Structured Review

Epitomics egfr
Expressions of Tat-interacting protein (TIP)30 and epidermal growth factor receptor <t>(EGFR)</t> in glioma and normal brain tissue samples. (A) (a) Negative expression of <t>TIP30</t> in glioma tissue samples. (b) Positive expression of TIP30 in normal tissue samples. (c) Strong positive expression of EGFR in glioma tissue samples. (d) Weak positive expression of epidermal growth factor receptor (EGFR) in normal brain tissue samples. (Magnification, ×400) (B) Protein expression of TIP30 and EGFR in glioma and normal brain tissue samples (P
Egfr, supplied by Epitomics, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/egfr/product/Epitomics
Average 92 stars, based on 7 article reviews
Price from $9.99 to $1999.99
egfr - by Bioz Stars, 2020-08
92/100 stars

Images

1) Product Images from "Overexpression of TIP30 inhibits the growth and invasion of glioma cells"

Article Title: Overexpression of TIP30 inhibits the growth and invasion of glioma cells

Journal: Molecular Medicine Reports

doi: 10.3892/mmr.2015.4619

Expressions of Tat-interacting protein (TIP)30 and epidermal growth factor receptor (EGFR) in glioma and normal brain tissue samples. (A) (a) Negative expression of TIP30 in glioma tissue samples. (b) Positive expression of TIP30 in normal tissue samples. (c) Strong positive expression of EGFR in glioma tissue samples. (d) Weak positive expression of epidermal growth factor receptor (EGFR) in normal brain tissue samples. (Magnification, ×400) (B) Protein expression of TIP30 and EGFR in glioma and normal brain tissue samples (P
Figure Legend Snippet: Expressions of Tat-interacting protein (TIP)30 and epidermal growth factor receptor (EGFR) in glioma and normal brain tissue samples. (A) (a) Negative expression of TIP30 in glioma tissue samples. (b) Positive expression of TIP30 in normal tissue samples. (c) Strong positive expression of EGFR in glioma tissue samples. (d) Weak positive expression of epidermal growth factor receptor (EGFR) in normal brain tissue samples. (Magnification, ×400) (B) Protein expression of TIP30 and EGFR in glioma and normal brain tissue samples (P

Techniques Used: Expressing

U87 glioma cell infection with lentivirus (LV)-Tat-interacting protein (TIP)30 induced significant downregulation of epidermal growth factor receptor (EGFR)/phosphorylated (p) extracellular signal-regulated kinases (ERK)/pAKT. The expression levels of EGFR, pERK, and pAKT were examined by western blotting in LV-TIP30 and LV-control (Con) U87 cells.
Figure Legend Snippet: U87 glioma cell infection with lentivirus (LV)-Tat-interacting protein (TIP)30 induced significant downregulation of epidermal growth factor receptor (EGFR)/phosphorylated (p) extracellular signal-regulated kinases (ERK)/pAKT. The expression levels of EGFR, pERK, and pAKT were examined by western blotting in LV-TIP30 and LV-control (Con) U87 cells.

Techniques Used: Infection, Expressing, Western Blot

2) Product Images from "Heterozygous deletion of ATG5 in ApcMin/+ mice promotes intestinal adenoma growth and enhances the antitumor efficacy of interferon-gamma"

Article Title: Heterozygous deletion of ATG5 in ApcMin/+ mice promotes intestinal adenoma growth and enhances the antitumor efficacy of interferon-gamma

Journal: Cancer Biology & Therapy

doi: 10.1080/15384047.2014.1002331

Heterozygous deletion of ATG5 promotes cell proliferation, activates Wnt/β-catenin and EGFR/ERK1/2 pathways and enhances the effects of IFN-γ-dependent suppression of these 2 signaling pathways. Western blotting assay showed the protein levels of PCNA (A), apoptosis-related protein including bax, bcl - 2 and PARP (B), Wnt signaling-related protein including nuclear β-catenin, cyclin D1 and Survivin (C) and EGFR/Erk1/2 signaling-related protein including EGFR, phospho-EGFR and phospho-Erk1/2 (D). The protein β-actin served as a loading control and for the study involving phospho-Erk1/2, total Erk1/2 served as a control. The data presented is representative of 3 experiments. Significant differences are not shown.
Figure Legend Snippet: Heterozygous deletion of ATG5 promotes cell proliferation, activates Wnt/β-catenin and EGFR/ERK1/2 pathways and enhances the effects of IFN-γ-dependent suppression of these 2 signaling pathways. Western blotting assay showed the protein levels of PCNA (A), apoptosis-related protein including bax, bcl - 2 and PARP (B), Wnt signaling-related protein including nuclear β-catenin, cyclin D1 and Survivin (C) and EGFR/Erk1/2 signaling-related protein including EGFR, phospho-EGFR and phospho-Erk1/2 (D). The protein β-actin served as a loading control and for the study involving phospho-Erk1/2, total Erk1/2 served as a control. The data presented is representative of 3 experiments. Significant differences are not shown.

