anti phospho src y416  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho src y416
    The effect of TAT-Cx43 266–283 depends on EGFR alterations. A set of murine SVZ NSCs with EGFR alterations (SVZ-EGFRwt and SVZ-EGFRvIII) and a set of murine SVZ NSCs with EGFRvIII mutation (NSC-EGFRvIII), with Nf1/PTEN deletion (NP) or with a combination of Nf1/PTEN deletion and EGFRvIII mutation (NPE, and their immune evasive version, NPE-IE) and their non-modified counterparts (SVZ-NSCs) were treated with 50 µM TAT, 50 µM TAT-Cx43 274–291 (2 cell-penetrating peptides used as additional controls), 50 µM TAT-Cx43 266–283 , 100 µM temozolomide, 1 µM erlotinib, 0.05% DMSO (v/v) (vehicle for erlotinib) and the combination of 1 µM erlotinib plus 50 µM TAT-Cx43 266–283 . (A) Alamar blue viability assay of SVZ NSCs with EGFR alterations and healthy NSCs after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: * P < .05, *** P < .001 vs control; ## P < .01, ### P < .001 vs TAT; @@ P < .01 vs TAT-Cx43 274-291 ; +++ P < .001 vs temozolomide). (B) Phase-contrast images of murine NSCs with and without EGFR alterations treated as described previously. Scale bar: 100 µm. (C) WB analysis of EGFR and EGFRvIII levels and activity (p-EGFR Y1068 and p-EGFRvIII Y1068) after 24 h treatment. GAPDH was used as a loading control. (D) Alamar blue viability assay of SVZ NSCs with EGFR and additional GBM-driver alterations after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: *** P value < .001). (E) Phase-contrast images of murine SVZ NSCs with GBM-driver alterations treated as described in (A). Scale bar: 100 µm. (F) WB analysis of EGFR, EGFRvIII, and Src levels and activity (p-EGFR Y1068, p-EGFRvIII Y1068, and p-Src <t>Y416)</t> after 24 h treatment. β-actin was used as a loading control. (G) Correlation graph depicting the relationship between GSC EGFR status and Src inhibition after treatment with TAT-Cx43 266–283 in murine and patient-derived GSCs. (H) Contingency table graph showing the magnitude of TAT-Cx43 266–283 response and EGFR status of all the murine NSCs and GSCs. χ 2 test was used for statistical analysis.
    Anti Phospho Src Y416, 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 src y416/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
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    1) Product Images from "EGFR amplification and EGFRvIII predict and participate in TAT-Cx43 266–283 antitumor response in preclinical glioblastoma models"

    Article Title: EGFR amplification and EGFRvIII predict and participate in TAT-Cx43 266–283 antitumor response in preclinical glioblastoma models

    Journal: Neuro-Oncology

    doi: 10.1093/neuonc/noae060

    The effect of TAT-Cx43 266–283 depends on EGFR alterations. A set of murine SVZ NSCs with EGFR alterations (SVZ-EGFRwt and SVZ-EGFRvIII) and a set of murine SVZ NSCs with EGFRvIII mutation (NSC-EGFRvIII), with Nf1/PTEN deletion (NP) or with a combination of Nf1/PTEN deletion and EGFRvIII mutation (NPE, and their immune evasive version, NPE-IE) and their non-modified counterparts (SVZ-NSCs) were treated with 50 µM TAT, 50 µM TAT-Cx43 274–291 (2 cell-penetrating peptides used as additional controls), 50 µM TAT-Cx43 266–283 , 100 µM temozolomide, 1 µM erlotinib, 0.05% DMSO (v/v) (vehicle for erlotinib) and the combination of 1 µM erlotinib plus 50 µM TAT-Cx43 266–283 . (A) Alamar blue viability assay of SVZ NSCs with EGFR alterations and healthy NSCs after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: * P < .05, *** P < .001 vs control; ## P < .01, ### P < .001 vs TAT; @@ P < .01 vs TAT-Cx43 274-291 ; +++ P < .001 vs temozolomide). (B) Phase-contrast images of murine NSCs with and without EGFR alterations treated as described previously. Scale bar: 100 µm. (C) WB analysis of EGFR and EGFRvIII levels and activity (p-EGFR Y1068 and p-EGFRvIII Y1068) after 24 h treatment. GAPDH was used as a loading control. (D) Alamar blue viability assay of SVZ NSCs with EGFR and additional GBM-driver alterations after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: *** P value < .001). (E) Phase-contrast images of murine SVZ NSCs with GBM-driver alterations treated as described in (A). Scale bar: 100 µm. (F) WB analysis of EGFR, EGFRvIII, and Src levels and activity (p-EGFR Y1068, p-EGFRvIII Y1068, and p-Src Y416) after 24 h treatment. β-actin was used as a loading control. (G) Correlation graph depicting the relationship between GSC EGFR status and Src inhibition after treatment with TAT-Cx43 266–283 in murine and patient-derived GSCs. (H) Contingency table graph showing the magnitude of TAT-Cx43 266–283 response and EGFR status of all the murine NSCs and GSCs. χ 2 test was used for statistical analysis.
    Figure Legend Snippet: The effect of TAT-Cx43 266–283 depends on EGFR alterations. A set of murine SVZ NSCs with EGFR alterations (SVZ-EGFRwt and SVZ-EGFRvIII) and a set of murine SVZ NSCs with EGFRvIII mutation (NSC-EGFRvIII), with Nf1/PTEN deletion (NP) or with a combination of Nf1/PTEN deletion and EGFRvIII mutation (NPE, and their immune evasive version, NPE-IE) and their non-modified counterparts (SVZ-NSCs) were treated with 50 µM TAT, 50 µM TAT-Cx43 274–291 (2 cell-penetrating peptides used as additional controls), 50 µM TAT-Cx43 266–283 , 100 µM temozolomide, 1 µM erlotinib, 0.05% DMSO (v/v) (vehicle for erlotinib) and the combination of 1 µM erlotinib plus 50 µM TAT-Cx43 266–283 . (A) Alamar blue viability assay of SVZ NSCs with EGFR alterations and healthy NSCs after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: * P < .05, *** P < .001 vs control; ## P < .01, ### P < .001 vs TAT; @@ P < .01 vs TAT-Cx43 274-291 ; +++ P < .001 vs temozolomide). (B) Phase-contrast images of murine NSCs with and without EGFR alterations treated as described previously. Scale bar: 100 µm. (C) WB analysis of EGFR and EGFRvIII levels and activity (p-EGFR Y1068 and p-EGFRvIII Y1068) after 24 h treatment. GAPDH was used as a loading control. (D) Alamar blue viability assay of SVZ NSCs with EGFR and additional GBM-driver alterations after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: *** P value < .001). (E) Phase-contrast images of murine SVZ NSCs with GBM-driver alterations treated as described in (A). Scale bar: 100 µm. (F) WB analysis of EGFR, EGFRvIII, and Src levels and activity (p-EGFR Y1068, p-EGFRvIII Y1068, and p-Src Y416) after 24 h treatment. β-actin was used as a loading control. (G) Correlation graph depicting the relationship between GSC EGFR status and Src inhibition after treatment with TAT-Cx43 266–283 in murine and patient-derived GSCs. (H) Contingency table graph showing the magnitude of TAT-Cx43 266–283 response and EGFR status of all the murine NSCs and GSCs. χ 2 test was used for statistical analysis.

