egfr  (Thermo Fisher)


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    Name:
    EGF Antibody 3 HCLC
    Description:
    EGF Oligoclonal Antibody for ELISA
    Catalog Number:
    710569
    Price:
    None
    Category:
    Antibodies Secondary Detection Reagents
    Applications:
    Cell Analysis|Cellular Imaging|Immunocytochemistry (ICC)|Protein Assays and Analysis|Protein Biology|Western Blotting
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    Structured Review

    Thermo Fisher egfr
    Mechanistic characterization of miR-1254 and <t>CCAR1</t> 5′ UTR in modulating cellular sensitivity to tamoxifen. (A) miR-1254 targets predicted by TargetScan and miRanda with further GO analysis. NCOA1 , NCOA3 , <t>EGFR</t> , ERBB2 and SNAI1 are selected. (B) Relative luciferase activity of wild-type or mutant 3′ UTRs with forced expression of miR-1254. Error bars indicate SEM. *** P
    EGF Oligoclonal Antibody for ELISA
    https://www.bioz.com/result/egfr/product/Thermo Fisher
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    egfr - by Bioz Stars, 2021-05
    93/100 stars

    Images

    1) Product Images from "CCAR1 5′ UTR as a natural miRancer of miR-1254 overrides tamoxifen resistance"

    Article Title: CCAR1 5′ UTR as a natural miRancer of miR-1254 overrides tamoxifen resistance

    Journal: Cell Research

    doi: 10.1038/cr.2016.32

    Mechanistic characterization of miR-1254 and CCAR1 5′ UTR in modulating cellular sensitivity to tamoxifen. (A) miR-1254 targets predicted by TargetScan and miRanda with further GO analysis. NCOA1 , NCOA3 , EGFR , ERBB2 and SNAI1 are selected. (B) Relative luciferase activity of wild-type or mutant 3′ UTRs with forced expression of miR-1254. Error bars indicate SEM. *** P
    Figure Legend Snippet: Mechanistic characterization of miR-1254 and CCAR1 5′ UTR in modulating cellular sensitivity to tamoxifen. (A) miR-1254 targets predicted by TargetScan and miRanda with further GO analysis. NCOA1 , NCOA3 , EGFR , ERBB2 and SNAI1 are selected. (B) Relative luciferase activity of wild-type or mutant 3′ UTRs with forced expression of miR-1254. Error bars indicate SEM. *** P

    Techniques Used: Luciferase, Activity Assay, Mutagenesis, Expressing

    2) Product Images from "Breast Cancer Metastasis Suppressor-1 Differentially Modulates Growth Factor Signaling *Breast Cancer Metastasis Suppressor-1 Differentially Modulates Growth Factor Signaling * S⃞"

    Article Title: Breast Cancer Metastasis Suppressor-1 Differentially Modulates Growth Factor Signaling *Breast Cancer Metastasis Suppressor-1 Differentially Modulates Growth Factor Signaling * S⃞

    Journal:

    doi: 10.1074/jbc.M710068200

    BRMS1 selectively modulates growth factor receptor expression. Receptor expression status for EGFR, PDGFR-β, and HGF receptor (c-Met) were examined by immunoblotting. Receptor expression was examined in multiple clones of BRMS1-expressing MDA-MB-231
    Figure Legend Snippet: BRMS1 selectively modulates growth factor receptor expression. Receptor expression status for EGFR, PDGFR-β, and HGF receptor (c-Met) were examined by immunoblotting. Receptor expression was examined in multiple clones of BRMS1-expressing MDA-MB-231

    Techniques Used: Expressing, Clone Assay, Multiple Displacement Amplification

    BRMS1 transcriptionally regulates EGFR expression. A , EGFR mRNA was measured using real-time quantitative PCR. Relative quantity ( RQ ) from 231/435 cells and three BRMS1-expressing clones is shown for each cell line. Ribosomal S9 was used as internal
    Figure Legend Snippet: BRMS1 transcriptionally regulates EGFR expression. A , EGFR mRNA was measured using real-time quantitative PCR. Relative quantity ( RQ ) from 231/435 cells and three BRMS1-expressing clones is shown for each cell line. Ribosomal S9 was used as internal

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Clone Assay

    3) Product Images from "Identification of Anti-EGFR and Anti-ErbB3 Dual Variable Domains Immunoglobulin (DVD-Ig) Proteins with Unique Activities"

    Article Title: Identification of Anti-EGFR and Anti-ErbB3 Dual Variable Domains Immunoglobulin (DVD-Ig) Proteins with Unique Activities

