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p her3 bs 3491r antibodies  (Bioss)


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    Bioss p her3 bs 3491r antibodies
    Targeting the ESM1-epidermal growth factor receptor (EGFR) interaction by therapeutic peptides suppresses EGFR/human EGFR3 <t>(HER3)-driven</t> epithelial-mesenchymal transition (EMT) and cell mobility in gastric cancer (GC) cells. ( A ) Wild-type ESM1 (WT-ESM1) was introduced into AGS, Kato-III, and NCI-N87 cells, and then cells were subjected to a Western blot assay to evaluate the phosphorylation status of HER3. ( B, C ) Co-immunoprecipitation assays were conducted to assess the interaction between EGFR, ESM1, and HER3 in AGS/WT-ESM cells ( B ). Comparing the association of EGFR and HER3 in the AGS cells transfected with either WT-ESM1 or a control vector (Ctrl) ( C ). Subsequently, a Western blot analysis was performed to examine the formation of this complex. ( D ) Schematic diagram of two synthetic peptides including peptide 1 (1-27 aas) and peptide 2 (26-46 aas) of the ESM1 protein. ( E, F ) AGS cells were infected with a lentivirus carrying a control vector or WT-ESM1 following treatment of cells with synthetic peptides (1 µM) as indicated. The phosphorylation status of HER3, EGFR and Akt, and expressions of angiopoietin-2, Snail, and Slug were all detected by Western blotting ( E ). The migratory ability of cells was determined by a transwell migration assay ( F ). Differences are presented as the mean ± SD. *** p < 0.001, compared to the WT-ESM1-overexpressing only group.
    P Her3 Bs 3491r Antibodies, supplied by Bioss, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p her3 bs 3491r antibodies/product/Bioss
    Average 94 stars, based on 1 article reviews
    p her3 bs 3491r antibodies - by Bioz Stars, 2026-02
    94/100 stars

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    1) Product Images from "ESM1 facilitates the EGFR/HER3-triggered epithelial-to-mesenchymal transition and progression of gastric cancer via modulating interplay between Akt and angiopoietin-2 signaling"

    Article Title: ESM1 facilitates the EGFR/HER3-triggered epithelial-to-mesenchymal transition and progression of gastric cancer via modulating interplay between Akt and angiopoietin-2 signaling

    Journal: International Journal of Biological Sciences

    doi: 10.7150/ijbs.100276

    Targeting the ESM1-epidermal growth factor receptor (EGFR) interaction by therapeutic peptides suppresses EGFR/human EGFR3 (HER3)-driven epithelial-mesenchymal transition (EMT) and cell mobility in gastric cancer (GC) cells. ( A ) Wild-type ESM1 (WT-ESM1) was introduced into AGS, Kato-III, and NCI-N87 cells, and then cells were subjected to a Western blot assay to evaluate the phosphorylation status of HER3. ( B, C ) Co-immunoprecipitation assays were conducted to assess the interaction between EGFR, ESM1, and HER3 in AGS/WT-ESM cells ( B ). Comparing the association of EGFR and HER3 in the AGS cells transfected with either WT-ESM1 or a control vector (Ctrl) ( C ). Subsequently, a Western blot analysis was performed to examine the formation of this complex. ( D ) Schematic diagram of two synthetic peptides including peptide 1 (1-27 aas) and peptide 2 (26-46 aas) of the ESM1 protein. ( E, F ) AGS cells were infected with a lentivirus carrying a control vector or WT-ESM1 following treatment of cells with synthetic peptides (1 µM) as indicated. The phosphorylation status of HER3, EGFR and Akt, and expressions of angiopoietin-2, Snail, and Slug were all detected by Western blotting ( E ). The migratory ability of cells was determined by a transwell migration assay ( F ). Differences are presented as the mean ± SD. *** p < 0.001, compared to the WT-ESM1-overexpressing only group.
    Figure Legend Snippet: Targeting the ESM1-epidermal growth factor receptor (EGFR) interaction by therapeutic peptides suppresses EGFR/human EGFR3 (HER3)-driven epithelial-mesenchymal transition (EMT) and cell mobility in gastric cancer (GC) cells. ( A ) Wild-type ESM1 (WT-ESM1) was introduced into AGS, Kato-III, and NCI-N87 cells, and then cells were subjected to a Western blot assay to evaluate the phosphorylation status of HER3. ( B, C ) Co-immunoprecipitation assays were conducted to assess the interaction between EGFR, ESM1, and HER3 in AGS/WT-ESM cells ( B ). Comparing the association of EGFR and HER3 in the AGS cells transfected with either WT-ESM1 or a control vector (Ctrl) ( C ). Subsequently, a Western blot analysis was performed to examine the formation of this complex. ( D ) Schematic diagram of two synthetic peptides including peptide 1 (1-27 aas) and peptide 2 (26-46 aas) of the ESM1 protein. ( E, F ) AGS cells were infected with a lentivirus carrying a control vector or WT-ESM1 following treatment of cells with synthetic peptides (1 µM) as indicated. The phosphorylation status of HER3, EGFR and Akt, and expressions of angiopoietin-2, Snail, and Slug were all detected by Western blotting ( E ). The migratory ability of cells was determined by a transwell migration assay ( F ). Differences are presented as the mean ± SD. *** p < 0.001, compared to the WT-ESM1-overexpressing only group.