    Techniques Used: Mutagenesis, Modification, Viability Assay, Control, Activity Assay, Inhibition, Derivative Assay

    EGFR alterations correlate with Src activity in GBM patients. Analyses were carried out using IDHwt GBM samples from the TCGA GBM database. (A) Volcano plot depicting levels of proteins in GBM patients with or without EGFR alterations. (B) Proteins with significantly higher levels in patients with EGFR alterations (see for a complete list). (C) Comparative graph of p-Src Y416 levels in patients with and without EGFR alterations (Student’s t -test, *** P value < .001). (D) Correlation graph showing the relationship between EGFR mRNA expression and p-Src Y416 protein levels in GBM patients. (E) Overall survival curve of patients with and without EGFR alterations (log-rank test, * P value < .05).
    Figure Legend Snippet: EGFR alterations correlate with Src activity in GBM patients. Analyses were carried out using IDHwt GBM samples from the TCGA GBM database. (A) Volcano plot depicting levels of proteins in GBM patients with or without EGFR alterations. (B) Proteins with significantly higher levels in patients with EGFR alterations (see for a complete list). (C) Comparative graph of p-Src Y416 levels in patients with and without EGFR alterations (Student’s t -test, *** P value < .001). (D) Correlation graph showing the relationship between EGFR mRNA expression and p-Src Y416 protein levels in GBM patients. (E) Overall survival curve of patients with and without EGFR alterations (log-rank test, * P value < .05).

    Techniques Used: Activity Assay, Expressing

    anti phospho src  (Danaher Inc)


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    Danaher Inc anti phospho src
    Anti Phospho Src, 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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    rabbit anti phospho src antibody for psfk  (Danaher Inc)


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    Danaher Inc rabbit anti phospho src antibody for psfk
    Rabbit Anti Phospho Src Antibody For Psfk, 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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    phospho src  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc phospho src
    Phospho Src, 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/phospho src/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
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    phospho src  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho src
    Phospho Src, 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/phospho src/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
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    phospho src - by Bioz Stars, 2024-07
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    phospho src  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc phospho src
    Phospho Src, 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/phospho src/product/Cell Signaling Technology Inc
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    phospho src y416 tyr416  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho src y416 tyr416
    Phospho Src Y416 Tyr416, 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 src phospho y418 1 1000 abcam  (Danaher Inc)


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    Danaher Inc anti src phospho y418 1 1000 abcam
    Anti Src Phospho Y418 1 1000 Abcam, 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
    https://www.bioz.com/result/anti src phospho y418 1 1000 abcam/product/Danaher Inc
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    Structured Review

    ABclonal Biotechnology anti phospho src y419 antibody
    Low concentrations of SAR promote Definitive Endoderm (DE) differentiation. DE differentiation was performed using the previously reported protocol ( A ) for 3 days. After 3 days of differentiation, total RNAs were extracted and the expressions of FOXA2 and SOX17 in DE cells derived from the H1 cells were determined by qPCR ( B ). ( C ) QPCR results of FOXA2 and SOX17 in two different ESC lines (H1 and H9) and two iPSC lines (K0 and β) treated with 0.5 µM SAR. ( D ) Flow cytometric analysis of DE cells derived from hESC line H1 expressing FOXA2 and SOX17 with or without the treatment of 0.5 µM SAR. ( E ) Quantitative statistics of FOXA2 + /SOX17 + cells corresponding to ( D ). ( F ) Immunofluorescent staining examined FOXA2 + (green) and SOX17 + (red) cells treated with 0.5 µM SAR differentiated from hESC line H1. The nucleus was counterstained with Hoechst 33,342. Quantitative statistics were shown in ( G ). ( H ) The p-Src <t>Y419</t> and Src protein levels in DE cells treated with different concentrations of SAR were detected using western blotting. GAPDH was used as a loading control. ( I ) Quantitative statistics of p-Src Y419/Src corresponding to H. Data are presented as mean ± SEM ( n = 3–8). * p < 0.05; ** p < 0.01; *** p < 0.001; ns, not significant
    Anti Phospho Src Y419 Antibody, supplied by ABclonal 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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    Images