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0124135

    Anti- EGFR/ErbB3 DVD-Ig protein internalization. (A) A431 and (B) FaDu cells were treated with 10nM pHRodo-labeled anti-EGFR mAb alone, the bsAb, or anti-EGFR/ErbB3 DVD-Ig proteins on ice or at 37°C for 2 hours in PBS. Fluorescence intensity was measured via FACS. The error bars indicate standard deviation from the mean. p value was calculated via student T-test. *p
    Figure Legend Snippet: Anti- EGFR/ErbB3 DVD-Ig protein internalization. (A) A431 and (B) FaDu cells were treated with 10nM pHRodo-labeled anti-EGFR mAb alone, the bsAb, or anti-EGFR/ErbB3 DVD-Ig proteins on ice or at 37°C for 2 hours in PBS. Fluorescence intensity was measured via FACS. The error bars indicate standard deviation from the mean. p value was calculated via student T-test. *p

    Techniques Used: Labeling, Fluorescence, FACS, Standard Deviation

    Anti- EGFR/ErbB3 DVD-Ig proteins induce apoptosis and arrest cell cycle. An apoptosis assay was used to analyze (A) A431 or (B) FaDu cells after DVD-Ig proteins, mAbs, or combination treatment. Apoptotic (Annexin V-positive) cells were quantitated via FACS. A BrdU-incorporation assay was used to analyze (C) A431 or (D) FaDu cells after DVD-Ig proteins, mAbs, or combination treatment. BrdU-positive cells were quantitated via FACS. Three independent experiments with triplicates were performed. The error bars indicate standard deviation from the mean. p value was calculated via student T-test. *p
    Figure Legend Snippet: Anti- EGFR/ErbB3 DVD-Ig proteins induce apoptosis and arrest cell cycle. An apoptosis assay was used to analyze (A) A431 or (B) FaDu cells after DVD-Ig proteins, mAbs, or combination treatment. Apoptotic (Annexin V-positive) cells were quantitated via FACS. A BrdU-incorporation assay was used to analyze (C) A431 or (D) FaDu cells after DVD-Ig proteins, mAbs, or combination treatment. BrdU-positive cells were quantitated via FACS. Three independent experiments with triplicates were performed. The error bars indicate standard deviation from the mean. p value was calculated via student T-test. *p

    Techniques Used: Apoptosis Assay, FACS, BrdU Incorporation Assay, Standard Deviation

    Anti-EGFR/ErbB3 DVD-Ig proteins inhibit cell proliferation. (A) A431, (B) FaDu, (C) LNCaP, and (D) PC3 cells were treated with different dosages of anti-EGFR/ErbB3 DVD-Ig proteins, anti-EGFR/ErbB3 half DVD-Ig proteins anti-EGFR and anti-ErbB3 mAbs alone, anti-EGFR and anti-ErbB3 mAbs in combination, or the bsAb for 10 days. After 10 days, cells were fixed and stained with with Crystal Violet. Cell proliferation was measured with Crystal Violet staining. The error bars indicate standard deviation from the mean.
    Figure Legend Snippet: Anti-EGFR/ErbB3 DVD-Ig proteins inhibit cell proliferation. (A) A431, (B) FaDu, (C) LNCaP, and (D) PC3 cells were treated with different dosages of anti-EGFR/ErbB3 DVD-Ig proteins, anti-EGFR/ErbB3 half DVD-Ig proteins anti-EGFR and anti-ErbB3 mAbs alone, anti-EGFR and anti-ErbB3 mAbs in combination, or the bsAb for 10 days. After 10 days, cells were fixed and stained with with Crystal Violet. Cell proliferation was measured with Crystal Violet staining. The error bars indicate standard deviation from the mean.

    Techniques Used: Staining, Standard Deviation

    Anti- EGFR/ErbB3 DVD-Ig proteins in cell signaling assay. A431 and FaDu cells were cultured in medium containing 3nM HRG and 1% serum were treated with 100nM anti-EGFR and anti-ErbB3 mAbs alone, anti-EGFR and anti-ErbB3 mAbs in combination, the bsAb or anti-EGFR/ErbB3 DVD-Ig proteins for 24 hours. Cells were then harvested and lysed for Western blot. * indicates that 10% of sample lysates were used for A431 cells.
    Figure Legend Snippet: Anti- EGFR/ErbB3 DVD-Ig proteins in cell signaling assay. A431 and FaDu cells were cultured in medium containing 3nM HRG and 1% serum were treated with 100nM anti-EGFR and anti-ErbB3 mAbs alone, anti-EGFR and anti-ErbB3 mAbs in combination, the bsAb or anti-EGFR/ErbB3 DVD-Ig proteins for 24 hours. Cells were then harvested and lysed for Western blot. * indicates that 10% of sample lysates were used for A431 cells.

