p-her3-y1289 antibody  (Cell Signaling Technology Inc)

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

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

Journal: Oncology Reports

Article Title: Evaluation of co‑inhibition of ErbB family kinases and PI3K for HPV‑negative head and neck squamous cell carcinoma

doi: 10.3892/or.2025.8871

Figure Lengend Snippet: A combination of copanlisib and afatinib effectively blocked the phosphorylation of HER2, HER3 and Akt, and enhanced caspase-3 cleavage. (A) Cal27 and (B) FaDu cells were treated with increasing concentrations of copanlisib, 0.5 µM afatinib or their combination for 24 h before lysis. The indicated proteins were detected by western blot analysis. C-, cleaved; P-, phosphorylated.

Article Snippet: The following antibodies were purchased from Cell Signaling Technology, Inc.: Phosphorylated (P)-Akt-S473 (cat. no. 4058), P-Akt-T308 (cat. no. 9275), Akt (cat. no. 2938), P-HER2-Y1248 (cat. no. 2247), HER2 (cat. no. 4290), P-HER3-Y1289 (cat. no. 2842), HER3 (cat. no. 12708), caspase-3 (cat. no. 9665), cleaved-caspase-3 (cat. no. 9664) and β-actin (cat. no. 4967).

Techniques: Phospho-proteomics, Lysis, Western Blot

Journal: EMBO Molecular Medicine

Article Title: PlexinD1 is a driver and a therapeutic target in advanced prostate cancer

doi: 10.1038/s44321-024-00186-z

Figure Lengend Snippet: Reagents and tools table

Article Snippet: p-ErbB3 (Tyr1289) (WB: 1/1000; IHC: 1/1000) , Cell Signaling Technology , 2842.

Techniques: Recombinant, Sequencing, Control, Transfection, Membrane, Reverse Transcription, Software, Microarray, Subcloning, shRNA, Cell Viability Assay, Viability Assay, Reporter Assay, In Situ, Enzyme-linked Immunosorbent Assay, Phospho-proteomics, Extraction, Bicinchoninic Acid Protein Assay, Magnetic Beads, Gel Extraction, Purification, Ligation, Mutagenesis, Chromatin Immunoprecipitation

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

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