Techniques Used: Western Blot

3) Product Images from "Dimerization of EGFR and HER2 induces breast cancer cell motility through STAT1-dependent ACTA2 induction"

Article Title: Dimerization of EGFR and HER2 induces breast cancer cell motility through STAT1-dependent ACTA2 induction

Journal: Oncotarget

doi: 10.18632/oncotarget.10843

ACTA2 and STAT1 expression are increased by HER2 overexpression in breast cancer cells A . The levels of p-HER2 (pT877), t-HER2, and t-EGFR expression were analyzed by western blots. ACTA2 and STAT1 mRNA expression were analyzed by real-time PCR. EGFR and HER2 expression were analyzed by confocal microscopy. B . ACTA2 and STAT1 expression patterns were analyzed by cDNA microarray analysis. C . Heatmap of ACTA2 and STAT1 expression in tumors from breast cancer patients generated using R statistical software. D . ACTA2, p-STAT1 (pS727), t-STAT1, and β-actin expression analyzed by western blots. ACTA2 and STAT1 mRNA expression were analyzed by real-time PCR. ACTA2 expression was analyzed by confocal microscopy. Results are representative of three independent experiments. Values are means ± SEM. * p
Figure Legend Snippet: ACTA2 and STAT1 expression are increased by HER2 overexpression in breast cancer cells A . The levels of p-HER2 (pT877), t-HER2, and t-EGFR expression were analyzed by western blots. ACTA2 and STAT1 mRNA expression were analyzed by real-time PCR. EGFR and HER2 expression were analyzed by confocal microscopy. B . ACTA2 and STAT1 expression patterns were analyzed by cDNA microarray analysis. C . Heatmap of ACTA2 and STAT1 expression in tumors from breast cancer patients generated using R statistical software. D . ACTA2, p-STAT1 (pS727), t-STAT1, and β-actin expression analyzed by western blots. ACTA2 and STAT1 mRNA expression were analyzed by real-time PCR. ACTA2 expression was analyzed by confocal microscopy. Results are representative of three independent experiments. Values are means ± SEM. * p

Techniques Used: Expressing, Over Expression, Western Blot, Real-time Polymerase Chain Reaction, Confocal Microscopy, Microarray, Generated, Software

4) Product Images from "The role of Thyroid Transcription Factor-1 and Tumor differentiation in Resected Lung Adenocarcinoma"

Article Title: The role of Thyroid Transcription Factor-1 and Tumor differentiation in Resected Lung Adenocarcinoma

Journal: Scientific Reports

doi: 10.1038/s41598-017-14651-y

( A ) Reverse transcription-polymerase chain reaction revealed that TTF-1 expression was significantly higher in CL1-0 cells. ( B ) Western blot analysis validated the difference in tumor aggressiveness between CL1-0, CL1-5, and H1299 cells with different E-cadherin and Vimentin expression. ( C ) The less aggressive cell lines CL1-0 revealed higher TTF-1 expression and lower high-mobility group AT-hook 2 expression. There was reciprocal change in EGFR expression.
Figure Legend Snippet: ( A ) Reverse transcription-polymerase chain reaction revealed that TTF-1 expression was significantly higher in CL1-0 cells. ( B ) Western blot analysis validated the difference in tumor aggressiveness between CL1-0, CL1-5, and H1299 cells with different E-cadherin and Vimentin expression. ( C ) The less aggressive cell lines CL1-0 revealed higher TTF-1 expression and lower high-mobility group AT-hook 2 expression. There was reciprocal change in EGFR expression.

Techniques Used: Reverse Transcription Polymerase Chain Reaction, Expressing, Western Blot

The expression of TTF-1, HMGA2, EMT markers and EGFR in CL1-0-SC, CL1-0-shTTF1, HCC827-SC, HCC827-shTTF1, CL1-5-Vector, CL1-5-TTF1, HCC827-GR-Vector and HCC827-GR-TTF1 cells were evaluated by western blotting. ( A ) The expression of HMGA2, mesenchymal markers and EGFR increased in CL1-0 and HCC827 cells but expression of epithelial markers decreased after knocked down TTF-1 by shRNA. ( B ) The expression of HMGA2, mesenchymal markers and EGFR decreased but expression of epithelial markers increased in CL1-5 and HCC827-GR cells following overexpression of TTF-1 by human TTF-1 cDNA ORF clone. The Western blotting was independently repeated three times, and the representative data are shown. GAPDH was served as a loading control.
Figure Legend Snippet: The expression of TTF-1, HMGA2, EMT markers and EGFR in CL1-0-SC, CL1-0-shTTF1, HCC827-SC, HCC827-shTTF1, CL1-5-Vector, CL1-5-TTF1, HCC827-GR-Vector and HCC827-GR-TTF1 cells were evaluated by western blotting. ( A ) The expression of HMGA2, mesenchymal markers and EGFR increased in CL1-0 and HCC827 cells but expression of epithelial markers decreased after knocked down TTF-1 by shRNA. ( B ) The expression of HMGA2, mesenchymal markers and EGFR decreased but expression of epithelial markers increased in CL1-5 and HCC827-GR cells following overexpression of TTF-1 by human TTF-1 cDNA ORF clone. The Western blotting was independently repeated three times, and the representative data are shown. GAPDH was served as a loading control.

