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Cell Signaling Technology Inc antibodies against total epha2

<t>EphA2</t> phosphorylation at Ser-897 is suppressed by SHP2 inhibitors. ( A ) HeLa cells were pretreated with SHP099 (SHP, 10 µM), TNO155 (TNO, 1 µM), BI-D1870 (BI, 10 µM), or trametinib (Tram, 0.03 µM) for 1–2 h and were then stimulated with EGF (10 ng/mL), TNF-⍺ (20 ng/mL), or TPA (10 ng/mL) for 15–30 min. Whole-cell lysates were immunoblotted with EphA2, pS-EphA2, RSK1, pS-RSK1, p-ERK and β-actin antibodies. The relative quantification of pS-EphA2 shown in ( B ) is expressed as the mean ± SD of three independent experiments. P values were calculated by an ANOVA. * p < 0.05; ** p < 0.01; *** p < 0.001. ( C ) HeLa cells were pretreated with TNO155 (TNO, 1 µM) or BI-D1870 (BI, 10 µM) for 1 h and were then stimulated with TNF-⍺ (20 ng/mL) for 15 min. The expression of pS-EphA2 and EphA2 was analyzed by immunofluorescence. Representative images from three independent experiments are shown. ( D ) HeLa cells were transfected with siRNAs against GRB2 or the negative control and were then incubated for 48 h. Cells were stimulated with 20 ng/mL TNF-⍺ for 15 min. Whole-cell lysates were immunoblotted with GRB2, EphA2, pS-EphA2, and β-actin antibodies.

Antibodies Against Total Epha2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 203 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Allosteric SHP2 inhibitors suppress lung cancer cell migration by inhibiting non-canonical activation of EphA2 via the ERK-RSK signaling pathway"

Article Title: Allosteric SHP2 inhibitors suppress lung cancer cell migration by inhibiting non-canonical activation of EphA2 via the ERK-RSK signaling pathway

Journal: Scientific Reports

doi: 10.1038/s41598-025-20770-8

EphA2 phosphorylation at Ser-897 is suppressed by SHP2 inhibitors. ( A ) HeLa cells were pretreated with SHP099 (SHP, 10 µM), TNO155 (TNO, 1 µM), BI-D1870 (BI, 10 µM), or trametinib (Tram, 0.03 µM) for 1–2 h and were then stimulated with EGF (10 ng/mL), TNF-⍺ (20 ng/mL), or TPA (10 ng/mL) for 15–30 min. Whole-cell lysates were immunoblotted with EphA2, pS-EphA2, RSK1, pS-RSK1, p-ERK and β-actin antibodies. The relative quantification of pS-EphA2 shown in ( B ) is expressed as the mean ± SD of three independent experiments. P values were calculated by an ANOVA. * p < 0.05; ** p < 0.01; *** p < 0.001. ( C ) HeLa cells were pretreated with TNO155 (TNO, 1 µM) or BI-D1870 (BI, 10 µM) for 1 h and were then stimulated with TNF-⍺ (20 ng/mL) for 15 min. The expression of pS-EphA2 and EphA2 was analyzed by immunofluorescence. Representative images from three independent experiments are shown. ( D ) HeLa cells were transfected with siRNAs against GRB2 or the negative control and were then incubated for 48 h. Cells were stimulated with 20 ng/mL TNF-⍺ for 15 min. Whole-cell lysates were immunoblotted with GRB2, EphA2, pS-EphA2, and β-actin antibodies.

Figure Legend Snippet: EphA2 phosphorylation at Ser-897 is suppressed by SHP2 inhibitors. ( A ) HeLa cells were pretreated with SHP099 (SHP, 10 µM), TNO155 (TNO, 1 µM), BI-D1870 (BI, 10 µM), or trametinib (Tram, 0.03 µM) for 1–2 h and were then stimulated with EGF (10 ng/mL), TNF-⍺ (20 ng/mL), or TPA (10 ng/mL) for 15–30 min. Whole-cell lysates were immunoblotted with EphA2, pS-EphA2, RSK1, pS-RSK1, p-ERK and β-actin antibodies. The relative quantification of pS-EphA2 shown in ( B ) is expressed as the mean ± SD of three independent experiments. P values were calculated by an ANOVA. * p < 0.05; ** p < 0.01; *** p < 0.001. ( C ) HeLa cells were pretreated with TNO155 (TNO, 1 µM) or BI-D1870 (BI, 10 µM) for 1 h and were then stimulated with TNF-⍺ (20 ng/mL) for 15 min. The expression of pS-EphA2 and EphA2 was analyzed by immunofluorescence. Representative images from three independent experiments are shown. ( D ) HeLa cells were transfected with siRNAs against GRB2 or the negative control and were then incubated for 48 h. Cells were stimulated with 20 ng/mL TNF-⍺ for 15 min. Whole-cell lysates were immunoblotted with GRB2, EphA2, pS-EphA2, and β-actin antibodies.