    Techniques Used: Western Blot, Immunoprecipitation, Transfection, Control, Plasmid Preparation, Infection, Transwell Migration Assay

    A working model shows the molecular mechanism underlying the ability of ESM1 to promote progression of gastric cancer (GC) cells. The oncogenic role of ESM1 was attributed to triggering the epithelial-to-mesenchymal transition (EMT) by activating epidermal growth factor receptor (EGFR)/human EGFR3 (HER3) and their downstream signal, Akt. Angiopoietin-2 was highly correlated with ESM1 and interplayed with Akt to promote EMT progression. Blocking the interaction of ESM1 and the EGFR by synthetic ESM1 peptides attenuated the EGFR/HER3 activation-driven EMT, cell motility, and proliferation. This schematic representation was created using BioRender software.
    Figure Legend Snippet: A working model shows the molecular mechanism underlying the ability of ESM1 to promote progression of gastric cancer (GC) cells. The oncogenic role of ESM1 was attributed to triggering the epithelial-to-mesenchymal transition (EMT) by activating epidermal growth factor receptor (EGFR)/human EGFR3 (HER3) and their downstream signal, Akt. Angiopoietin-2 was highly correlated with ESM1 and interplayed with Akt to promote EMT progression. Blocking the interaction of ESM1 and the EGFR by synthetic ESM1 peptides attenuated the EGFR/HER3 activation-driven EMT, cell motility, and proliferation. This schematic representation was created using BioRender software.