Techniques Used: Expressing, Plasmid Preparation, Western Blot, shRNA, Over Expression

5) Product Images from "SERPINA3 promotes endometrial cancer cells growth by regulating G2/M cell cycle checkpoint and apoptosis"

Article Title: SERPINA3 promotes endometrial cancer cells growth by regulating G2/M cell cycle checkpoint and apoptosis

Journal: International Journal of Clinical and Experimental Pathology

doi:

Knockdown of SERPINA3 inhibits activation of ERK1/2 and AKT. Analysis of activation of ERK1/2, AKT, Src, EGFR and FAK in SERPINA3 knockdown HEC-1A and KLE cells, using GAPDH as a loading control.
Figure Legend Snippet: Knockdown of SERPINA3 inhibits activation of ERK1/2 and AKT. Analysis of activation of ERK1/2, AKT, Src, EGFR and FAK in SERPINA3 knockdown HEC-1A and KLE cells, using GAPDH as a loading control.

Techniques Used: Activation Assay

Related Articles

Staining:

Article Title: The Significance of Co-Expression of Epidermal Growth Factor Receptor (EGFR) and Ki67 on Clinical Outcome in Patients with Anal Cancer Treated with Chemoradiotherapy: An Analysis of NRG Oncology RTOG 9811
Article Snippet: .. Slides were incubated for 15 minutes in Signal Stain® Antibody Diluent, followed by a 60 minute room temperature incubation in Signal Stain® Antibody Diluent with a 1:1000 dilution of EGFR (rabbit monoclonal anti-EGFR, Epitomics) combined with a 1:100 dilution of guinea pig anti-pan-cytokeratin antibody (polyclonal, Acris) to identify tumor cells. .. After three washes in wash buffer, the secondary antibody was applied for 60 minutes at room temperature (goat anti-rabbit antibody conjugated to a horseradish peroxidase-decorated dextran polymer backbone from the Dako EnVision™+ system and a 1:200 dilution of Alexa488 conjugated anti-guinea pig secondary antibody, Invitrogen).

Incubation:

Article Title: The Significance of Co-Expression of Epidermal Growth Factor Receptor (EGFR) and Ki67 on Clinical Outcome in Patients with Anal Cancer Treated with Chemoradiotherapy: An Analysis of NRG Oncology RTOG 9811
Article Snippet: .. Slides were incubated for 15 minutes in Signal Stain® Antibody Diluent, followed by a 60 minute room temperature incubation in Signal Stain® Antibody Diluent with a 1:1000 dilution of EGFR (rabbit monoclonal anti-EGFR, Epitomics) combined with a 1:100 dilution of guinea pig anti-pan-cytokeratin antibody (polyclonal, Acris) to identify tumor cells. .. After three washes in wash buffer, the secondary antibody was applied for 60 minutes at room temperature (goat anti-rabbit antibody conjugated to a horseradish peroxidase-decorated dextran polymer backbone from the Dako EnVision™+ system and a 1:200 dilution of Alexa488 conjugated anti-guinea pig secondary antibody, Invitrogen).

Article Title: The role of Thyroid Transcription Factor-1 and Tumor differentiation in Resected Lung Adenocarcinoma
Article Snippet: .. The membrane was incubated with primary antibodies against TTF-1 (1:500, SC-53136, Santa Cruz, Dallas, USA), HMGA2 (1:500, #5269, Cell Signaling, Danvers, MA, USA), EGFR (1:1000, #2116 S, Epitomics, Burlingame, USA), E-cadherin (1:1,000, #610182, BD, San Jose, CA,USA), ZO-1 (1:1,000, #610966, BD, San Jose, CA,USA), Vimentin (1:500, #5741, Cell Signaling, Danvers, MA, USA), Fibronectin (1:500, ab32419, Abcam, Cambridge, UK), phosphor-EGFR (1:25; ab134005, Abcam, Cambridge, UK). .. GAPDH (1:5000, #5147, Cell Signaling, Danvers, MA, USA) was used as the loading control.

Article Title: Overexpression of TIP30 inhibits the growth and invasion of glioma cells
Article Snippet: .. The samples were then incubated with polyclonal antibodies targeting TIP30 (1:50; cat. no. ab22841; Abcam, Cambridge, UK) and EGFR (1:400; cat. no. 1902–1; Epitomics, Burlingame, CA, USA) at 4°C overnight. .. IHC images were captured using an Olympus fluorescence microscope (Olympus CKX41; Olympus Corporation, Tokyo, Japan) equipped with a camera.

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    Epitomics antibodies against egfr
    Correlation of gefitinib sensitivity with expression levels of <t>EGFR</t> and <t>HER2.</t> (A) Cellular protein levels of EGFR and HER2 were determined by western blotting using 30 µg total cell lysates of each cell type. MTT assays were performed for cells
    Antibodies Against Egfr, supplied by Epitomics, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/antibodies against egfr/product/Epitomics
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    antibodies against egfr - by Bioz Stars, 2020-08
    90/100 stars
      Buy from Supplier

    85
    Epitomics anti egfr rabbit monoclonal antibody
    <t>CXCR7</t> depletion slows PC-3 tumor growth in mice A , Tumor growth over time in athymic mice was recorded for mice injected with PC-3 cells stably expressing CXCR7 shRNA (T73 and T74) or scrambled sequence-shRNA (V) B , Blots of CXCR7, cyclin D1 <t>p-EGFR</t> CXCR7 tumor tissue of PC-3V, T73 and T74 C–D , CXCR7 and VEGF mRNA level were decreased in T73 and T74 tumors as analyzed by q-PCR. There was a significant delay (p
    Anti Egfr Rabbit Monoclonal Antibody, supplied by Epitomics, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti egfr rabbit monoclonal antibody/product/Epitomics
    Average 85 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    anti egfr rabbit monoclonal antibody - by Bioz Stars, 2020-08
    85/100 stars
      Buy from Supplier