Techniques Used: Phospho-proteomics, Quantitative Proteomics, Expressing, Immunofluorescence, Transfection, Negative Control, Incubation

Effects of SHP2 inhibitors on non-canonical EphA2 activation in LUAD cells. ( A ) Human lung adenocarcinoma cells (PC-9, HCC827, A925L, and A549) were treated with SHP099 (SHP, 10 µM), TNO155 (TNO, 1 µM), BI-D1870 (BI, 10 µM), or trametinib (Tram, 0.03 µM) for 1 h and were then stimulated with TNF-⍺ (20 ng/mL) for 15 min. Whole-cell lysates were immunoblotted with EphA2, pS-EphA2, RSK1, pS-RSK1, p-ERK and β-actin antibodies. ( B ) The relative quantification of pS-EphA2 shown in (A) is expressed as the mean ± SD of three independent experiments. P values were calculated by an ANOVA. * p < 0.05; ** p < 0.01; *** p < 0.001, n.s., not significant.

Figure Legend Snippet: Effects of SHP2 inhibitors on non-canonical EphA2 activation in LUAD cells. ( A ) Human lung adenocarcinoma cells (PC-9, HCC827, A925L, and A549) were treated with SHP099 (SHP, 10 µM), TNO155 (TNO, 1 µM), BI-D1870 (BI, 10 µM), or trametinib (Tram, 0.03 µM) for 1 h and were then stimulated with TNF-⍺ (20 ng/mL) for 15 min. Whole-cell lysates were immunoblotted with EphA2, pS-EphA2, RSK1, pS-RSK1, p-ERK and β-actin antibodies. ( B ) The relative quantification of pS-EphA2 shown in (A) is expressed as the mean ± SD of three independent experiments. P values were calculated by an ANOVA. * p < 0.05; ** p < 0.01; *** p < 0.001, n.s., not significant.

Techniques Used: Activation Assay, Quantitative Proteomics

The SHP2 inhibitor suppresses the migration of lung cancer cells. ( A ) PC-9 and A549 cells were treated with SHP099 (SHP, 10 µM), TNO155 (TNO, 1 µM), BI-D1870 (BI, 10 µM), or trametinib (Tram, 0.03 µM) for 1 h. Whole-cell lysates were immunoblotted with EphA2, pS-EphA2, RSK1, p-RSK1, p-ERK and β-actin antibodies. ( B ) The relative quantification of pS-EphA2/EphA2 shown in (A) is expressed as the mean ± SD of three independent experiments. ( C , D ) A549 cells were transfected with siRNAs targeting EphA2 or the negative control RNA and subsequently subjected to a wound healing assay. A monolayer of cells was scratched mechanically and incubated for 48 h. The EphA2 expression was analyzed by immunoblotting. ( E , F ) The wound healing assay was conducted using PC-9 and A549 cells treated with TNO155 (1–3 µM) or BI-D1870 (10 µM) for 24 and 48 h, respectively. ( G , H ) The wound healing assay was conducted using A549-EphA2-KO cells treated with TNO155 (1–3 µM). ( D , F , H ) Quantification of the wound area was performed by the ImageJ software and expressed as the mean ± SD of three independent experiments. P values were calculated by an ANOVA. * p < 0.05; ** p < 0.01; *** p < 0.001.