    Techniques Used: Blocking Assay, Activation Assay, Software



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    p her3 bs 3491r antibodies  (Bioss)
    94
    Bioss p her3 bs 3491r antibodies
    Targeting the ESM1-epidermal growth factor receptor (EGFR) interaction by therapeutic peptides suppresses EGFR/human EGFR3 <t>(HER3)-driven</t> epithelial-mesenchymal transition (EMT) and cell mobility in gastric cancer (GC) cells. ( A ) Wild-type ESM1 (WT-ESM1) was introduced into AGS, Kato-III, and NCI-N87 cells, and then cells were subjected to a Western blot assay to evaluate the phosphorylation status of HER3. ( B, C ) Co-immunoprecipitation assays were conducted to assess the interaction between EGFR, ESM1, and HER3 in AGS/WT-ESM cells ( B ). Comparing the association of EGFR and HER3 in the AGS cells transfected with either WT-ESM1 or a control vector (Ctrl) ( C ). Subsequently, a Western blot analysis was performed to examine the formation of this complex. ( D ) Schematic diagram of two synthetic peptides including peptide 1 (1-27 aas) and peptide 2 (26-46 aas) of the ESM1 protein. ( E, F ) AGS cells were infected with a lentivirus carrying a control vector or WT-ESM1 following treatment of cells with synthetic peptides (1 µM) as indicated. The phosphorylation status of HER3, EGFR and Akt, and expressions of angiopoietin-2, Snail, and Slug were all detected by Western blotting ( E ). The migratory ability of cells was determined by a transwell migration assay ( F ). Differences are presented as the mean ± SD. *** p < 0.001, compared to the WT-ESM1-overexpressing only group.
    P Her3 Bs 3491r Antibodies, supplied by Bioss, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p her3 bs 3491r antibodies/product/Bioss
    Average 94 stars, based on 1 article reviews
    p her3 bs 3491r antibodies - by Bioz Stars, 2026-02
    94/100 stars
    		  Buy from Supplier
    p her3 bs 3491r antibodies  (Proteintech)
    93
    Proteintech p her3 bs 3491r antibodies
    Targeting the ESM1-epidermal growth factor receptor (EGFR) interaction by therapeutic peptides suppresses EGFR/human EGFR3 <t>(HER3)-driven</t> epithelial-mesenchymal transition (EMT) and cell mobility in gastric cancer (GC) cells. ( A ) Wild-type ESM1 (WT-ESM1) was introduced into AGS, Kato-III, and NCI-N87 cells, and then cells were subjected to a Western blot assay to evaluate the phosphorylation status of HER3. ( B, C ) Co-immunoprecipitation assays were conducted to assess the interaction between EGFR, ESM1, and HER3 in AGS/WT-ESM cells ( B ). Comparing the association of EGFR and HER3 in the AGS cells transfected with either WT-ESM1 or a control vector (Ctrl) ( C ). Subsequently, a Western blot analysis was performed to examine the formation of this complex. ( D ) Schematic diagram of two synthetic peptides including peptide 1 (1-27 aas) and peptide 2 (26-46 aas) of the ESM1 protein. ( E, F ) AGS cells were infected with a lentivirus carrying a control vector or WT-ESM1 following treatment of cells with synthetic peptides (1 µM) as indicated. The phosphorylation status of HER3, EGFR and Akt, and expressions of angiopoietin-2, Snail, and Slug were all detected by Western blotting ( E ). The migratory ability of cells was determined by a transwell migration assay ( F ). Differences are presented as the mean ± SD. *** p < 0.001, compared to the WT-ESM1-overexpressing only group.
    P Her3 Bs 3491r Antibodies, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p her3 bs 3491r antibodies/product/Proteintech
    Average 93 stars, based on 1 article reviews
    p her3 bs 3491r antibodies - by Bioz Stars, 2026-02
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    Targeting the ESM1-epidermal growth factor receptor (EGFR) interaction by therapeutic peptides suppresses EGFR/human EGFR3 (HER3)-driven epithelial-mesenchymal transition (EMT) and cell mobility in gastric cancer (GC) cells. ( A ) Wild-type ESM1 (WT-ESM1) was introduced into AGS, Kato-III, and NCI-N87 cells, and then cells were subjected to a Western blot assay to evaluate the phosphorylation status of HER3. ( B, C ) Co-immunoprecipitation assays were conducted to assess the interaction between EGFR, ESM1, and HER3 in AGS/WT-ESM cells ( B ). Comparing the association of EGFR and HER3 in the AGS cells transfected with either WT-ESM1 or a control vector (Ctrl) ( C ). Subsequently, a Western blot analysis was performed to examine the formation of this complex. ( D ) Schematic diagram of two synthetic peptides including peptide 1 (1-27 aas) and peptide 2 (26-46 aas) of the ESM1 protein. ( E, F ) AGS cells were infected with a lentivirus carrying a control vector or WT-ESM1 following treatment of cells with synthetic peptides (1 µM) as indicated. The phosphorylation status of HER3, EGFR and Akt, and expressions of angiopoietin-2, Snail, and Slug were all detected by Western blotting ( E ). The migratory ability of cells was determined by a transwell migration assay ( F ). Differences are presented as the mean ± SD. *** p < 0.001, compared to the WT-ESM1-overexpressing only group.