    85
    Epitomics polyclonal rabbit anti phosho egfr s695
    Distribution of epidermal growth factor and transferrin receptors in control and breast cancer tissue. Representative tissues were stained with (A) monoclonal rabbit <t>anti-phospho-EGFr</t> (pT693); <t>polyclonal</t> rabbit <t>anti-phosho-EGFr</t> (s695) (B) and monoclonal rabbit anti-CD71 (TFRC). (A) Weak staining of both EGFr (pT693) and EGFr (s659) was observed in the control breast tissue in contrast to strong staining observed in the invasive breast carcinoma tissue. (C) Control breast expressing transferrin receptor (red) (i) showed relatively equal amounts of expression in breast cancer (ii). Merged image: nucleus stained with DAPI (blue), EGFr and CD71 (red), β-actin (green). Images were acquired using an Olympus BX61 fluorescence microscope with automated FVII camera. Bar = 200μm, 100μm; x10, x20 magnification respectively.
    Polyclonal Rabbit Anti Phosho Egfr S695, supplied by Epitomics, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal rabbit anti phosho egfr s695/product/Epitomics
    Average 85 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    polyclonal rabbit anti phosho egfr s695 - by Bioz Stars, 2020-08
    85/100 stars
      Buy from Supplier

    Image Search Results


    Correlation of gefitinib sensitivity with expression levels of EGFR and HER2. (A) Cellular protein levels of EGFR and HER2 were determined by western blotting using 30 µg total cell lysates of each cell type. MTT assays were performed for cells

    Journal: Oncology Letters

    Article Title: HER2 overexpression reverses the relative resistance of EGFR-mutant H1975 cell line to gefitinib

    doi: 10.3892/ol.2016.5373

    Figure Lengend Snippet: Correlation of gefitinib sensitivity with expression levels of EGFR and HER2. (A) Cellular protein levels of EGFR and HER2 were determined by western blotting using 30 µg total cell lysates of each cell type. MTT assays were performed for cells

    Article Snippet: Antibodies against EGFR (ab52894; 1:1,000), HER2 (ab134182; 1:10,000), HER3 (ab32121; 1:1,000), Erk1/2 (ab196883; 1:1,000), Akt (ab32505; 1:5,000); phospho-Akt (Ser473) (ab81283; 1:5,000), phospho-HER3 (ab5470; 1:500) and β-actin (ab6276; 1:5,000) were obtained from Epitomics (Abcam, Cambridge, MA, USA).

    Techniques: Expressing, Western Blot, MTT Assay

    CXCR7 depletion slows PC-3 tumor growth in mice A , Tumor growth over time in athymic mice was recorded for mice injected with PC-3 cells stably expressing CXCR7 shRNA (T73 and T74) or scrambled sequence-shRNA (V) B , Blots of CXCR7, cyclin D1 p-EGFR CXCR7 tumor tissue of PC-3V, T73 and T74 C–D , CXCR7 and VEGF mRNA level were decreased in T73 and T74 tumors as analyzed by q-PCR. There was a significant delay (p

    Journal: Cancer research

    Article Title: The IL-8 regulated Chemokine Receptor CXCR7 Stimulates EGFR Signaling to Promote Prostate Cancer Growth

    doi: 10.1158/0008-5472.CAN-10-2769

    Figure Lengend Snippet: CXCR7 depletion slows PC-3 tumor growth in mice A , Tumor growth over time in athymic mice was recorded for mice injected with PC-3 cells stably expressing CXCR7 shRNA (T73 and T74) or scrambled sequence-shRNA (V) B , Blots of CXCR7, cyclin D1 p-EGFR CXCR7 tumor tissue of PC-3V, T73 and T74 C–D , CXCR7 and VEGF mRNA level were decreased in T73 and T74 tumors as analyzed by q-PCR. There was a significant delay (p

    Article Snippet: In brief, lysates were incubated with anti-CXCR7 rabbit IgG (10 μg/ml, GeneTex)), with anti-EGFR Rabbit monoclonal antibody (Epitomics Inc., Santa Clara, CA) or normal rabbit IgG, overnight at 4°C, followed by incubation with protein A-Sepharose beads for 6 h at 4°C.

    Techniques: Mouse Assay, Injection, Stable Transfection, Expressing, shRNA, Sequencing, Polymerase Chain Reaction

    Forced Expression of CXCR7 increases cell proliferation and p-EGFR levels A , Increase in cell density of RWPE-1 cultures stably expressing CXCR7 (RWCX7) as compared to RW-V cells, B , A comparison of levels of p-EGFR, p-Erk1/2 and cyclinD1 in cells described in A and CaP cells. C , Levels of p-EGFR and p-Erk1/2 in CaP cells following transient transfection with either c-siRNA (c-si) or CXCR7 siRNA (CX7) and stimulated with EGF (5 nM) for 5 min. CXCR7siRNA transfectants had lower level of p-EGFR and p-Erk1/2 compared to that of c-siRNA transfected cells (C Lanes 2 and 4). D , Western blots of pEGFR y1110 from cells described in A that were growth factor starved for 24 h and then stimulated with 5 nM EGF, CXCL11 or SDF-1 (both 100 ng/ml). Total EGFR and ß-actin levels are shown as loading controls.