    1) Product Images from "Low concentrations of saracatinib promote definitive endoderm differentiation through inhibition of FAK-YAP signaling axis"

    Article Title: Low concentrations of saracatinib promote definitive endoderm differentiation through inhibition of FAK-YAP signaling axis

    Journal: Cell Communication and Signaling : CCS

    doi: 10.1186/s12964-024-01679-7

    Low concentrations of SAR promote Definitive Endoderm (DE) differentiation. DE differentiation was performed using the previously reported protocol ( A ) for 3 days. After 3 days of differentiation, total RNAs were extracted and the expressions of FOXA2 and SOX17 in DE cells derived from the H1 cells were determined by qPCR ( B ). ( C ) QPCR results of FOXA2 and SOX17 in two different ESC lines (H1 and H9) and two iPSC lines (K0 and β) treated with 0.5 µM SAR. ( D ) Flow cytometric analysis of DE cells derived from hESC line H1 expressing FOXA2 and SOX17 with or without the treatment of 0.5 µM SAR. ( E ) Quantitative statistics of FOXA2 + /SOX17 + cells corresponding to ( D ). ( F ) Immunofluorescent staining examined FOXA2 + (green) and SOX17 + (red) cells treated with 0.5 µM SAR differentiated from hESC line H1. The nucleus was counterstained with Hoechst 33,342. Quantitative statistics were shown in ( G ). ( H ) The p-Src Y419 and Src protein levels in DE cells treated with different concentrations of SAR were detected using western blotting. GAPDH was used as a loading control. ( I ) Quantitative statistics of p-Src Y419/Src corresponding to H. Data are presented as mean ± SEM ( n = 3–8). * p < 0.05; ** p < 0.01; *** p < 0.001; ns, not significant
    Figure Legend Snippet: Low concentrations of SAR promote Definitive Endoderm (DE) differentiation. DE differentiation was performed using the previously reported protocol ( A ) for 3 days. After 3 days of differentiation, total RNAs were extracted and the expressions of FOXA2 and SOX17 in DE cells derived from the H1 cells were determined by qPCR ( B ). ( C ) QPCR results of FOXA2 and SOX17 in two different ESC lines (H1 and H9) and two iPSC lines (K0 and β) treated with 0.5 µM SAR. ( D ) Flow cytometric analysis of DE cells derived from hESC line H1 expressing FOXA2 and SOX17 with or without the treatment of 0.5 µM SAR. ( E ) Quantitative statistics of FOXA2 + /SOX17 + cells corresponding to ( D ). ( F ) Immunofluorescent staining examined FOXA2 + (green) and SOX17 + (red) cells treated with 0.5 µM SAR differentiated from hESC line H1. The nucleus was counterstained with Hoechst 33,342. Quantitative statistics were shown in ( G ). ( H ) The p-Src Y419 and Src protein levels in DE cells treated with different concentrations of SAR were detected using western blotting. GAPDH was used as a loading control. ( I ) Quantitative statistics of p-Src Y419/Src corresponding to H. Data are presented as mean ± SEM ( n = 3–8). * p < 0.05; ** p < 0.01; *** p < 0.001; ns, not significant

    Techniques Used: Derivative Assay, Expressing, Staining, Western Blot

    polyclonal rabbit anti phospho src tyr527 antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc polyclonal rabbit anti phospho src tyr527 antibody

    Polyclonal Rabbit Anti Phospho Src Tyr527 Antibody, 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/polyclonal rabbit anti phospho src tyr527 antibody/product/Cell Signaling Technology Inc
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    1) Product Images from "Acetyl-NPKY of integrin-β1 binds KINDLIN2 to control endothelial cell proliferation and junctional integrity"

    Article Title: Acetyl-NPKY of integrin-β1 binds KINDLIN2 to control endothelial cell proliferation and junctional integrity

    Journal: iScience

    doi: 10.1016/j.isci.2024.110129


    Figure Legend Snippet:

    Techniques Used: Virus, Recombinant, Synthesized, Real-time Polymerase Chain Reaction, Plasmid Preparation, Software