    Techniques Used: Cell Culture, Western Blot

    DVD-Ig proteins inhibit HRG binding to FaDu cells. Serial dilutions of HRG were incubated with 100 nM anti-EGFR and anti-ErbB3 mAbs alone, anti-EGFR and anti-ErbB3 mAbs in combination, the bsAb, or anti-EGFR/ErbB3 DVD-Ig proteins. HRG binding affinity to FaDu cells was measured via FACS. MFI: median fluorescence intensity. The error bars indicate standard deviation from the mean.
    Figure Legend Snippet: DVD-Ig proteins inhibit HRG binding to FaDu cells. Serial dilutions of HRG were incubated with 100 nM anti-EGFR and anti-ErbB3 mAbs alone, anti-EGFR and anti-ErbB3 mAbs in combination, the bsAb, or anti-EGFR/ErbB3 DVD-Ig proteins. HRG binding affinity to FaDu cells was measured via FACS. MFI: median fluorescence intensity. The error bars indicate standard deviation from the mean.

    Techniques Used: Binding Assay, Incubation, FACS, Fluorescence, Standard Deviation

    Generation of anti-EGFR and anti-ErbB3 DVD-Ig and half DVD-Ig proteins. (A) DVD-Ig molecules were generated by linking the variable domains mAb1 and mAb2, using various orientations of the two variable domains and linkers. (B) Half DVD-Ig molecules were generated with two mutations (C220S and C226S) in the hinge region and four mutations in the C H 3 region (P395A, F405R, Y407R, and K409D).
    Figure Legend Snippet: Generation of anti-EGFR and anti-ErbB3 DVD-Ig and half DVD-Ig proteins. (A) DVD-Ig molecules were generated by linking the variable domains mAb1 and mAb2, using various orientations of the two variable domains and linkers. (B) Half DVD-Ig molecules were generated with two mutations (C220S and C226S) in the hinge region and four mutations in the C H 3 region (P395A, F405R, Y407R, and K409D).

    Techniques Used: Generated

    4) Product Images from "HER2 and EGFR overexpression support metastatic progression of prostate cancer to bone"

    Article Title: HER2 and EGFR overexpression support metastatic progression of prostate cancer to bone

    Journal: Cancer research

    doi: 10.1158/0008-5472.CAN-16-1656

    Analysis of circulating tumor cells (CTCs) from 10 patients with metastatic prostate cancer A , Cluster of white blood cells surrounding a CK+/EGFR+ CTC from patient 3. White blood cells stained positive for CD45. B,C , Other representative images of CK+/EGFR+ CTCs from patients 3 and 5 respectively. D , Clinical history of prostate cancer patients analyzed for circulating tumor cells. E , Number of cytokeratin (CK)+/EGFR+ and CK+/EGFR− CTCs isolated per 1mL whole blood. Numbers above the columns indicate the total number of CTCs isolated from patients 1–10.
    Figure Legend Snippet: Analysis of circulating tumor cells (CTCs) from 10 patients with metastatic prostate cancer A , Cluster of white blood cells surrounding a CK+/EGFR+ CTC from patient 3. White blood cells stained positive for CD45. B,C , Other representative images of CK+/EGFR+ CTCs from patients 3 and 5 respectively. D , Clinical history of prostate cancer patients analyzed for circulating tumor cells. E , Number of cytokeratin (CK)+/EGFR+ and CK+/EGFR− CTCs isolated per 1mL whole blood. Numbers above the columns indicate the total number of CTCs isolated from patients 1–10.

    Techniques Used: Staining, Isolation

    5) Product Images from "Epidermal Growth Factor Receptor-Dependent Regulation of Integrin-Mediated Signaling and Cell Cycle Entry in Epithelial Cells"

    Article Title: Epidermal Growth Factor Receptor-Dependent Regulation of Integrin-Mediated Signaling and Cell Cycle Entry in Epithelial Cells