    Journal: Cancer research

    Article Title: The IL-8 regulated Chemokine Receptor CXCR7 Stimulates EGFR Signaling to Promote Prostate Cancer Growth

    doi: 10.1158/0008-5472.CAN-10-2769

    Figure Lengend Snippet: Forced Expression of CXCR7 increases cell proliferation and p-EGFR levels A , Increase in cell density of RWPE-1 cultures stably expressing CXCR7 (RWCX7) as compared to RW-V cells, B , A comparison of levels of p-EGFR, p-Erk1/2 and cyclinD1 in cells described in A and CaP cells. C , Levels of p-EGFR and p-Erk1/2 in CaP cells following transient transfection with either c-siRNA (c-si) or CXCR7 siRNA (CX7) and stimulated with EGF (5 nM) for 5 min. CXCR7siRNA transfectants had lower level of p-EGFR and p-Erk1/2 compared to that of c-siRNA transfected cells (C Lanes 2 and 4). D , Western blots of pEGFR y1110 from cells described in A that were growth factor starved for 24 h and then stimulated with 5 nM EGF, CXCL11 or SDF-1 (both 100 ng/ml). Total EGFR and ß-actin levels are shown as loading controls.

    Article Snippet: In brief, lysates were incubated with anti-CXCR7 rabbit IgG (10 μg/ml, GeneTex)), with anti-EGFR Rabbit monoclonal antibody (Epitomics Inc., Santa Clara, CA) or normal rabbit IgG, overnight at 4°C, followed by incubation with protein A-Sepharose beads for 6 h at 4°C.

    Techniques: Expressing, Stable Transfection, Transfection, Western Blot

    CXCR7 associates with EGFR in CaP cells A–B , Demonstration of coimmunoprecipitation of CXCR7 and EGFR. Cell lysates of PC-3 and LNCaP were immunoprecipitated with CXCR7 antibody followed by western blotting against p-EGFR and vice versa . C , EGFR co-precipitated with CXCR7 in RWCX7 cells. RWCX7 cells or control vector (RW-V), were immunoprecipitated with CXCR7 antibody followed by western blotting with an anti- p-EGFR (pY1110) or an antibody recognizing phospho-Ser at residue 1070-71 in EGFR (pS1070-71) (Epitomics).

    Journal: Cancer research

    Article Title: The IL-8 regulated Chemokine Receptor CXCR7 Stimulates EGFR Signaling to Promote Prostate Cancer Growth

    doi: 10.1158/0008-5472.CAN-10-2769

    Figure Lengend Snippet: CXCR7 associates with EGFR in CaP cells A–B , Demonstration of coimmunoprecipitation of CXCR7 and EGFR. Cell lysates of PC-3 and LNCaP were immunoprecipitated with CXCR7 antibody followed by western blotting against p-EGFR and vice versa . C , EGFR co-precipitated with CXCR7 in RWCX7 cells. RWCX7 cells or control vector (RW-V), were immunoprecipitated with CXCR7 antibody followed by western blotting with an anti- p-EGFR (pY1110) or an antibody recognizing phospho-Ser at residue 1070-71 in EGFR (pS1070-71) (Epitomics).

    Article Snippet: In brief, lysates were incubated with anti-CXCR7 rabbit IgG (10 μg/ml, GeneTex)), with anti-EGFR Rabbit monoclonal antibody (Epitomics Inc., Santa Clara, CA) or normal rabbit IgG, overnight at 4°C, followed by incubation with protein A-Sepharose beads for 6 h at 4°C.

    Techniques: Immunoprecipitation, Western Blot, Plasmid Preparation

    SB431542, but not SIS, inhibited EGFR signaling in WT COCs. A, Egfr mRNA expression in COCs treated with DMSO, SB431542, or SIS for 20 h. B, Western blot analysis of EGFR, p-SMAD2, and β-actin (ACTB) in the same experimental groups as stated in panel A 20 h after culture. C, Changes of the levels of p-MAPK3/1 in the same experimental groups as stated in panel A after the initial 20-h culture and then treated with or without (control) AREG for 30 min. Groups indicated with different letters are significantly different, P

    Journal: Molecular Endocrinology

    Article Title: Mouse Oocytes Enable LH-Induced Maturation of the Cumulus-Oocyte Complex via Promoting EGF Receptor-Dependent Signaling

    doi: 10.1210/me.2009-0497

    Figure Lengend Snippet: SB431542, but not SIS, inhibited EGFR signaling in WT COCs. A, Egfr mRNA expression in COCs treated with DMSO, SB431542, or SIS for 20 h. B, Western blot analysis of EGFR, p-SMAD2, and β-actin (ACTB) in the same experimental groups as stated in panel A 20 h after culture. C, Changes of the levels of p-MAPK3/1 in the same experimental groups as stated in panel A after the initial 20-h culture and then treated with or without (control) AREG for 30 min. Groups indicated with different letters are significantly different, P

    Article Snippet: The following primary and secondary antibodies were used for protein detection: EGFR (pan) rabbit monoclonal antibody (Epitomics, Burlingame, CA), Monoclonal anti-β-actin (Sigma-Aldrich), rabbit antiphospho-Smad2 (Ser465/Ser467) (Zymed Laboratories, Inc., South San Francisco, CA; Invitrogen), monoclonal antidiphosphorylated ERK-1 and 2 antibody (Sigma-Aldrich), polyclonal anti-MAPK antibody (Sigma-Aldrich), stabilized peroxidase-conjugated goat antimouse IgG (Thermo Fisher Scientific, Rockford, IL), and stabilized peroxidase conjugated goat antirabbit IgG (Thermo Fisher Scientific, Rockford, IL).