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    Cell Signaling Technology Inc anti phospho src y416
    The effect of TAT-Cx43 266–283 depends on EGFR alterations. A set of murine SVZ NSCs with EGFR alterations (SVZ-EGFRwt and SVZ-EGFRvIII) and a set of murine SVZ NSCs with EGFRvIII mutation (NSC-EGFRvIII), with Nf1/PTEN deletion (NP) or with a combination of Nf1/PTEN deletion and EGFRvIII mutation (NPE, and their immune evasive version, NPE-IE) and their non-modified counterparts (SVZ-NSCs) were treated with 50 µM TAT, 50 µM TAT-Cx43 274–291 (2 cell-penetrating peptides used as additional controls), 50 µM TAT-Cx43 266–283 , 100 µM temozolomide, 1 µM erlotinib, 0.05% DMSO (v/v) (vehicle for erlotinib) and the combination of 1 µM erlotinib plus 50 µM TAT-Cx43 266–283 . (A) Alamar blue viability assay of SVZ NSCs with EGFR alterations and healthy NSCs after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: * P < .05, *** P < .001 vs control; ## P < .01, ### P < .001 vs TAT; @@ P < .01 vs TAT-Cx43 274-291 ; +++ P < .001 vs temozolomide). (B) Phase-contrast images of murine NSCs with and without EGFR alterations treated as described previously. Scale bar: 100 µm. (C) WB analysis of EGFR and EGFRvIII levels and activity (p-EGFR Y1068 and p-EGFRvIII Y1068) after 24 h treatment. GAPDH was used as a loading control. (D) Alamar blue viability assay of SVZ NSCs with EGFR and additional GBM-driver alterations after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: *** P value < .001). (E) Phase-contrast images of murine SVZ NSCs with GBM-driver alterations treated as described in (A). Scale bar: 100 µm. (F) WB analysis of EGFR, EGFRvIII, and Src levels and activity (p-EGFR Y1068, p-EGFRvIII Y1068, and p-Src <t>Y416)</t> after 24 h treatment. β-actin was used as a loading control. (G) Correlation graph depicting the relationship between GSC EGFR status and Src inhibition after treatment with TAT-Cx43 266–283 in murine and patient-derived GSCs. (H) Contingency table graph showing the magnitude of TAT-Cx43 266–283 response and EGFR status of all the murine NSCs and GSCs. χ 2 test was used for statistical analysis.
    Anti Phospho Src Y416, 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 src y416/product/Cell Signaling Technology Inc
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    Danaher Inc anti phospho src
    The effect of TAT-Cx43 266–283 depends on EGFR alterations. A set of murine SVZ NSCs with EGFR alterations (SVZ-EGFRwt and SVZ-EGFRvIII) and a set of murine SVZ NSCs with EGFRvIII mutation (NSC-EGFRvIII), with Nf1/PTEN deletion (NP) or with a combination of Nf1/PTEN deletion and EGFRvIII mutation (NPE, and their immune evasive version, NPE-IE) and their non-modified counterparts (SVZ-NSCs) were treated with 50 µM TAT, 50 µM TAT-Cx43 274–291 (2 cell-penetrating peptides used as additional controls), 50 µM TAT-Cx43 266–283 , 100 µM temozolomide, 1 µM erlotinib, 0.05% DMSO (v/v) (vehicle for erlotinib) and the combination of 1 µM erlotinib plus 50 µM TAT-Cx43 266–283 . (A) Alamar blue viability assay of SVZ NSCs with EGFR alterations and healthy NSCs after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: * P < .05, *** P < .001 vs control; ## P < .01, ### P < .001 vs TAT; @@ P < .01 vs TAT-Cx43 274-291 ; +++ P < .001 vs temozolomide). (B) Phase-contrast images of murine NSCs with and without EGFR alterations treated as described previously. Scale bar: 100 µm. (C) WB analysis of EGFR and EGFRvIII levels and activity (p-EGFR Y1068 and p-EGFRvIII Y1068) after 24 h treatment. GAPDH was used as a loading control. (D) Alamar blue viability assay of SVZ NSCs with EGFR and additional GBM-driver alterations after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: *** P value < .001). (E) Phase-contrast images of murine SVZ NSCs with GBM-driver alterations treated as described in (A). Scale bar: 100 µm. (F) WB analysis of EGFR, EGFRvIII, and Src levels and activity (p-EGFR Y1068, p-EGFRvIII Y1068, and p-Src <t>Y416)</t> after 24 h treatment. β-actin was used as a loading control. (G) Correlation graph depicting the relationship between GSC EGFR status and Src inhibition after treatment with TAT-Cx43 266–283 in murine and patient-derived GSCs. (H) Contingency table graph showing the magnitude of TAT-Cx43 266–283 response and EGFR status of all the murine NSCs and GSCs. χ 2 test was used for statistical analysis.
    Anti Phospho Src, 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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    Danaher Inc rabbit anti phospho src antibody for psfk
    The effect of TAT-Cx43 266–283 depends on EGFR alterations. A set of murine SVZ NSCs with EGFR alterations (SVZ-EGFRwt and SVZ-EGFRvIII) and a set of murine SVZ NSCs with EGFRvIII mutation (NSC-EGFRvIII), with Nf1/PTEN deletion (NP) or with a combination of Nf1/PTEN deletion and EGFRvIII mutation (NPE, and their immune evasive version, NPE-IE) and their non-modified counterparts (SVZ-NSCs) were treated with 50 µM TAT, 50 µM TAT-Cx43 274–291 (2 cell-penetrating peptides used as additional controls), 50 µM TAT-Cx43 266–283 , 100 µM temozolomide, 1 µM erlotinib, 0.05% DMSO (v/v) (vehicle for erlotinib) and the combination of 1 µM erlotinib plus 50 µM TAT-Cx43 266–283 . (A) Alamar blue viability assay of SVZ NSCs with EGFR alterations and healthy NSCs after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: * P < .05, *** P < .001 vs control; ## P < .01, ### P < .001 vs TAT; @@ P < .01 vs TAT-Cx43 274-291 ; +++ P < .001 vs temozolomide). (B) Phase-contrast images of murine NSCs with and without EGFR alterations treated as described previously. Scale bar: 100 µm. (C) WB analysis of EGFR and EGFRvIII levels and activity (p-EGFR Y1068 and p-EGFRvIII Y1068) after 24 h treatment. GAPDH was used as a loading control. (D) Alamar blue viability assay of SVZ NSCs with EGFR and additional GBM-driver alterations after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: *** P value < .001). (E) Phase-contrast images of murine SVZ NSCs with GBM-driver alterations treated as described in (A). Scale bar: 100 µm. (F) WB analysis of EGFR, EGFRvIII, and Src levels and activity (p-EGFR Y1068, p-EGFRvIII Y1068, and p-Src <t>Y416)</t> after 24 h treatment. β-actin was used as a loading control. (G) Correlation graph depicting the relationship between GSC EGFR status and Src inhibition after treatment with TAT-Cx43 266–283 in murine and patient-derived GSCs. (H) Contingency table graph showing the magnitude of TAT-Cx43 266–283 response and EGFR status of all the murine NSCs and GSCs. χ 2 test was used for statistical analysis.