Figure Legend Snippet: The SHP2 inhibitor suppresses the migration of lung cancer cells. ( A ) PC-9 and A549 cells were treated with SHP099 (SHP, 10 µM), TNO155 (TNO, 1 µM), BI-D1870 (BI, 10 µM), or trametinib (Tram, 0.03 µM) for 1 h. Whole-cell lysates were immunoblotted with EphA2, pS-EphA2, RSK1, p-RSK1, p-ERK and β-actin antibodies. ( B ) The relative quantification of pS-EphA2/EphA2 shown in (A) is expressed as the mean ± SD of three independent experiments. ( C , D ) A549 cells were transfected with siRNAs targeting EphA2 or the negative control RNA and subsequently subjected to a wound healing assay. A monolayer of cells was scratched mechanically and incubated for 48 h. The EphA2 expression was analyzed by immunoblotting. ( E , F ) The wound healing assay was conducted using PC-9 and A549 cells treated with TNO155 (1–3 µM) or BI-D1870 (10 µM) for 24 and 48 h, respectively. ( G , H ) The wound healing assay was conducted using A549-EphA2-KO cells treated with TNO155 (1–3 µM). ( D , F , H ) Quantification of the wound area was performed by the ImageJ software and expressed as the mean ± SD of three independent experiments. P values were calculated by an ANOVA. * p < 0.05; ** p < 0.01; *** p < 0.001.

Techniques Used: Migration, Quantitative Proteomics, Transfection, Negative Control, Wound Healing Assay, Incubation, Expressing, Western Blot, Software

Membrane:

Article Title: Calcium phosphate-based nanomedicine mediated CRISPR/Cas9 delivery for prostate cancer therapy.
Article Snippet: The lysates were separated by 10% SDS-PAGE gel (Epizyme, China) and transferred onto polyvinylidene fluoride (PVDF) transfer membrane (Millipore, United States). .. The PVDF membrane was incubated with primary antibody against EphA2 (Rabbit mAb #4513, Cell Signaling Technology) at dilution of 1:1000, and then incubated in the secondary antibody for 1 h at room temperature. .. The protein bands were detected using an Enhanced Chemiluminescence (ECL) detection kit (Epizyme, China) and quantified using an Image J software (National Institutes of Health, Bethesda, MD, United States). β-actin was usually used as a loading control.

Article Title: Calcium phosphate-based nanomedicine mediated CRISPR/Cas9 delivery for prostate cancer therapy
Article Snippet: The lysates were separated by 10% SDS-PAGE gel (Epizyme, China) and transferred onto polyvinylidene fluoride (PVDF) transfer membrane (Millipore, United States). .. The PVDF membrane was incubated with primary antibody against EphA2 (Rabbit mAb #4513, Cell Signaling Technology) at dilution of 1:1000, and then incubated in the secondary antibody for 1 h at room temperature. .. The protein bands were detected using an Enhanced Chemiluminescence (ECL) detection kit (Epizyme, China) and quantified using an Image J software (National Institutes of Health, Bethesda, MD, United States). β-actin was usually used as a loading control.

Incubation:

Article Title: The EphA2 Receptor Regulates Invasiveness and Drug Sensitivity in Canine and Human Osteosarcoma Cells
Article Snippet: .. The primary antibody against EphA2 (#12927, Cell Signaling Technologies) was diluted in PBS containing 1% BSA and 0.3% Triton X-100 and added to sections, followed by incubation with the antibody for 1 h at room temperature. .. After three PBS washes, sections were incubated with HRP-conjugated secondary antibodies (Mouse specific HRP/DAB (ABC) Detection IHC Kit, Abcam, Toronto, ON, Canada, ab64259) for 30 min at room temperature.

Image Search Results

Journal: Scientific Reports

Article Title: Allosteric SHP2 inhibitors suppress lung cancer cell migration by inhibiting non-canonical activation of EphA2 via the ERK-RSK signaling pathway

doi: 10.1038/s41598-025-20770-8

Figure Lengend Snippet: EphA2 phosphorylation at Ser-897 is suppressed by SHP2 inhibitors. ( A ) HeLa cells were pretreated with SHP099 (SHP, 10 µM), TNO155 (TNO, 1 µM), BI-D1870 (BI, 10 µM), or trametinib (Tram, 0.03 µM) for 1–2 h and were then stimulated with EGF (10 ng/mL), TNF-⍺ (20 ng/mL), or TPA (10 ng/mL) for 15–30 min. Whole-cell lysates were immunoblotted with EphA2, pS-EphA2, RSK1, pS-RSK1, p-ERK and β-actin antibodies. The relative quantification of pS-EphA2 shown in ( B ) is expressed as the mean ± SD of three independent experiments. P values were calculated by an ANOVA. * p < 0.05; ** p < 0.01; *** p < 0.001. ( C ) HeLa cells were pretreated with TNO155 (TNO, 1 µM) or BI-D1870 (BI, 10 µM) for 1 h and were then stimulated with TNF-⍺ (20 ng/mL) for 15 min. The expression of pS-EphA2 and EphA2 was analyzed by immunofluorescence. Representative images from three independent experiments are shown. ( D ) HeLa cells were transfected with siRNAs against GRB2 or the negative control and were then incubated for 48 h. Cells were stimulated with 20 ng/mL TNF-⍺ for 15 min. Whole-cell lysates were immunoblotted with GRB2, EphA2, pS-EphA2, and β-actin antibodies.