    Journal: Molecular and Cellular Biology

    doi: 10.1128/MCB.24.19.8586-8599.2004

    EGFR is required for FN-induced signaling events. Cos7 cells were placed in suspension (S), either left untreated or treated with 1 μM AG1478 or 0.5 μM PD168393, and plated on FN for 30 min. (A through F) EGFR (A), Shc (B), Erk (C), Akt (D), Cbl (E), and PLCγ (F) phosphorylation was analyzed by immunoblotting of EGFR, Shc, PLCγ, or Cbl immunoprecipitates with an anti-phosphotyrosine monoclonal antibody (P-Tyr Blot) or by immunoblotting of total-cell extracts with a phosphospecific antibody against Erk (P-Erk Blot) or Akt (P-Akt Blot). Total levels of EGFR, Shc, Erk, Akt, PLCγ, or Cbl in the immunoprecipitates or cell lysates were analyzed by immunoblotting with their respective antibodies (EGFR Blot, Shc Blot, Erk Blot, Akt Blot, PLCγ Blot, and Cbl Blot). (G) Cos7 cells were transfected with 0.2 μg of pSLV-HA-Erk2 and 1 μg of pDEST12.2-dnEGFR (Dn) or 1 μg of vector (Vec). Forty-eight hours later, cells were harvested and either placed in suspension or plated on FN. The level of Erk activation was measured by immunoblotting of HA immunoprecipitates with an anti-P-Erk antibody. Total levels of Erk2 were measured by immunoblotting with an anti-Erk antibody. The level of dnEGFR expressed (Tf Dn) compared to endogenous EGFR expression (En Wt) was measured by immunoblotting cell lysates with an anti-EGFR antibody. (H) CV1 cells were infected with a virus containing an empty pLPCX vector (Vec) or a virus expressing GFP-FRNK. Erk activation in the vector- or GFP-FRNK-expressing cells was monitored in cell lysates with a phosphospecific anti-Erk antibody. Total levels of Erk in the immunoprecipitates were analyzed by immunoblotting with anti-Erk antibodies. Levels of GFP-FRNK expression were monitored by immunoblotting with an anti-FRNK antibody. Levels of endogenous FAK are also shown.
    Figure Legend Snippet: EGFR is required for FN-induced signaling events. Cos7 cells were placed in suspension (S), either left untreated or treated with 1 μM AG1478 or 0.5 μM PD168393, and plated on FN for 30 min. (A through F) EGFR (A), Shc (B), Erk (C), Akt (D), Cbl (E), and PLCγ (F) phosphorylation was analyzed by immunoblotting of EGFR, Shc, PLCγ, or Cbl immunoprecipitates with an anti-phosphotyrosine monoclonal antibody (P-Tyr Blot) or by immunoblotting of total-cell extracts with a phosphospecific antibody against Erk (P-Erk Blot) or Akt (P-Akt Blot). Total levels of EGFR, Shc, Erk, Akt, PLCγ, or Cbl in the immunoprecipitates or cell lysates were analyzed by immunoblotting with their respective antibodies (EGFR Blot, Shc Blot, Erk Blot, Akt Blot, PLCγ Blot, and Cbl Blot). (G) Cos7 cells were transfected with 0.2 μg of pSLV-HA-Erk2 and 1 μg of pDEST12.2-dnEGFR (Dn) or 1 μg of vector (Vec). Forty-eight hours later, cells were harvested and either placed in suspension or plated on FN. The level of Erk activation was measured by immunoblotting of HA immunoprecipitates with an anti-P-Erk antibody. Total levels of Erk2 were measured by immunoblotting with an anti-Erk antibody. The level of dnEGFR expressed (Tf Dn) compared to endogenous EGFR expression (En Wt) was measured by immunoblotting cell lysates with an anti-EGFR antibody. (H) CV1 cells were infected with a virus containing an empty pLPCX vector (Vec) or a virus expressing GFP-FRNK. Erk activation in the vector- or GFP-FRNK-expressing cells was monitored in cell lysates with a phosphospecific anti-Erk antibody. Total levels of Erk in the immunoprecipitates were analyzed by immunoblotting with anti-Erk antibodies. Levels of GFP-FRNK expression were monitored by immunoblotting with an anti-FRNK antibody. Levels of endogenous FAK are also shown.

    Techniques Used: Transfection, Plasmid Preparation, Activation Assay, Expressing, Infection