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    The effect of TAT-Cx43 266–283 depends on EGFR alterations. A set of murine SVZ NSCs with EGFR alterations (SVZ-EGFRwt and SVZ-EGFRvIII) and a set of murine SVZ NSCs with EGFRvIII mutation (NSC-EGFRvIII), with Nf1/PTEN deletion (NP) or with a combination of Nf1/PTEN deletion and EGFRvIII mutation (NPE, and their immune evasive version, NPE-IE) and their non-modified counterparts (SVZ-NSCs) were treated with 50 µM TAT, 50 µM TAT-Cx43 274–291 (2 cell-penetrating peptides used as additional controls), 50 µM TAT-Cx43 266–283 , 100 µM temozolomide, 1 µM erlotinib, 0.05% DMSO (v/v) (vehicle for erlotinib) and the combination of 1 µM erlotinib plus 50 µM TAT-Cx43 266–283 . (A) Alamar blue viability assay of SVZ NSCs with EGFR alterations and healthy NSCs after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: * P < .05, *** P < .001 vs control; ## P < .01, ### P < .001 vs TAT; @@ P < .01 vs TAT-Cx43 274-291 ; +++ P < .001 vs temozolomide). (B) Phase-contrast images of murine NSCs with and without EGFR alterations treated as described previously. Scale bar: 100 µm. (C) WB analysis of EGFR and EGFRvIII levels and activity (p-EGFR Y1068 and p-EGFRvIII Y1068) after 24 h treatment. GAPDH was used as a loading control. (D) Alamar blue viability assay of SVZ NSCs with EGFR and additional GBM-driver alterations after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: *** P value < .001). (E) Phase-contrast images of murine SVZ NSCs with GBM-driver alterations treated as described in (A). Scale bar: 100 µm. (F) WB analysis of EGFR, EGFRvIII, and Src levels and activity (p-EGFR Y1068, p-EGFRvIII Y1068, and p-Src <t>Y416)</t> after 24 h treatment. β-actin was used as a loading control. (G) Correlation graph depicting the relationship between GSC EGFR status and Src inhibition after treatment with TAT-Cx43 266–283 in murine and patient-derived GSCs. (H) Contingency table graph showing the magnitude of TAT-Cx43 266–283 response and EGFR status of all the murine NSCs and GSCs. χ 2 test was used for statistical analysis.
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    Cell Signaling Technology Inc phospho src y416 tyr416
    The effect of TAT-Cx43 266–283 depends on EGFR alterations. A set of murine SVZ NSCs with EGFR alterations (SVZ-EGFRwt and SVZ-EGFRvIII) and a set of murine SVZ NSCs with EGFRvIII mutation (NSC-EGFRvIII), with Nf1/PTEN deletion (NP) or with a combination of Nf1/PTEN deletion and EGFRvIII mutation (NPE, and their immune evasive version, NPE-IE) and their non-modified counterparts (SVZ-NSCs) were treated with 50 µM TAT, 50 µM TAT-Cx43 274–291 (2 cell-penetrating peptides used as additional controls), 50 µM TAT-Cx43 266–283 , 100 µM temozolomide, 1 µM erlotinib, 0.05% DMSO (v/v) (vehicle for erlotinib) and the combination of 1 µM erlotinib plus 50 µM TAT-Cx43 266–283 . (A) Alamar blue viability assay of SVZ NSCs with EGFR alterations and healthy NSCs after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: * P < .05, *** P < .001 vs control; ## P < .01, ### P < .001 vs TAT; @@ P < .01 vs TAT-Cx43 274-291 ; +++ P < .001 vs temozolomide). (B) Phase-contrast images of murine NSCs with and without EGFR alterations treated as described previously. Scale bar: 100 µm. (C) WB analysis of EGFR and EGFRvIII levels and activity (p-EGFR Y1068 and p-EGFRvIII Y1068) after 24 h treatment. GAPDH was used as a loading control. (D) Alamar blue viability assay of SVZ NSCs with EGFR and additional GBM-driver alterations after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: *** P value < .001). (E) Phase-contrast images of murine SVZ NSCs with GBM-driver alterations treated as described in (A). Scale bar: 100 µm. (F) WB analysis of EGFR, EGFRvIII, and Src levels and activity (p-EGFR Y1068, p-EGFRvIII Y1068, and p-Src <t>Y416)</t> after 24 h treatment. β-actin was used as a loading control. (G) Correlation graph depicting the relationship between GSC EGFR status and Src inhibition after treatment with TAT-Cx43 266–283 in murine and patient-derived GSCs. (H) Contingency table graph showing the magnitude of TAT-Cx43 266–283 response and EGFR status of all the murine NSCs and GSCs. χ 2 test was used for statistical analysis.
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    The effect of TAT-Cx43 266–283 depends on EGFR alterations. A set of murine SVZ NSCs with EGFR alterations (SVZ-EGFRwt and SVZ-EGFRvIII) and a set of murine SVZ NSCs with EGFRvIII mutation (NSC-EGFRvIII), with Nf1/PTEN deletion (NP) or with a combination of Nf1/PTEN deletion and EGFRvIII mutation (NPE, and their immune evasive version, NPE-IE) and their non-modified counterparts (SVZ-NSCs) were treated with 50 µM TAT, 50 µM TAT-Cx43 274–291 (2 cell-penetrating peptides used as additional controls), 50 µM TAT-Cx43 266–283 , 100 µM temozolomide, 1 µM erlotinib, 0.05% DMSO (v/v) (vehicle for erlotinib) and the combination of 1 µM erlotinib plus 50 µM TAT-Cx43 266–283 . (A) Alamar blue viability assay of SVZ NSCs with EGFR alterations and healthy NSCs after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: * P < .05, *** P < .001 vs control; ## P < .01, ### P < .001 vs TAT; @@ P < .01 vs TAT-Cx43 274-291 ; +++ P < .001 vs temozolomide). (B) Phase-contrast images of murine NSCs with and without EGFR alterations treated as described previously. Scale bar: 100 µm. (C) WB analysis of EGFR and EGFRvIII levels and activity (p-EGFR Y1068 and p-EGFRvIII Y1068) after 24 h treatment. GAPDH was used as a loading control. (D) Alamar blue viability assay of SVZ NSCs with EGFR and additional GBM-driver alterations after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: *** P value < .001). (E) Phase-contrast images of murine SVZ NSCs with GBM-driver alterations treated as described in (A). Scale bar: 100 µm. (F) WB analysis of EGFR, EGFRvIII, and Src levels and activity (p-EGFR Y1068, p-EGFRvIII Y1068, and p-Src <t>Y416)</t> after 24 h treatment. β-actin was used as a loading control. (G) Correlation graph depicting the relationship between GSC EGFR status and Src inhibition after treatment with TAT-Cx43 266–283 in murine and patient-derived GSCs. (H) Contingency table graph showing the magnitude of TAT-Cx43 266–283 response and EGFR status of all the murine NSCs and GSCs. χ 2 test was used for statistical analysis.
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    ABclonal Biotechnology anti phospho src y419 antibody
    Low concentrations of SAR promote Definitive Endoderm (DE) differentiation. DE differentiation was performed using the previously reported protocol ( A ) for 3 days. After 3 days of differentiation, total RNAs were extracted and the expressions of FOXA2 and SOX17 in DE cells derived from the H1 cells were determined by qPCR ( B ). ( C ) QPCR results of FOXA2 and SOX17 in two different ESC lines (H1 and H9) and two iPSC lines (K0 and β) treated with 0.5 µM SAR. ( D ) Flow cytometric analysis of DE cells derived from hESC line H1 expressing FOXA2 and SOX17 with or without the treatment of 0.5 µM SAR. ( E ) Quantitative statistics of FOXA2 + /SOX17 + cells corresponding to ( D ). ( F ) Immunofluorescent staining examined FOXA2 + (green) and SOX17 + (red) cells treated with 0.5 µM SAR differentiated from hESC line H1. The nucleus was counterstained with Hoechst 33,342. Quantitative statistics were shown in ( G ). ( H ) The p-Src <t>Y419</t> and Src protein levels in DE cells treated with different concentrations of SAR were detected using western blotting. GAPDH was used as a loading control. ( I ) Quantitative statistics of p-Src Y419/Src corresponding to H. Data are presented as mean ± SEM ( n = 3–8). * p < 0.05; ** p < 0.01; *** p < 0.001; ns, not significant
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    Image Search Results