    Techniques: Expressing, Western Blot

    Coculture with WT- but not DM-oocytes promotes EGFR signaling in WT OOX cumulus cells. A, Levels of Egfr mRNA expressed in WT, COCs, OOX cumulus cells (OOX), OOX cumulus cell cocultured with WT Oocytes (OOX+WT), or DM oocytes (OOX+DM), 20 h after culture. B, Western blot analysis of EGFR, p-SMAD2, and β-actin (ACTB) in the same experimental groups as stated in panel A 20 h after culture. C, Changes of the levels of p-MAPK3/1 in the same experimental groups as stated in panel A after the initial 20-h culture and then treated with or without (control) AREG for 30 min. Groups indicated with different letters are significantly different, P

    Journal: Molecular Endocrinology

    Article Title: Mouse Oocytes Enable LH-Induced Maturation of the Cumulus-Oocyte Complex via Promoting EGF Receptor-Dependent Signaling

    doi: 10.1210/me.2009-0497

    Figure Lengend Snippet: Coculture with WT- but not DM-oocytes promotes EGFR signaling in WT OOX cumulus cells. A, Levels of Egfr mRNA expressed in WT, COCs, OOX cumulus cells (OOX), OOX cumulus cell cocultured with WT Oocytes (OOX+WT), or DM oocytes (OOX+DM), 20 h after culture. B, Western blot analysis of EGFR, p-SMAD2, and β-actin (ACTB) in the same experimental groups as stated in panel A 20 h after culture. C, Changes of the levels of p-MAPK3/1 in the same experimental groups as stated in panel A after the initial 20-h culture and then treated with or without (control) AREG for 30 min. Groups indicated with different letters are significantly different, P

    Article Snippet: The following primary and secondary antibodies were used for protein detection: EGFR (pan) rabbit monoclonal antibody (Epitomics, Burlingame, CA), Monoclonal anti-β-actin (Sigma-Aldrich), rabbit antiphospho-Smad2 (Ser465/Ser467) (Zymed Laboratories, Inc., South San Francisco, CA; Invitrogen), monoclonal antidiphosphorylated ERK-1 and 2 antibody (Sigma-Aldrich), polyclonal anti-MAPK antibody (Sigma-Aldrich), stabilized peroxidase-conjugated goat antimouse IgG (Thermo Fisher Scientific, Rockford, IL), and stabilized peroxidase conjugated goat antirabbit IgG (Thermo Fisher Scientific, Rockford, IL).

    Techniques: Western Blot

    Recombinant GDF9 and/or BMP15 promote EGFR signaling in WT OOX cumulus cells. A, Egfr mRNA expression in OOX cumulus cells after being treated with GDF9 and/or BMP15 for 20 h. Levels of Egfr mRNA are presented as relative to COCs (COC = 1). B, Western blot analysis of EGFR, p-SMAD2, and β-actin (ACTB) in the same experimental groups as stated in panel A 20 h after culture. C, Changes of the levels of p-MAPK3/1 in the same experimental groups as stated in panel A after the initial 20-h culture and then treated with or without (control) AREG for 30 min. Groups indicated with different letters are significantly different, P

    Journal: Molecular Endocrinology

    Article Title: Mouse Oocytes Enable LH-Induced Maturation of the Cumulus-Oocyte Complex via Promoting EGF Receptor-Dependent Signaling

    doi: 10.1210/me.2009-0497

    Figure Lengend Snippet: Recombinant GDF9 and/or BMP15 promote EGFR signaling in WT OOX cumulus cells. A, Egfr mRNA expression in OOX cumulus cells after being treated with GDF9 and/or BMP15 for 20 h. Levels of Egfr mRNA are presented as relative to COCs (COC = 1). B, Western blot analysis of EGFR, p-SMAD2, and β-actin (ACTB) in the same experimental groups as stated in panel A 20 h after culture. C, Changes of the levels of p-MAPK3/1 in the same experimental groups as stated in panel A after the initial 20-h culture and then treated with or without (control) AREG for 30 min. Groups indicated with different letters are significantly different, P

    Article Snippet: The following primary and secondary antibodies were used for protein detection: EGFR (pan) rabbit monoclonal antibody (Epitomics, Burlingame, CA), Monoclonal anti-β-actin (Sigma-Aldrich), rabbit antiphospho-Smad2 (Ser465/Ser467) (Zymed Laboratories, Inc., South San Francisco, CA; Invitrogen), monoclonal antidiphosphorylated ERK-1 and 2 antibody (Sigma-Aldrich), polyclonal anti-MAPK antibody (Sigma-Aldrich), stabilized peroxidase-conjugated goat antimouse IgG (Thermo Fisher Scientific, Rockford, IL), and stabilized peroxidase conjugated goat antirabbit IgG (Thermo Fisher Scientific, Rockford, IL).