    Journal: International Journal of Biological Sciences

    Article Title: ESM1 facilitates the EGFR/HER3-triggered epithelial-to-mesenchymal transition and progression of gastric cancer via modulating interplay between Akt and angiopoietin-2 signaling

    doi: 10.7150/ijbs.100276

    Figure Lengend Snippet: Targeting the ESM1-epidermal growth factor receptor (EGFR) interaction by therapeutic peptides suppresses EGFR/human EGFR3 (HER3)-driven epithelial-mesenchymal transition (EMT) and cell mobility in gastric cancer (GC) cells. ( A ) Wild-type ESM1 (WT-ESM1) was introduced into AGS, Kato-III, and NCI-N87 cells, and then cells were subjected to a Western blot assay to evaluate the phosphorylation status of HER3. ( B, C ) Co-immunoprecipitation assays were conducted to assess the interaction between EGFR, ESM1, and HER3 in AGS/WT-ESM cells ( B ). Comparing the association of EGFR and HER3 in the AGS cells transfected with either WT-ESM1 or a control vector (Ctrl) ( C ). Subsequently, a Western blot analysis was performed to examine the formation of this complex. ( D ) Schematic diagram of two synthetic peptides including peptide 1 (1-27 aas) and peptide 2 (26-46 aas) of the ESM1 protein. ( E, F ) AGS cells were infected with a lentivirus carrying a control vector or WT-ESM1 following treatment of cells with synthetic peptides (1 µM) as indicated. The phosphorylation status of HER3, EGFR and Akt, and expressions of angiopoietin-2, Snail, and Slug were all detected by Western blotting ( E ). The migratory ability of cells was determined by a transwell migration assay ( F ). Differences are presented as the mean ± SD. *** p < 0.001, compared to the WT-ESM1-overexpressing only group.

    Article Snippet: The following primary antibodies were used: endocan (LIA-1001; Lunginnov, Lille, France); phosphorylated (p)-EGFR (#3777), p-Akt (#9271), p-ERK (#4370), p-STAT3 (#9145), EGFR (#2239), Akt (#9272), STAT3 (#9139), ERK (#4695), E-cadherin (#3195), vimentin (#5741), Snail (#3879), Slug (#9585), p-HER3 (#2842), and HER3 (#12708) antibodies all obtained from Cell Signaling Technology (Danvers, MA, USA); angiopoietin-2 (bs-0677R-TR) and p-HER3 (bs-3491R) antibodies purchased from Bioss (Woburn, MA, USA); α-tubulin (#66031-1-Ig) antibodies respectively obtained from Proteintech (Rosemont, IL, USA).

    Techniques: Western Blot, Immunoprecipitation, Transfection, Control, Plasmid Preparation, Infection, Transwell Migration Assay

    A working model shows the molecular mechanism underlying the ability of ESM1 to promote progression of gastric cancer (GC) cells. The oncogenic role of ESM1 was attributed to triggering the epithelial-to-mesenchymal transition (EMT) by activating epidermal growth factor receptor (EGFR)/human EGFR3 (HER3) and their downstream signal, Akt. Angiopoietin-2 was highly correlated with ESM1 and interplayed with Akt to promote EMT progression. Blocking the interaction of ESM1 and the EGFR by synthetic ESM1 peptides attenuated the EGFR/HER3 activation-driven EMT, cell motility, and proliferation. This schematic representation was created using BioRender software.

    Journal: International Journal of Biological Sciences

    Article Title: ESM1 facilitates the EGFR/HER3-triggered epithelial-to-mesenchymal transition and progression of gastric cancer via modulating interplay between Akt and angiopoietin-2 signaling

    doi: 10.7150/ijbs.100276

    Figure Lengend Snippet: A working model shows the molecular mechanism underlying the ability of ESM1 to promote progression of gastric cancer (GC) cells. The oncogenic role of ESM1 was attributed to triggering the epithelial-to-mesenchymal transition (EMT) by activating epidermal growth factor receptor (EGFR)/human EGFR3 (HER3) and their downstream signal, Akt. Angiopoietin-2 was highly correlated with ESM1 and interplayed with Akt to promote EMT progression. Blocking the interaction of ESM1 and the EGFR by synthetic ESM1 peptides attenuated the EGFR/HER3 activation-driven EMT, cell motility, and proliferation. This schematic representation was created using BioRender software.