    The effect of TAT-Cx43 266–283 depends on EGFR alterations. A set of murine SVZ NSCs with EGFR alterations (SVZ-EGFRwt and SVZ-EGFRvIII) and a set of murine SVZ NSCs with EGFRvIII mutation (NSC-EGFRvIII), with Nf1/PTEN deletion (NP) or with a combination of Nf1/PTEN deletion and EGFRvIII mutation (NPE, and their immune evasive version, NPE-IE) and their non-modified counterparts (SVZ-NSCs) were treated with 50 µM TAT, 50 µM TAT-Cx43 274–291 (2 cell-penetrating peptides used as additional controls), 50 µM TAT-Cx43 266–283 , 100 µM temozolomide, 1 µM erlotinib, 0.05% DMSO (v/v) (vehicle for erlotinib) and the combination of 1 µM erlotinib plus 50 µM TAT-Cx43 266–283 . (A) Alamar blue viability assay of SVZ NSCs with EGFR alterations and healthy NSCs after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: * P < .05, *** P < .001 vs control; ## P < .01, ### P < .001 vs TAT; @@ P < .01 vs TAT-Cx43 274-291 ; +++ P < .001 vs temozolomide). (B) Phase-contrast images of murine NSCs with and without EGFR alterations treated as described previously. Scale bar: 100 µm. (C) WB analysis of EGFR and EGFRvIII levels and activity (p-EGFR Y1068 and p-EGFRvIII Y1068) after 24 h treatment. GAPDH was used as a loading control. (D) Alamar blue viability assay of SVZ NSCs with EGFR and additional GBM-driver alterations after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: *** P value < .001). (E) Phase-contrast images of murine SVZ NSCs with GBM-driver alterations treated as described in (A). Scale bar: 100 µm. (F) WB analysis of EGFR, EGFRvIII, and Src levels and activity (p-EGFR Y1068, p-EGFRvIII Y1068, and p-Src Y416) after 24 h treatment. β-actin was used as a loading control. (G) Correlation graph depicting the relationship between GSC EGFR status and Src inhibition after treatment with TAT-Cx43 266–283 in murine and patient-derived GSCs. (H) Contingency table graph showing the magnitude of TAT-Cx43 266–283 response and EGFR status of all the murine NSCs and GSCs. χ 2 test was used for statistical analysis.

