (top row) and Na + /K + ATPase as a loading control (bottom row) in membrane protein extract lysates of WT MCF7 and MCF7‐RPTPγ‐KO cells stably expressing RPTPγ‐mCitrine. 17 (left and middle) and 28 (right) times more total protein was loaded for WT cells compared to MCF7‐RPTPγ‐KO cells expressing RPTPγ‐mCitrine to maintain band intensity within the dynamic range of the fluorescence detector of the scanner. Western blot showing endogenous TCPTP expression (top row) and GAPDH (loading control; bottom row) in cell lysates obtained from WT with (lane1) and without (lane2) ectopic TCPTP expression and different clones of MCF7 cells subjected to CRISPR‐Cas9 mediated TCPTP‐KO (3–7 lanes). Same as (A) for TCPTP‐KO EmCit_MCF7 cells. Same as (A) for TCPTP‐KO EmCit_MCF7 cells with TCPTP‐mTFP (fourth row) ectopic expression. Data information: All scale bars: 10 μm.

    Techniques Used: Fluorescence, Imaging, Binding Assay, Derivative Assay, Western Blot, Positive Control, Expressing, Two Tailed Test, Stable Transfection, Clone Assay, CRISPR

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