    EGFR is not required for all FN-induced signaling events. Cos7 cells were placed in suspension (S), either left untreated or treated with 1 μM AG1478 or 0.5 μM PD168393, and plated on FN. (A) Tyrosine phosphorylation of FAK was analyzed by immunoblotting of FAK immunoprecipitates with an anti-phosphotyrosine monoclonal antibody (P-Tyr Blot). Total levels of FAK in the immunoprecipitates were monitored by immunoblotting with an anti-FAK monoclonal antibody (FAK Blot). (B) Src activation was measured by immunoblotting of Src immunoprecipitates with an anti-phospho-Src antibody (Y-416 Blot), and total levels of Src in the immunoprecipitates were analyzed by immunoblotting with the anti-Src monoclonal antibody 327 (Src Blot). (C) Following adhesion, Cos7 cells were fractionated into soluble cytoplasmic (Su) and detergent-soluble pellet (Pe) fractions, and the level of each PKC isoform in each fraction was analyzed by immunoblotting with specific anti-PKC antibodies as indicated (PKC Blots). (D) Tyrosine phosphorylation of PKCδ was analyzed by immunoblotting of PKCδ immunoprecipitates of the cytoplasmic and detergent-soluble fractions (P-Tyr Blot). Total levels of PKCδ in the immunoprecipitates were monitored by immunoblotting with an anti-PKCδ monoclonal antibody (PKCδ Blot). Note that membrane-associated PKCδ migrates more slowly in gels due to phosphorylation. (E) Model depicting the EGFR dependence of a subset of integrin-mediated signaling events, specifically Cbl, PLCγ, Shc, Erk, and Akt. Also shown is the EGFR independence of Src, FAK, and PKC activation. Integrin activation of FAK is dependent on actin polymerization (data not shown).
    Figure Legend Snippet: EGFR is not required for all FN-induced signaling events. Cos7 cells were placed in suspension (S), either left untreated or treated with 1 μM AG1478 or 0.5 μM PD168393, and plated on FN. (A) Tyrosine phosphorylation of FAK was analyzed by immunoblotting of FAK immunoprecipitates with an anti-phosphotyrosine monoclonal antibody (P-Tyr Blot). Total levels of FAK in the immunoprecipitates were monitored by immunoblotting with an anti-FAK monoclonal antibody (FAK Blot). (B) Src activation was measured by immunoblotting of Src immunoprecipitates with an anti-phospho-Src antibody (Y-416 Blot), and total levels of Src in the immunoprecipitates were analyzed by immunoblotting with the anti-Src monoclonal antibody 327 (Src Blot). (C) Following adhesion, Cos7 cells were fractionated into soluble cytoplasmic (Su) and detergent-soluble pellet (Pe) fractions, and the level of each PKC isoform in each fraction was analyzed by immunoblotting with specific anti-PKC antibodies as indicated (PKC Blots). (D) Tyrosine phosphorylation of PKCδ was analyzed by immunoblotting of PKCδ immunoprecipitates of the cytoplasmic and detergent-soluble fractions (P-Tyr Blot). Total levels of PKCδ in the immunoprecipitates were monitored by immunoblotting with an anti-PKCδ monoclonal antibody (PKCδ Blot). Note that membrane-associated PKCδ migrates more slowly in gels due to phosphorylation. (E) Model depicting the EGFR dependence of a subset of integrin-mediated signaling events, specifically Cbl, PLCγ, Shc, Erk, and Akt. Also shown is the EGFR independence of Src, FAK, and PKC activation. Integrin activation of FAK is dependent on actin polymerization (data not shown).