    Journal: Neuro-Oncology

    Article Title: EGFR amplification and EGFRvIII predict and participate in TAT-Cx43 266–283 antitumor response in preclinical glioblastoma models

    doi: 10.1093/neuonc/noae060

    Figure Lengend Snippet: The effect of TAT-Cx43 266–283 depends on EGFR alterations. A set of murine SVZ NSCs with EGFR alterations (SVZ-EGFRwt and SVZ-EGFRvIII) and a set of murine SVZ NSCs with EGFRvIII mutation (NSC-EGFRvIII), with Nf1/PTEN deletion (NP) or with a combination of Nf1/PTEN deletion and EGFRvIII mutation (NPE, and their immune evasive version, NPE-IE) and their non-modified counterparts (SVZ-NSCs) were treated with 50 µM TAT, 50 µM TAT-Cx43 274–291 (2 cell-penetrating peptides used as additional controls), 50 µM TAT-Cx43 266–283 , 100 µM temozolomide, 1 µM erlotinib, 0.05% DMSO (v/v) (vehicle for erlotinib) and the combination of 1 µM erlotinib plus 50 µM TAT-Cx43 266–283 . (A) Alamar blue viability assay of SVZ NSCs with EGFR alterations and healthy NSCs after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: * P < .05, *** P < .001 vs control; ## P < .01, ### P < .001 vs TAT; @@ P < .01 vs TAT-Cx43 274-291 ; +++ P < .001 vs temozolomide). (B) Phase-contrast images of murine NSCs with and without EGFR alterations treated as described previously. Scale bar: 100 µm. (C) WB analysis of EGFR and EGFRvIII levels and activity (p-EGFR Y1068 and p-EGFRvIII Y1068) after 24 h treatment. GAPDH was used as a loading control. (D) Alamar blue viability assay of SVZ NSCs with EGFR and additional GBM-driver alterations after 6 days of treatment administered at days 0 and 3. Results are expressed as the percentage of the control (mean ± SEM of at least 3 independent experiments, ANOVA: *** P value < .001). (E) Phase-contrast images of murine SVZ NSCs with GBM-driver alterations treated as described in (A). Scale bar: 100 µm. (F) WB analysis of EGFR, EGFRvIII, and Src levels and activity (p-EGFR Y1068, p-EGFRvIII Y1068, and p-Src Y416) after 24 h treatment. β-actin was used as a loading control. (G) Correlation graph depicting the relationship between GSC EGFR status and Src inhibition after treatment with TAT-Cx43 266–283 in murine and patient-derived GSCs. (H) Contingency table graph showing the magnitude of TAT-Cx43 266–283 response and EGFR status of all the murine NSCs and GSCs. χ 2 test was used for statistical analysis.

    Article Snippet: Primary antibodies used for WB were: anti-phospho-EGFR Y1068 (1:1000, Cell Signaling, ref: 3777) and anti-EGFR (1:1000, Cell Signaling, ref: 4267), anti-VEGF (1:200, Santa Cruz Biotechnology, ref: sc-7269), anti-phospho-Src Y416 (1:250, Cell Signaling, ref: 2101), anti-Src (1:500, Cell Signaling, ref: 2110), anti-GAPDH (1:5000, Invitrogen, ref: AM4300), and anti-β-actin (1:1000, Sigma, ref: A5441).

    Techniques: Mutagenesis, Modification, Viability Assay, Control, Activity Assay, Inhibition, Derivative Assay

    EGFR alterations correlate with Src activity in GBM patients. Analyses were carried out using IDHwt GBM samples from the TCGA GBM database. (A) Volcano plot depicting levels of proteins in GBM patients with or without EGFR alterations. (B) Proteins with significantly higher levels in patients with EGFR alterations (see for a complete list). (C) Comparative graph of p-Src Y416 levels in patients with and without EGFR alterations (Student’s t -test, *** P value < .001). (D) Correlation graph showing the relationship between EGFR mRNA expression and p-Src Y416 protein levels in GBM patients. (E) Overall survival curve of patients with and without EGFR alterations (log-rank test, * P value < .05).

    Journal: Neuro-Oncology

    Article Title: EGFR amplification and EGFRvIII predict and participate in TAT-Cx43 266–283 antitumor response in preclinical glioblastoma models

    doi: 10.1093/neuonc/noae060

    Figure Lengend Snippet: EGFR alterations correlate with Src activity in GBM patients. Analyses were carried out using IDHwt GBM samples from the TCGA GBM database. (A) Volcano plot depicting levels of proteins in GBM patients with or without EGFR alterations. (B) Proteins with significantly higher levels in patients with EGFR alterations (see for a complete list). (C) Comparative graph of p-Src Y416 levels in patients with and without EGFR alterations (Student’s t -test, *** P value < .001). (D) Correlation graph showing the relationship between EGFR mRNA expression and p-Src Y416 protein levels in GBM patients. (E) Overall survival curve of patients with and without EGFR alterations (log-rank test, * P value < .05).