    Techniques: Recombinant, Expressing, Western Blot

    SB431542, but not SIS, inhibited GDF9-induced EGFR signaling in WT OOX cumulus cells. A, Quantification of Egfr mRNA expressed in OOX cumulus cells (OOX), OOX cumulus cells treated with GDF9 (OOX+GDF9), GDF9 and SB431542 (OOX+GDF9+SB), or SIS (OOX+GDF9+SIS) for 20 h. B, Western blot analysis of EGFR, p-SMAD2, and β-actin (ACTB) in the same experimental groups as stated in panel A 20 h after culture. C, Changes of the levels of p-MAPK3/1 in the same experimental groups as stated in panel A after the initial 20-h culture and then treated with or without (control) AREG for 30 min. Groups indicated with different letters are significantly different, P

    Journal: Molecular Endocrinology

    Article Title: Mouse Oocytes Enable LH-Induced Maturation of the Cumulus-Oocyte Complex via Promoting EGF Receptor-Dependent Signaling

    doi: 10.1210/me.2009-0497

    Figure Lengend Snippet: SB431542, but not SIS, inhibited GDF9-induced EGFR signaling in WT OOX cumulus cells. A, Quantification of Egfr mRNA expressed in OOX cumulus cells (OOX), OOX cumulus cells treated with GDF9 (OOX+GDF9), GDF9 and SB431542 (OOX+GDF9+SB), or SIS (OOX+GDF9+SIS) for 20 h. B, Western blot analysis of EGFR, p-SMAD2, and β-actin (ACTB) in the same experimental groups as stated in panel A 20 h after culture. C, Changes of the levels of p-MAPK3/1 in the same experimental groups as stated in panel A after the initial 20-h culture and then treated with or without (control) AREG for 30 min. Groups indicated with different letters are significantly different, P

    Article Snippet: The following primary and secondary antibodies were used for protein detection: EGFR (pan) rabbit monoclonal antibody (Epitomics, Burlingame, CA), Monoclonal anti-β-actin (Sigma-Aldrich), rabbit antiphospho-Smad2 (Ser465/Ser467) (Zymed Laboratories, Inc., South San Francisco, CA; Invitrogen), monoclonal antidiphosphorylated ERK-1 and 2 antibody (Sigma-Aldrich), polyclonal anti-MAPK antibody (Sigma-Aldrich), stabilized peroxidase-conjugated goat antimouse IgG (Thermo Fisher Scientific, Rockford, IL), and stabilized peroxidase conjugated goat antirabbit IgG (Thermo Fisher Scientific, Rockford, IL).

    Techniques: Western Blot

    Impaired EGFR signaling in cumulus cells freshly isolated from eCG-primed Bmp15 −/− and DM mice. A, Real-time RT-PCR quantification of Egfr mRNA expressed in WT-, Bmp15 −/− - and DM cumulus cells. B, Western blot analysis of EGFR, phosphorylated SMAD2 (p-SMAD2), and β-actin (ACTB) in WT-, Bmp15 −/− -, and DM cumulus cells. *, P

    Journal: Molecular Endocrinology

    Article Title: Mouse Oocytes Enable LH-Induced Maturation of the Cumulus-Oocyte Complex via Promoting EGF Receptor-Dependent Signaling

    doi: 10.1210/me.2009-0497

    Figure Lengend Snippet: Impaired EGFR signaling in cumulus cells freshly isolated from eCG-primed Bmp15 −/− and DM mice. A, Real-time RT-PCR quantification of Egfr mRNA expressed in WT-, Bmp15 −/− - and DM cumulus cells. B, Western blot analysis of EGFR, phosphorylated SMAD2 (p-SMAD2), and β-actin (ACTB) in WT-, Bmp15 −/− -, and DM cumulus cells. *, P

    Article Snippet: The following primary and secondary antibodies were used for protein detection: EGFR (pan) rabbit monoclonal antibody (Epitomics, Burlingame, CA), Monoclonal anti-β-actin (Sigma-Aldrich), rabbit antiphospho-Smad2 (Ser465/Ser467) (Zymed Laboratories, Inc., South San Francisco, CA; Invitrogen), monoclonal antidiphosphorylated ERK-1 and 2 antibody (Sigma-Aldrich), polyclonal anti-MAPK antibody (Sigma-Aldrich), stabilized peroxidase-conjugated goat antimouse IgG (Thermo Fisher Scientific, Rockford, IL), and stabilized peroxidase conjugated goat antirabbit IgG (Thermo Fisher Scientific, Rockford, IL).

    Techniques: Isolation, Mouse Assay, Quantitative RT-PCR, Western Blot

    Distribution of epidermal growth factor and transferrin receptors in control and breast cancer tissue. Representative tissues were stained with (A) monoclonal rabbit anti-phospho-EGFr (pT693); polyclonal rabbit anti-phosho-EGFr (s695) (B) and monoclonal rabbit anti-CD71 (TFRC). (A) Weak staining of both EGFr (pT693) and EGFr (s659) was observed in the control breast tissue in contrast to strong staining observed in the invasive breast carcinoma tissue. (C) Control breast expressing transferrin receptor (red) (i) showed relatively equal amounts of expression in breast cancer (ii). Merged image: nucleus stained with DAPI (blue), EGFr and CD71 (red), β-actin (green). Images were acquired using an Olympus BX61 fluorescence microscope with automated FVII camera. Bar = 200μm, 100μm; x10, x20 magnification respectively.