    Techniques Used: Activation Assay

    EGFR and Myc overexpression rescues S phase. (A) CV1 cells were serum starved for 48 h and either left in suspension (S) or plated on FN in the absence (FN) or presence (EGF) of 40 ng of EGF/ml for the indicated times. The levels of cyclin D1 (cycD1), p27, cyclin A (cycA), and Rb phosphorylation at Thr821 (P-Rb T821) were monitored by immunoblotting with the respective antibodies. Total levels of Akt were monitored to control for total protein levels. (B) CV1 cells (CV) were infected with retroviruses expressing EGFR (R1, R5) or cyclin D1 (D1) or with an empty vector (V). Levels of EGFR and cyclin D1 expression were monitored by immunoblotting of whole-cell extracts with their respective antibodies after plating of cells on FN for 12 h. Levels of EGFR activation in virus-infected cells held in suspension or attached to FN were monitored by immunoblotting of EGFR immunoprecipitates with anti-phosphotyrosine antibodies (P-Tyr Blot). Total levels of EGFR were monitored by immunoblotting with an anti-EGFR antibody (EGFR Blot). *, the length of film exposure to enhanced chemiluminescence was 5 times less for EGFR-overexpressing cells than for other samples. (C) Adherent CV1 cells infected with retroviral vectors encoding either EGFR, cyclin D1, or no cDNA (Vector) were serum starved for 48 h and either placed in suspension or plated on FN for the indicated times. Levels of cyclin A and p27 were monitored by immunoblotting cell lysates with their respective antibodies. Rb phosphorylation at Thr821 was monitored by immunoblotting of cell lysates with phosphospecific antibodies. Total levels of Akt were monitored by immunoblotting as a control for total protein levels in the extracts. (D) CV1 cells were serum starved for 48 h and either placed in suspension or plated on FN in the absence or presence of 40 ng of EGF/ml for the indicated times. Adherent CV1 cells infected with retroviral vectors encoding EGFR or no cDNA were serum starved for 48 h and then either placed in suspension or plated on FN for the indicated times. Levels of Myc expression were monitored by immunoblotting of cell lysates with anti-Myc antibodies. Total levels of Akt were monitored by immunoblotting as a control for total protein levels in the extracts. (E) Adherent CV1 cells infected with retroviral vectors encoding either EGFR or no cDNA were serum starved for 48 h and then either placed in suspension or plated on FN for the indicated times. Levels of cyclin D1 were monitored by immunoblotting of cell lysates with anti-cyclin D1 antibodies. Erk and Akt activation was monitored by immunoblotting of cell lysates with phosphospecific antibodies (P-Erk, P-Akt). Total levels of Erk and Akt were monitored by immunoblotting as a control for total protein levels in the extracts (Erk, Akt). (F) CV1 cells were infected with a virus containing an empty vector or expressing MycER. Levels of MycER expression were monitored by immunoblotting with anti-Myc antibodies after plating on FN in the absence (FN) or presence (Tx) of 50 nM tamoxifen. Levels of p27 and cyclin A expression in cells in suspension or at the indicated times after plating on FN in the presence or absence of 50 nM tamoxifen were monitored by immunoblotting. Total levels of Akt were monitored by immunoblotting as a control for total protein levels in the extracts.
    Figure Legend Snippet: EGFR and Myc overexpression rescues S phase. (A) CV1 cells were serum starved for 48 h and either left in suspension (S) or plated on FN in the absence (FN) or presence (EGF) of 40 ng of EGF/ml for the indicated times. The levels of cyclin D1 (cycD1), p27, cyclin A (cycA), and Rb phosphorylation at Thr821 (P-Rb T821) were monitored by immunoblotting with the respective antibodies. Total levels of Akt were monitored to control for total protein levels. (B) CV1 cells (CV) were infected with retroviruses expressing EGFR (R1, R5) or cyclin D1 (D1) or with an empty vector (V). Levels of EGFR and cyclin D1 expression were monitored by immunoblotting of whole-cell extracts with their respective antibodies after plating of cells on FN for 12 h. Levels of EGFR activation in virus-infected cells held in suspension or attached to FN were monitored by immunoblotting of EGFR immunoprecipitates with anti-phosphotyrosine antibodies (P-Tyr Blot). Total levels of EGFR were monitored by immunoblotting with an anti-EGFR antibody (EGFR Blot). *, the length of film exposure to enhanced chemiluminescence was 5 times less for EGFR-overexpressing cells than for other samples. (C) Adherent CV1 cells infected with retroviral vectors encoding either EGFR, cyclin D1, or no cDNA (Vector) were serum starved for 48 h and either placed in suspension or plated on FN for the indicated times. Levels of cyclin A and p27 were monitored by immunoblotting cell lysates with their respective antibodies. Rb phosphorylation at Thr821 was monitored by immunoblotting of cell lysates with phosphospecific antibodies. Total levels of Akt were monitored by immunoblotting as a control for total protein levels in the extracts. (D) CV1 cells were serum starved for 48 h and either placed in suspension or plated on FN in the absence or presence of 40 ng of EGF/ml for the indicated times. Adherent CV1 cells infected with retroviral vectors encoding EGFR or no cDNA were serum starved for 48 h and then either placed in suspension or plated on FN for the indicated times. Levels of Myc expression were monitored by immunoblotting of cell lysates with anti-Myc antibodies. Total levels of Akt were monitored by immunoblotting as a control for total protein levels in the extracts. (E) Adherent CV1 cells infected with retroviral vectors encoding either EGFR or no cDNA were serum starved for 48 h and then either placed in suspension or plated on FN for the indicated times. Levels of cyclin D1 were monitored by immunoblotting of cell lysates with anti-cyclin D1 antibodies. Erk and Akt activation was monitored by immunoblotting of cell lysates with phosphospecific antibodies (P-Erk, P-Akt). Total levels of Erk and Akt were monitored by immunoblotting as a control for total protein levels in the extracts (Erk, Akt). (F) CV1 cells were infected with a virus containing an empty vector or expressing MycER. Levels of MycER expression were monitored by immunoblotting with anti-Myc antibodies after plating on FN in the absence (FN) or presence (Tx) of 50 nM tamoxifen. Levels of p27 and cyclin A expression in cells in suspension or at the indicated times after plating on FN in the presence or absence of 50 nM tamoxifen were monitored by immunoblotting. Total levels of Akt were monitored by immunoblotting as a control for total protein levels in the extracts.