Article Snippet: Phospho-specific antibodies against total EphA2 (D4A2; #6997S), phospho-EphA2 (Ser-897; #6347), phospho-ERK (Thr-202/Tyr-204; #9101), phospho-p38 (Thr-180/Tyr-182; #4511S), phospho-JNK (Thr-183/Tyr-185; #4671), phospho-p65 (Ser-536; #3033), phospho-SHP2 (Tyr-542; #15543), and phospho-RSK1 (Ser-380; #11989) were purchased from Cell Signaling Technology (Danvers, MA, USA).

Techniques: Phospho-proteomics, Quantitative Proteomics, Expressing, Immunofluorescence, Transfection, Negative Control, Incubation

Journal: Scientific Reports

Article Title: Allosteric SHP2 inhibitors suppress lung cancer cell migration by inhibiting non-canonical activation of EphA2 via the ERK-RSK signaling pathway

doi: 10.1038/s41598-025-20770-8

Figure Lengend Snippet: Effects of SHP2 inhibitors on non-canonical EphA2 activation in LUAD cells. ( A ) Human lung adenocarcinoma cells (PC-9, HCC827, A925L, and A549) were treated with SHP099 (SHP, 10 µM), TNO155 (TNO, 1 µM), BI-D1870 (BI, 10 µM), or trametinib (Tram, 0.03 µM) for 1 h and were then stimulated with TNF-⍺ (20 ng/mL) for 15 min. Whole-cell lysates were immunoblotted with EphA2, pS-EphA2, RSK1, pS-RSK1, p-ERK and β-actin antibodies. ( B ) The relative quantification of pS-EphA2 shown in (A) is expressed as the mean ± SD of three independent experiments. P values were calculated by an ANOVA. * p < 0.05; ** p < 0.01; *** p < 0.001, n.s., not significant.

Techniques: Activation Assay, Quantitative Proteomics

Journal: Scientific Reports

Article Title: Allosteric SHP2 inhibitors suppress lung cancer cell migration by inhibiting non-canonical activation of EphA2 via the ERK-RSK signaling pathway

doi: 10.1038/s41598-025-20770-8

Figure Lengend Snippet: The SHP2 inhibitor suppresses the migration of lung cancer cells. ( A ) PC-9 and A549 cells were treated with SHP099 (SHP, 10 µM), TNO155 (TNO, 1 µM), BI-D1870 (BI, 10 µM), or trametinib (Tram, 0.03 µM) for 1 h. Whole-cell lysates were immunoblotted with EphA2, pS-EphA2, RSK1, p-RSK1, p-ERK and β-actin antibodies. ( B ) The relative quantification of pS-EphA2/EphA2 shown in (A) is expressed as the mean ± SD of three independent experiments. ( C , D ) A549 cells were transfected with siRNAs targeting EphA2 or the negative control RNA and subsequently subjected to a wound healing assay. A monolayer of cells was scratched mechanically and incubated for 48 h. The EphA2 expression was analyzed by immunoblotting. ( E , F ) The wound healing assay was conducted using PC-9 and A549 cells treated with TNO155 (1–3 µM) or BI-D1870 (10 µM) for 24 and 48 h, respectively. ( G , H ) The wound healing assay was conducted using A549-EphA2-KO cells treated with TNO155 (1–3 µM). ( D , F , H ) Quantification of the wound area was performed by the ImageJ software and expressed as the mean ± SD of three independent experiments. P values were calculated by an ANOVA. * p < 0.05; ** p < 0.01; *** p < 0.001.