    Journal: American Journal of Translational Research

    Article Title: An atlas of histone deacetylase expression in breast cancer: fluorescence methodology for comparative semi-quantitative analysis

    doi:

    Figure Lengend Snippet: Distribution of epidermal growth factor and transferrin receptors in control and breast cancer tissue. Representative tissues were stained with (A) monoclonal rabbit anti-phospho-EGFr (pT693); polyclonal rabbit anti-phosho-EGFr (s695) (B) and monoclonal rabbit anti-CD71 (TFRC). (A) Weak staining of both EGFr (pT693) and EGFr (s659) was observed in the control breast tissue in contrast to strong staining observed in the invasive breast carcinoma tissue. (C) Control breast expressing transferrin receptor (red) (i) showed relatively equal amounts of expression in breast cancer (ii). Merged image: nucleus stained with DAPI (blue), EGFr and CD71 (red), β-actin (green). Images were acquired using an Olympus BX61 fluorescence microscope with automated FVII camera. Bar = 200μm, 100μm; x10, x20 magnification respectively.

    Article Snippet: Tissue sections were outlined using a pap pen and blocked for 1 hour in Superblock (Thermo Scientific) followed by an overnight incubation in a humidified chamber with primary antibodies diluted in 1% BSA: polyclonal rabbit anti-HDAC1-11 (K333-11-30; Biovision) at a concentration of 10 μg/ml, monoclonal rabbit anti-HDAC4 (1576-1;Epitomics) diluted 1:500 and monoclonal mouse anti-HDAC8 (H6412; Sigma) diluted (1:500); polyclonal goat anti-beta actin (ab8229; Abcam) diluted to 5 μg/ml; monoclonal rabbit anti-Annexin V (2792-1; Epitomics); monoclonal rabbit anti-phospho-EGFr (pT693) (2343-1; Epitomics); polyclonal rabbit anti-phosho-EGFr (s695) (T3868; Epitomics) and monoclonal rabbit anti-CD71 (TFRC) (2918-1; Epitomics).

    Techniques: Staining, Expressing, Fluorescence, Microscopy

    Distribution epidermal growth factor (EGFr) and transferrin receptors. MCF7 and A431 cells were stained with monoclonal rabbit anti-phospho-EGFr (pT693); polyclonal rabbit anti-phosho-EGFr (s695) and monoclonal rabbit anti-CD71 (TFRC) antibodies. (A) Non specific background staining of EGF receptor phosphorylated on threonine 693 (pT693) was observed in MCF7 cell in contrast to (B) strong positive staining observed A431 cells. (C) Medium staining of EGF receptor phosphorylated on serine 695 (s695) was observed in MCF7 cells in contrast to (D) strong staining observed in A431 cells. Transferrin receptor (red) was found to be negative in both (E) MCF7 and (F) A431 cells. Merged image: nucleus stained with DAPI (blue), EGFr and CD71 (red), β-actin (green). Images were acquired using an Olympus BX61 fluorescence microscope with automated FVII camera. Bar = 200μm x20 magnification.

    Journal: American Journal of Translational Research

    Article Title: An atlas of histone deacetylase expression in breast cancer: fluorescence methodology for comparative semi-quantitative analysis

    doi:

    Figure Lengend Snippet: Distribution epidermal growth factor (EGFr) and transferrin receptors. MCF7 and A431 cells were stained with monoclonal rabbit anti-phospho-EGFr (pT693); polyclonal rabbit anti-phosho-EGFr (s695) and monoclonal rabbit anti-CD71 (TFRC) antibodies. (A) Non specific background staining of EGF receptor phosphorylated on threonine 693 (pT693) was observed in MCF7 cell in contrast to (B) strong positive staining observed A431 cells. (C) Medium staining of EGF receptor phosphorylated on serine 695 (s695) was observed in MCF7 cells in contrast to (D) strong staining observed in A431 cells. Transferrin receptor (red) was found to be negative in both (E) MCF7 and (F) A431 cells. Merged image: nucleus stained with DAPI (blue), EGFr and CD71 (red), β-actin (green). Images were acquired using an Olympus BX61 fluorescence microscope with automated FVII camera. Bar = 200μm x20 magnification.

    Article Snippet: Tissue sections were outlined using a pap pen and blocked for 1 hour in Superblock (Thermo Scientific) followed by an overnight incubation in a humidified chamber with primary antibodies diluted in 1% BSA: polyclonal rabbit anti-HDAC1-11 (K333-11-30; Biovision) at a concentration of 10 μg/ml, monoclonal rabbit anti-HDAC4 (1576-1;Epitomics) diluted 1:500 and monoclonal mouse anti-HDAC8 (H6412; Sigma) diluted (1:500); polyclonal goat anti-beta actin (ab8229; Abcam) diluted to 5 μg/ml; monoclonal rabbit anti-Annexin V (2792-1; Epitomics); monoclonal rabbit anti-phospho-EGFr (pT693) (2343-1; Epitomics); polyclonal rabbit anti-phosho-EGFr (s695) (T3868; Epitomics) and monoclonal rabbit anti-CD71 (TFRC) (2918-1; Epitomics).

    Techniques: Staining, Fluorescence, Microscopy