    Techniques Used: Over Expression, Infection, Expressing, Plasmid Preparation, Activation Assay

    6) Product Images from "18F-fludrodeoxyglucose maximal standardized uptake value and metabolic tumor burden are associated with major chemotherapy-related tumor markers in NSCLC patients"

    Article Title: 18F-fludrodeoxyglucose maximal standardized uptake value and metabolic tumor burden are associated with major chemotherapy-related tumor markers in NSCLC patients

    Journal: OncoTargets and therapy

    doi: 10.2147/OTT.S113832

    Correlationship analysis among the parameters. Notes: ( A ) SUV max was significantly correlated with p53 IHC score ( R =0.473, P =0.001); ( B ) MTV was significantly correlated with ERCC1 IHC score ( R =0.667, P =0.000); ( C ) TLG was significantly correlated with ERCC1 IHC score ( R =0.712, P =0.000). Abbreviations: EGFR, epidermal growth factor receptor; ERCC1, excision repair cross-complementing group 1 protein; IHC, immunohistochemistry; MTV, metabolic tumor volume; SUV max , maximum standardized uptake value; TLG, total lesion glycolysis.
    Figure Legend Snippet: Correlationship analysis among the parameters. Notes: ( A ) SUV max was significantly correlated with p53 IHC score ( R =0.473, P =0.001); ( B ) MTV was significantly correlated with ERCC1 IHC score ( R =0.667, P =0.000); ( C ) TLG was significantly correlated with ERCC1 IHC score ( R =0.712, P =0.000). Abbreviations: EGFR, epidermal growth factor receptor; ERCC1, excision repair cross-complementing group 1 protein; IHC, immunohistochemistry; MTV, metabolic tumor volume; SUV max , maximum standardized uptake value; TLG, total lesion glycolysis.

    Techniques Used: Immunohistochemistry

    Representative images of immunohistochemistry. Notes: ( A ) EGFR, ( B ) p53, and ( C ) ERCC1; (magnification, ×400). Abbreviations: EGFR, epidermal growth factor receptor; ERCC1, excision repair cross-complementing group 1 protein.
    Figure Legend Snippet: Representative images of immunohistochemistry. Notes: ( A ) EGFR, ( B ) p53, and ( C ) ERCC1; (magnification, ×400). Abbreviations: EGFR, epidermal growth factor receptor; ERCC1, excision repair cross-complementing group 1 protein.

    Techniques Used: Immunohistochemistry

    The ROC curve. Notes: ( A ) ROC curve for the optimal cutoff value of SUV max suggesting p53-positive NSCLC. Area under the curve: 0.737; 95% CI: 0.592–0.881; P =0.006. A SUV max value of 7.68 or higher suggests a NSCLC to be p53 positive with a sensitivity of 91% and specificity of 50%; ( B ) ROC curve for the optimal cutoff value of MTV suggesting ERCC1-positive NSCLC. Area under the curve: 0.825; 95% CI: 0.705–0.945; P =0.000. A MTV value of 23.62 cm 3 or lower suggests NSCLC to be ERCC1 positive with a sensitivity of 83% and specificity of 69%; ( C ) ROC curve for the optimal cutoff value of TLG suggesting ERCC1-positive NSCLC. Area under the curve: 0.835; 95% CI: 0.714–0.956; P =0.000. A TLG value of 129.65 or lower suggests a NSCLC to be p53 positive, with a sensitivity of 80% and specificity of 75%. Abbreviations: CI, confidence interval; EGFR, epidermal growth factor receptor; ERCC1, excision repair cross-complementing group 1 protein; MTV, metabolic tumor volume; NSCLC, non-small cell lung cancer; ROC, receiver operating characteristics; SUV max , maximum standardized uptake value; TLG, total lesion glycolysis.
    Figure Legend Snippet: The ROC curve. Notes: ( A ) ROC curve for the optimal cutoff value of SUV max suggesting p53-positive NSCLC. Area under the curve: 0.737; 95% CI: 0.592–0.881; P =0.006. A SUV max value of 7.68 or higher suggests a NSCLC to be p53 positive with a sensitivity of 91% and specificity of 50%; ( B ) ROC curve for the optimal cutoff value of MTV suggesting ERCC1-positive NSCLC. Area under the curve: 0.825; 95% CI: 0.705–0.945; P =0.000. A MTV value of 23.62 cm 3 or lower suggests NSCLC to be ERCC1 positive with a sensitivity of 83% and specificity of 69%; ( C ) ROC curve for the optimal cutoff value of TLG suggesting ERCC1-positive NSCLC. Area under the curve: 0.835; 95% CI: 0.714–0.956; P =0.000. A TLG value of 129.65 or lower suggests a NSCLC to be p53 positive, with a sensitivity of 80% and specificity of 75%. Abbreviations: CI, confidence interval; EGFR, epidermal growth factor receptor; ERCC1, excision repair cross-complementing group 1 protein; MTV, metabolic tumor volume; NSCLC, non-small cell lung cancer; ROC, receiver operating characteristics; SUV max , maximum standardized uptake value; TLG, total lesion glycolysis.