Techniques: Migration, Quantitative Proteomics, Transfection, Negative Control, Wound Healing Assay, Incubation, Expressing, Western Blot, Software

EphA2 confers growth advantage to NSCLC in vivo but not in vitro. ( A ) Confirmation of EphA2 overexpression in KPL and LLC cells by western blot. ( B , C ) In vitro cell viability of KPL and LLC cells with control and EphA2 overexpression by MTT and colony formation assays ( n = 4). ( D ) Representative image of bioluminescence signal in control and EphA2-overexpressing KPL tumors 14 days after subcutaneous implantation. ( E ) Representative image of bioluminescence signal 14 days after tail vein injection of control and EphA2-overexpressing KPL cells and quantification of bioluminescence signal at indicated time points (** p < 0.01, two-way ANOVA) ( F ) Representative gross specimens of GFP+ vector and EphA2-overexpressing KPL tumor-bearing lungs. ( G ) Survival of mice injected with vector or EphA2-overexpressiong KPL cells via tail vein (** p < 0.01, log-rank test). Data shown are averages ± SD.

Journal: Cancers

Article Title: Tumor-Specific EphA2 Receptor Tyrosine Kinase Inhibits Anti-Tumor Immunity by Recruiting Suppressive Myeloid Populations in Murine Models of Non-Small Cell Lung Cancer

doi: 10.3390/cancers17162693

Figure Lengend Snippet: EphA2 confers growth advantage to NSCLC in vivo but not in vitro. ( A ) Confirmation of EphA2 overexpression in KPL and LLC cells by western blot. ( B , C ) In vitro cell viability of KPL and LLC cells with control and EphA2 overexpression by MTT and colony formation assays ( n = 4). ( D ) Representative image of bioluminescence signal in control and EphA2-overexpressing KPL tumors 14 days after subcutaneous implantation. ( E ) Representative image of bioluminescence signal 14 days after tail vein injection of control and EphA2-overexpressing KPL cells and quantification of bioluminescence signal at indicated time points (** p < 0.01, two-way ANOVA) ( F ) Representative gross specimens of GFP+ vector and EphA2-overexpressing KPL tumor-bearing lungs. ( G ) Survival of mice injected with vector or EphA2-overexpressiong KPL cells via tail vein (** p < 0.01, log-rank test). Data shown are averages ± SD.

Article Snippet: Membranes were incubated with primary monoclonal antibodies against EphA2 (Cell Signaling Technologies #6997, 1/1000, Danvers, MA, USA) and tubulin (Sigma-Aldrich #T4026, 1/2000) overnight at 4 °C, followed by three washes with TBS-T and incubation with secondary antibodies goat anti-rabbit IRDye 800CW (LI-COR #926-32211, Lincoln, NE, USA) and anti-mouse IRDye 680LT (LI-COR #926-68020, 1/20,000) for one hour at room temperature.

Techniques: In Vivo, In Vitro, Over Expression, Western Blot, Control, Injection, Plasmid Preparation

EphA2 overexpression in NSCLC does not significantly impact tumor burden or immune infiltration in nude mice. ( A ) Tumor volumes over time and weights on day 14 post-implantation of control and EphA2-overexpressing KPL subcutaneous tumors from nude mice. ( B ) Flow cytometric analysis of GFP+ KPL tumor cells and total tumor-infiltrating immune cells, as well as ( C ) tumor-infiltrating NK cells, B cells, DCs, macrophages, and Gr1+ myeloid cells. ( D ) Similar flow cytometry analysis of immune populations from draining inguinal lymph nodes. Data shown are averages ± SD ( n = 4 mice per group).

Journal: Cancers

Article Title: Tumor-Specific EphA2 Receptor Tyrosine Kinase Inhibits Anti-Tumor Immunity by Recruiting Suppressive Myeloid Populations in Murine Models of Non-Small Cell Lung Cancer

doi: 10.3390/cancers17162693

Figure Lengend Snippet: EphA2 overexpression in NSCLC does not significantly impact tumor burden or immune infiltration in nude mice. ( A ) Tumor volumes over time and weights on day 14 post-implantation of control and EphA2-overexpressing KPL subcutaneous tumors from nude mice. ( B ) Flow cytometric analysis of GFP+ KPL tumor cells and total tumor-infiltrating immune cells, as well as ( C ) tumor-infiltrating NK cells, B cells, DCs, macrophages, and Gr1+ myeloid cells. ( D ) Similar flow cytometry analysis of immune populations from draining inguinal lymph nodes. Data shown are averages ± SD ( n = 4 mice per group).