    Article Snippet: Primary antibodies used for WB were: anti-phospho-EGFR Y1068 (1:1000, Cell Signaling, ref: 3777) and anti-EGFR (1:1000, Cell Signaling, ref: 4267), anti-VEGF (1:200, Santa Cruz Biotechnology, ref: sc-7269), anti-phospho-Src Y416 (1:250, Cell Signaling, ref: 2101), anti-Src (1:500, Cell Signaling, ref: 2110), anti-GAPDH (1:5000, Invitrogen, ref: AM4300), and anti-β-actin (1:1000, Sigma, ref: A5441).

    Techniques: Activity Assay, Expressing

    Low concentrations of SAR promote Definitive Endoderm (DE) differentiation. DE differentiation was performed using the previously reported protocol ( A ) for 3 days. After 3 days of differentiation, total RNAs were extracted and the expressions of FOXA2 and SOX17 in DE cells derived from the H1 cells were determined by qPCR ( B ). ( C ) QPCR results of FOXA2 and SOX17 in two different ESC lines (H1 and H9) and two iPSC lines (K0 and β) treated with 0.5 µM SAR. ( D ) Flow cytometric analysis of DE cells derived from hESC line H1 expressing FOXA2 and SOX17 with or without the treatment of 0.5 µM SAR. ( E ) Quantitative statistics of FOXA2 + /SOX17 + cells corresponding to ( D ). ( F ) Immunofluorescent staining examined FOXA2 + (green) and SOX17 + (red) cells treated with 0.5 µM SAR differentiated from hESC line H1. The nucleus was counterstained with Hoechst 33,342. Quantitative statistics were shown in ( G ). ( H ) The p-Src Y419 and Src protein levels in DE cells treated with different concentrations of SAR were detected using western blotting. GAPDH was used as a loading control. ( I ) Quantitative statistics of p-Src Y419/Src corresponding to H. Data are presented as mean ± SEM ( n = 3–8). * p < 0.05; ** p < 0.01; *** p < 0.001; ns, not significant

    Journal: Cell Communication and Signaling : CCS

    Article Title: Low concentrations of saracatinib promote definitive endoderm differentiation through inhibition of FAK-YAP signaling axis

    doi: 10.1186/s12964-024-01679-7

    Figure Lengend Snippet: Low concentrations of SAR promote Definitive Endoderm (DE) differentiation. DE differentiation was performed using the previously reported protocol ( A ) for 3 days. After 3 days of differentiation, total RNAs were extracted and the expressions of FOXA2 and SOX17 in DE cells derived from the H1 cells were determined by qPCR ( B ). ( C ) QPCR results of FOXA2 and SOX17 in two different ESC lines (H1 and H9) and two iPSC lines (K0 and β) treated with 0.5 µM SAR. ( D ) Flow cytometric analysis of DE cells derived from hESC line H1 expressing FOXA2 and SOX17 with or without the treatment of 0.5 µM SAR. ( E ) Quantitative statistics of FOXA2 + /SOX17 + cells corresponding to ( D ). ( F ) Immunofluorescent staining examined FOXA2 + (green) and SOX17 + (red) cells treated with 0.5 µM SAR differentiated from hESC line H1. The nucleus was counterstained with Hoechst 33,342. Quantitative statistics were shown in ( G ). ( H ) The p-Src Y419 and Src protein levels in DE cells treated with different concentrations of SAR were detected using western blotting. GAPDH was used as a loading control. ( I ) Quantitative statistics of p-Src Y419/Src corresponding to H. Data are presented as mean ± SEM ( n = 3–8). * p < 0.05; ** p < 0.01; *** p < 0.001; ns, not significant

    Article Snippet: The membranes were incubated overnight at 4 °C with primary antibodies, including anti-phospho-Src-Y419 antibody (Abclonal, cat# AP1027, 1:1,000, Wuhan, China), anti-Src antibody (Abclonal, cat# A19119, 1:1,000), anti-phospho-FAK-Y397 antibody (Abclonal, cat# AP1447, 1:1,000), anti-FAK antibody (Abclonal, cat# A11131, 1:1,000), anti-FOXA2 antibody (Abclonal, cat# A19053, 1:1,000), anti-SOX17 antibody(Abclonal, cat# A18858, 1:1,000), anti-DYKDDDDK Tag antibody (CST, cat# 14,793, 1:4,000, Danvers, Massachusetts, USA), anti-phospho-FAK-Y925 antibody (Abclonal, cat# AP1098, 1:1,000), anti-phospho-FAK-Y576/577 antibody (Abclonal, cat# AP0536, 1:1,000), and anti-YAP1 antibody (Abclonal, cat# A19134, 1:1,000).

    Techniques: Derivative Assay, Expressing, Staining, Western Blot

    Journal: iScience

    Article Title: Acetyl-NPKY of integrin-β1 binds KINDLIN2 to control endothelial cell proliferation and junctional integrity

    doi: 10.1016/j.isci.2024.110129

    Figure Lengend Snippet:

    Article Snippet: Polyclonal rabbit anti-Phospho-Src (Tyr527) Antibody , Cell Signaling Technology , Cat# 2105, RRID: AB_331034.

    Techniques: Virus, Recombinant, Synthesized, Real-time Polymerase Chain Reaction, Plasmid Preparation, Software