    Article Snippet: The following primary antibodies were used: endocan (LIA-1001; Lunginnov, Lille, France); phosphorylated (p)-EGFR (#3777), p-Akt (#9271), p-ERK (#4370), p-STAT3 (#9145), EGFR (#2239), Akt (#9272), STAT3 (#9139), ERK (#4695), E-cadherin (#3195), vimentin (#5741), Snail (#3879), Slug (#9585), p-HER3 (#2842), and HER3 (#12708) antibodies all obtained from Cell Signaling Technology (Danvers, MA, USA); angiopoietin-2 (bs-0677R-TR) and p-HER3 (bs-3491R) antibodies purchased from Bioss (Woburn, MA, USA); α-tubulin (#66031-1-Ig) antibodies respectively obtained from Proteintech (Rosemont, IL, USA).

    Techniques: Blocking Assay, Activation Assay, Software

    Targeting the ESM1-epidermal growth factor receptor (EGFR) interaction by therapeutic peptides suppresses EGFR/human EGFR3 (HER3)-driven epithelial-mesenchymal transition (EMT) and cell mobility in gastric cancer (GC) cells. ( A ) Wild-type ESM1 (WT-ESM1) was introduced into AGS, Kato-III, and NCI-N87 cells, and then cells were subjected to a Western blot assay to evaluate the phosphorylation status of HER3. ( B, C ) Co-immunoprecipitation assays were conducted to assess the interaction between EGFR, ESM1, and HER3 in AGS/WT-ESM cells ( B ). Comparing the association of EGFR and HER3 in the AGS cells transfected with either WT-ESM1 or a control vector (Ctrl) ( C ). Subsequently, a Western blot analysis was performed to examine the formation of this complex. ( D ) Schematic diagram of two synthetic peptides including peptide 1 (1-27 aas) and peptide 2 (26-46 aas) of the ESM1 protein. ( E, F ) AGS cells were infected with a lentivirus carrying a control vector or WT-ESM1 following treatment of cells with synthetic peptides (1 µM) as indicated. The phosphorylation status of HER3, EGFR and Akt, and expressions of angiopoietin-2, Snail, and Slug were all detected by Western blotting ( E ). The migratory ability of cells was determined by a transwell migration assay ( F ). Differences are presented as the mean ± SD. *** p < 0.001, compared to the WT-ESM1-overexpressing only group.

    Journal: International Journal of Biological Sciences

    Article Title: ESM1 facilitates the EGFR/HER3-triggered epithelial-to-mesenchymal transition and progression of gastric cancer via modulating interplay between Akt and angiopoietin-2 signaling

    doi: 10.7150/ijbs.100276

    Figure Lengend Snippet: Targeting the ESM1-epidermal growth factor receptor (EGFR) interaction by therapeutic peptides suppresses EGFR/human EGFR3 (HER3)-driven epithelial-mesenchymal transition (EMT) and cell mobility in gastric cancer (GC) cells. ( A ) Wild-type ESM1 (WT-ESM1) was introduced into AGS, Kato-III, and NCI-N87 cells, and then cells were subjected to a Western blot assay to evaluate the phosphorylation status of HER3. ( B, C ) Co-immunoprecipitation assays were conducted to assess the interaction between EGFR, ESM1, and HER3 in AGS/WT-ESM cells ( B ). Comparing the association of EGFR and HER3 in the AGS cells transfected with either WT-ESM1 or a control vector (Ctrl) ( C ). Subsequently, a Western blot analysis was performed to examine the formation of this complex. ( D ) Schematic diagram of two synthetic peptides including peptide 1 (1-27 aas) and peptide 2 (26-46 aas) of the ESM1 protein. ( E, F ) AGS cells were infected with a lentivirus carrying a control vector or WT-ESM1 following treatment of cells with synthetic peptides (1 µM) as indicated. The phosphorylation status of HER3, EGFR and Akt, and expressions of angiopoietin-2, Snail, and Slug were all detected by Western blotting ( E ). The migratory ability of cells was determined by a transwell migration assay ( F ). Differences are presented as the mean ± SD. *** p < 0.001, compared to the WT-ESM1-overexpressing only group.