Techniques: Over Expression, Control, Flow Cytometry

EphA2 overexpression in NSCLC decreases lymphocytic and increases myeloid infiltrate in tumor-bearing lungs. ( A ) Representative flow cytometry plots and quantification of GFP+ KPL and immune cells from vector control and EphA2-overexpressing tumor-bearing lungs on day 14 post-tail vein injection. ( B ) Similar flow plots and analysis of CD4+ and CD8+ T cells and NK cells, as well as ( C ) quantification of DCs, macrophages, and monocytes. Data shown are averages ± SD ( n = 3 mice per group, * p < 0.05; ** p < 0.01; *** p < 0.001, two-tailed unpaired Student’s t test with Welch correction).

Journal: Cancers

Article Title: Tumor-Specific EphA2 Receptor Tyrosine Kinase Inhibits Anti-Tumor Immunity by Recruiting Suppressive Myeloid Populations in Murine Models of Non-Small Cell Lung Cancer

doi: 10.3390/cancers17162693

Figure Lengend Snippet: EphA2 overexpression in NSCLC decreases lymphocytic and increases myeloid infiltrate in tumor-bearing lungs. ( A ) Representative flow cytometry plots and quantification of GFP+ KPL and immune cells from vector control and EphA2-overexpressing tumor-bearing lungs on day 14 post-tail vein injection. ( B ) Similar flow plots and analysis of CD4+ and CD8+ T cells and NK cells, as well as ( C ) quantification of DCs, macrophages, and monocytes. Data shown are averages ± SD ( n = 3 mice per group, * p < 0.05; ** p < 0.01; *** p < 0.001, two-tailed unpaired Student’s t test with Welch correction).

Techniques: Over Expression, Flow Cytometry, Plasmid Preparation, Control, Injection, Two Tailed Test

EphA2 overexpression in NSCLC suppresses tumor-infiltrating T cells. ( A ) Lung weights and quantification of GFP+ KPL cells via flow cytometry from vector control and EphA2-overexpressing tumor-bearing lungs with equalized tumor burden. ( B ) Flow cytometric analysis of total immune cells, CD4+ and CD8+ T cells, and NK cells in KPL tumor-bearing lungs. ( C ) Representative flow histograms of CD44 and CD69 expression on CD8 T cells and quantification of CD44, CD69, and CD25 activation markers on CD4 and CD8 T cells. ( D ) Quantification of PD-1 and CTLA-4 exhaustion markers on CD4+ and CD8+ T cells. Data shown are averages ± SD ( n = 3–6 mice per group, * p < 0.05; ** p < 0.01, two-tailed unpaired Student’s t test with Welch correction).

Journal: Cancers

Article Title: Tumor-Specific EphA2 Receptor Tyrosine Kinase Inhibits Anti-Tumor Immunity by Recruiting Suppressive Myeloid Populations in Murine Models of Non-Small Cell Lung Cancer

doi: 10.3390/cancers17162693

Figure Lengend Snippet: EphA2 overexpression in NSCLC suppresses tumor-infiltrating T cells. ( A ) Lung weights and quantification of GFP+ KPL cells via flow cytometry from vector control and EphA2-overexpressing tumor-bearing lungs with equalized tumor burden. ( B ) Flow cytometric analysis of total immune cells, CD4+ and CD8+ T cells, and NK cells in KPL tumor-bearing lungs. ( C ) Representative flow histograms of CD44 and CD69 expression on CD8 T cells and quantification of CD44, CD69, and CD25 activation markers on CD4 and CD8 T cells. ( D ) Quantification of PD-1 and CTLA-4 exhaustion markers on CD4+ and CD8+ T cells. Data shown are averages ± SD ( n = 3–6 mice per group, * p < 0.05; ** p < 0.01, two-tailed unpaired Student’s t test with Welch correction).

Techniques: Over Expression, Flow Cytometry, Plasmid Preparation, Control, Expressing, Activation Assay, Two Tailed Test

Gene expression profiling reveals higher expression of myeloid markers and chemoattractants in EphA2-overexpressing tumors. ( A ) Average pathway scores of vector control and EphA2-overexpressing KPL tumors calculated from normalized gene expression data using nanoString nSolver software. ( B ) Comparison of cancer progression and macrophage functions pathway scores between control and EphA2-overexpressing samples. ( n = 6 mice per group, ** p < 0.01, unpaired Mann-Whitney test) ( C ) Volcano plot of statistically significant differentially expressed genes. ( D ) Heatmap depicting standardized expression of differentially expressed myeloid markers (green bar), myeloid-attracting chemokines (pink bar), and immunosuppressive proteins (yellow bar). ( E ) RT-PCR validation of nanoString hits. ( n = 6 mice per group, * p < 0.05, one-sample Wilcoxon signed rank test). Data shown are averages ± SD.

Journal: Cancers

Article Title: Tumor-Specific EphA2 Receptor Tyrosine Kinase Inhibits Anti-Tumor Immunity by Recruiting Suppressive Myeloid Populations in Murine Models of Non-Small Cell Lung Cancer

doi: 10.3390/cancers17162693

Figure Lengend Snippet: Gene expression profiling reveals higher expression of myeloid markers and chemoattractants in EphA2-overexpressing tumors. ( A ) Average pathway scores of vector control and EphA2-overexpressing KPL tumors calculated from normalized gene expression data using nanoString nSolver software. ( B ) Comparison of cancer progression and macrophage functions pathway scores between control and EphA2-overexpressing samples. ( n = 6 mice per group, ** p < 0.01, unpaired Mann-Whitney test) ( C ) Volcano plot of statistically significant differentially expressed genes. ( D ) Heatmap depicting standardized expression of differentially expressed myeloid markers (green bar), myeloid-attracting chemokines (pink bar), and immunosuppressive proteins (yellow bar). ( E ) RT-PCR validation of nanoString hits. ( n = 6 mice per group, * p < 0.05, one-sample Wilcoxon signed rank test). Data shown are averages ± SD.

Techniques: Gene Expression, Expressing, Plasmid Preparation, Control, Software, Comparison, MANN-WHITNEY, Reverse Transcription Polymerase Chain Reaction, Biomarker Discovery

Bioinformatics analysis of EphA2 in endometriosis. A ) Volcanic map of endometriosis protein expression. B ) Heat maps of Eph/ephrin family mRNA expression in endometriosis. C ) EphA2 mRNA expression difference in normal, ectopic, and eutopic endometrium. D ) Immunoinfiltration correlation analysis of EphA2 in endometriosis. E ) Pathway enrichment analysis of EphA2 in endometriosis. The values represent mean±SD of three independent experiments. * p <0.05; ** p <0.01; *** p <0.001; ns, no statistical significance.

Journal: European Journal of Histochemistry : EJH

Article Title: Targeting EphA2 suppresses the proliferation, migration and invasion of endometriosis via the AMPK signaling pathway

doi: 10.4081/ejh.2025.4168

Figure Lengend Snippet: Bioinformatics analysis of EphA2 in endometriosis. A ) Volcanic map of endometriosis protein expression. B ) Heat maps of Eph/ephrin family mRNA expression in endometriosis. C ) EphA2 mRNA expression difference in normal, ectopic, and eutopic endometrium. D ) Immunoinfiltration correlation analysis of EphA2 in endometriosis. E ) Pathway enrichment analysis of EphA2 in endometriosis. The values represent mean±SD of three independent experiments. * p <0.05; ** p <0.01; *** p <0.001; ns, no statistical significance.

Article Snippet: The slides were blocked with 3% BSA, first by incubation overnight at 4°C with primary antibodies against EphA2 (#6997; Cell Signaling Technology, Danvers, MA, USA), CK19 (GB15198-100; Servicebio), and Vimentin (GB11192-100; Servicebio) diluted 1:500.

Techniques: Expressing

Changes of Eph mRNA and protein expression levels in ectopic, eutopic, and normal endometrium tissues. A ) EphA2 mRNA expression level was increased in endometriosis tissue. B ) EphA2 protein expression level was higher in endometriosis than in normal endometrial tissues were determined by Western blot. C ) Immunohistochemical analysis showing that EphA2 protein was overexpressed in endometriosis. Scale bar: 20 μm (400× magnification). The values represent mean±SD of three independent experiments. * p <0.05; ** p <0.01; *** p <0.001; ns, no statistical significance.

Journal: European Journal of Histochemistry : EJH

Article Title: Targeting EphA2 suppresses the proliferation, migration and invasion of endometriosis via the AMPK signaling pathway

doi: 10.4081/ejh.2025.4168

Figure Lengend Snippet: Changes of Eph mRNA and protein expression levels in ectopic, eutopic, and normal endometrium tissues. A ) EphA2 mRNA expression level was increased in endometriosis tissue. B ) EphA2 protein expression level was higher in endometriosis than in normal endometrial tissues were determined by Western blot. C ) Immunohistochemical analysis showing that EphA2 protein was overexpressed in endometriosis. Scale bar: 20 μm (400× magnification). The values represent mean±SD of three independent experiments. * p <0.05; ** p <0.01; *** p <0.001; ns, no statistical significance.