    Article Snippet: The following primary antibodies were used: endocan (LIA-1001; Lunginnov, Lille, France); phosphorylated (p)-EGFR (#3777), p-Akt (#9271), p-ERK (#4370), p-STAT3 (#9145), EGFR (#2239), Akt (#9272), STAT3 (#9139), ERK (#4695), E-cadherin (#3195), vimentin (#5741), Snail (#3879), Slug (#9585), p-HER3 (#2842), and HER3 (#12708) antibodies all obtained from Cell Signaling Technology (Danvers, MA, USA); angiopoietin-2 (bs-0677R-TR) and p-HER3 (bs-3491R) antibodies purchased from Bioss (Woburn, MA, USA); α-tubulin (#66031-1-Ig) antibodies respectively obtained from Proteintech (Rosemont, IL, USA).

    Techniques: Western Blot, Phospho-proteomics, Immunoprecipitation, Transfection, Control, Plasmid Preparation, Infection, Transwell Migration Assay

    A working model shows the molecular mechanism underlying the ability of ESM1 to promote progression of gastric cancer (GC) cells. The oncogenic role of ESM1 was attributed to triggering the epithelial-to-mesenchymal transition (EMT) by activating epidermal growth factor receptor (EGFR)/human EGFR3 (HER3) and their downstream signal, Akt. Angiopoietin-2 was highly correlated with ESM1 and interplayed with Akt to promote EMT progression. Blocking the interaction of ESM1 and the EGFR by synthetic ESM1 peptides attenuated the EGFR/HER3 activation-driven EMT, cell motility, and proliferation. This schematic representation was created using BioRender software.

    Journal: International Journal of Biological Sciences

    Article Title: ESM1 facilitates the EGFR/HER3-triggered epithelial-to-mesenchymal transition and progression of gastric cancer via modulating interplay between Akt and angiopoietin-2 signaling

    doi: 10.7150/ijbs.100276

    Figure Lengend Snippet: A working model shows the molecular mechanism underlying the ability of ESM1 to promote progression of gastric cancer (GC) cells. The oncogenic role of ESM1 was attributed to triggering the epithelial-to-mesenchymal transition (EMT) by activating epidermal growth factor receptor (EGFR)/human EGFR3 (HER3) and their downstream signal, Akt. Angiopoietin-2 was highly correlated with ESM1 and interplayed with Akt to promote EMT progression. Blocking the interaction of ESM1 and the EGFR by synthetic ESM1 peptides attenuated the EGFR/HER3 activation-driven EMT, cell motility, and proliferation. This schematic representation was created using BioRender software.

    Article Snippet: The following primary antibodies were used: endocan (LIA-1001; Lunginnov, Lille, France); phosphorylated (p)-EGFR (#3777), p-Akt (#9271), p-ERK (#4370), p-STAT3 (#9145), EGFR (#2239), Akt (#9272), STAT3 (#9139), ERK (#4695), E-cadherin (#3195), vimentin (#5741), Snail (#3879), Slug (#9585), p-HER3 (#2842), and HER3 (#12708) antibodies all obtained from Cell Signaling Technology (Danvers, MA, USA); angiopoietin-2 (bs-0677R-TR) and p-HER3 (bs-3491R) antibodies purchased from Bioss (Woburn, MA, USA); α-tubulin (#66031-1-Ig) antibodies respectively obtained from Proteintech (Rosemont, IL, USA).

    Techniques: Blocking Assay, Activation Assay, Software