Techniques: Expressing, Western Blot, Immunohistochemical staining

Protein expression levels of primary eutopic endometriotic stromal cells after transfection with si-EphA2 or treatment with ALWII-41-27. A ) EphA2 protein expression in primary cells after si-EphA2 transfection. B ) EphA2 protein expression in primary cells treated with ALW-II-41-27. C ) Immunohistochemistry identification of primary cells; scale bar: 20 μm (400× magnification). D ) si-EphA2 sequence. The values represent mean ± SD of three independent experiments. * p <0.05; **p<0.01; *** p <0.001; ns, no statistical significance.

Journal: European Journal of Histochemistry : EJH

Article Title: Targeting EphA2 suppresses the proliferation, migration and invasion of endometriosis via the AMPK signaling pathway

doi: 10.4081/ejh.2025.4168

Figure Lengend Snippet: Protein expression levels of primary eutopic endometriotic stromal cells after transfection with si-EphA2 or treatment with ALWII-41-27. A ) EphA2 protein expression in primary cells after si-EphA2 transfection. B ) EphA2 protein expression in primary cells treated with ALW-II-41-27. C ) Immunohistochemistry identification of primary cells; scale bar: 20 μm (400× magnification). D ) si-EphA2 sequence. The values represent mean ± SD of three independent experiments. * p <0.05; **p<0.01; *** p <0.001; ns, no statistical significance.

Techniques: Expressing, Transfection, Immunohistochemistry, Sequencing

After transfection or si-EphA2 and treatment with ALW-II-41-27, the migration ability of primary eutopic endometriotic stromal cells were decreased. A ) Wound healing assay of primary cells after si-EphA2 transfection. B ) Wound healing assay of primary cells after treatment with ALW-II-41-27; representative images are shown at 0, 24 and 48 h; scale bar: 100 μm (100× magnification). The values represent mean±SD of three independent experiments. * p <0.05; ** p <0.01; *** p <0.001; ns, no statistical significance.

Journal: European Journal of Histochemistry : EJH

Article Title: Targeting EphA2 suppresses the proliferation, migration and invasion of endometriosis via the AMPK signaling pathway

doi: 10.4081/ejh.2025.4168

Figure Lengend Snippet: After transfection or si-EphA2 and treatment with ALW-II-41-27, the migration ability of primary eutopic endometriotic stromal cells were decreased. A ) Wound healing assay of primary cells after si-EphA2 transfection. B ) Wound healing assay of primary cells after treatment with ALW-II-41-27; representative images are shown at 0, 24 and 48 h; scale bar: 100 μm (100× magnification). The values represent mean±SD of three independent experiments. * p <0.05; ** p <0.01; *** p <0.001; ns, no statistical significance.

Techniques: Transfection, Migration, Wound Healing Assay

After transfection with si-EphA2 or treatment with ALW-II-41-27, the migration and invasion ability of primary eutopic endometriotic stromal cells were reduced. A ) Transwell migration experiment after transfection with si-EphA2 or treatment with ALW-II-41-27. B ) Transwell invasion experiment after transfection with si-EphA2 or treatment with ALW-II-41-27; scale bar: 100 μm (100× magnification). The values represent mean ± SD of three independent experiments. * p< 0.05; ** p <0.01; *** p <0.001; ns, no statistical significance.

Journal: European Journal of Histochemistry : EJH

Article Title: Targeting EphA2 suppresses the proliferation, migration and invasion of endometriosis via the AMPK signaling pathway

doi: 10.4081/ejh.2025.4168

Figure Lengend Snippet: After transfection with si-EphA2 or treatment with ALW-II-41-27, the migration and invasion ability of primary eutopic endometriotic stromal cells were reduced. A ) Transwell migration experiment after transfection with si-EphA2 or treatment with ALW-II-41-27. B ) Transwell invasion experiment after transfection with si-EphA2 or treatment with ALW-II-41-27; scale bar: 100 μm (100× magnification). The values represent mean ± SD of three independent experiments. * p< 0.05; ** p <0.01; *** p <0.001; ns, no statistical significance.

Techniques: Transfection, Migration

Review

antibodies against total epha2 (Cell Signaling Technology Inc)

Structured Review

Images

1) Product Images from "Allosteric SHP2 inhibitors suppress lung cancer cell migration by inhibiting non-canonical activation of EphA2 via the ERK-RSK signaling pathway"

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