    Techniques Used:

    Expressions of SUV max , MTV, and TLG and three different biomarkers. Notes: The differences of SUV max ( A ), MTV ( B ), and TLG ( C ) in the expressions of EGFR, p53, and ERCC1 among NSCLC patients. * P
    Figure Legend Snippet: Expressions of SUV max , MTV, and TLG and three different biomarkers. Notes: The differences of SUV max ( A ), MTV ( B ), and TLG ( C ) in the expressions of EGFR, p53, and ERCC1 among NSCLC patients. * P

    Techniques Used:

    7) Product Images from "Proteomics identifies EGF‐like domain multiple 7 as a potential therapeutic target for epidermal growth factor receptor‐positive glioma, et al. Proteomics identifies EGF‐like domain multiple 7 as a potential therapeutic target for epidermal growth factor receptor‐positive glioma"

    Article Title: Proteomics identifies EGF‐like domain multiple 7 as a potential therapeutic target for epidermal growth factor receptor‐positive glioma, et al. Proteomics identifies EGF‐like domain multiple 7 as a potential therapeutic target for epidermal growth factor receptor‐positive glioma

    Journal: Cancer Communications

    doi: 10.1002/cac2.12092

    EGFL7 knock down suppresses the proliferation of glioma cells by inhibiting the phosphorylation of members of the EGFR pathway. (A) Bioluminescence image of the representative mice in the three groups at day 14 after intracranial injection of tumor cells. (B) Tumor volumes in mice with or without selumetinib treatment were measured using the relative intensity of fluorescence. Data represent the mean ± SD of three independent experiments. (C) Overall survival of mice was calculated using Kaplan‐Meier survival curves. A log‐rank test was used to assess the differences. (D) The representative IHC images of U87 glioma in mice. KI67 (brown) is located in the nucleus, and hematoxylin (purple) staining shows the nucleus. U87‐MG cells show a higher KI67 positive rate than U87‐EGFL7kd and selumetinib‐treated U87‐MG cells. (E) Correlations of EGFL7 with p‐ERK and p‐PKM2. EGFR, epidermal growth factor receptor; EGFL7, EGF‐like domain multiple 7; ERK, extracellular regulated protein kinases; PKM2, pyruvate kinase isozyme M2; IHC, immunohistochemistry; KI67, marker of proliferation Ki‐67
    Figure Legend Snippet: EGFL7 knock down suppresses the proliferation of glioma cells by inhibiting the phosphorylation of members of the EGFR pathway. (A) Bioluminescence image of the representative mice in the three groups at day 14 after intracranial injection of tumor cells. (B) Tumor volumes in mice with or without selumetinib treatment were measured using the relative intensity of fluorescence. Data represent the mean ± SD of three independent experiments. (C) Overall survival of mice was calculated using Kaplan‐Meier survival curves. A log‐rank test was used to assess the differences. (D) The representative IHC images of U87 glioma in mice. KI67 (brown) is located in the nucleus, and hematoxylin (purple) staining shows the nucleus. U87‐MG cells show a higher KI67 positive rate than U87‐EGFL7kd and selumetinib‐treated U87‐MG cells. (E) Correlations of EGFL7 with p‐ERK and p‐PKM2. EGFR, epidermal growth factor receptor; EGFL7, EGF‐like domain multiple 7; ERK, extracellular regulated protein kinases; PKM2, pyruvate kinase isozyme M2; IHC, immunohistochemistry; KI67, marker of proliferation Ki‐67

    Techniques Used: Mouse Assay, Injection, Fluorescence, Immunohistochemistry, Staining, Marker

    The high‐level expression of EGFL7 is associated with poor prognosis and promotes growth of glioma. (A) Kaplan‐Meier overall survival curves of glioma patients from different datasets. The dashed lines indicate the median overall survival of patients in different groups. The median expression values were used as a cut‐off. P values were calculated using paired two‐sided moderated Student's t test. (B) EGFL7 expression levels and subcellular location in U87‐MG and U251‐MG cells are demonstrated using a confocal microscopy (800 ×). The medium intensity red signals in the cytoplasm indicate EGFL7 expression levels, and the strong blue oval signals indicate the location of EGFL7 in the nucleus. (C) Relative proliferation rates of U87‐MG and U251‐MG cells after knocking down EGFL7 were measured using CCK‐8 assays. All data are represented as the mean ± SEM. (D) Dose‐response curves of U87‐MG and U251‐MG cells to selumetinib treatment, with an endpoint measurement at 72 h (mean ± SEM of 3 biological repeats). EGFR, epidermal growth factor receptor; EGFL7, EGF‐like domain multiple 7; DAPI, 4',6‐diamidino‐2‐phenylindole; CGGA, Chinese Glioma Genome Atlas; TCGA, The Cancer Genome Atlas; IC 50 , half‐maximal inhibitory concentration; CCK‐8, cell counting kit‐8; SEM, standard error of mean
    Figure Legend Snippet: The high‐level expression of EGFL7 is associated with poor prognosis and promotes growth of glioma. (A) Kaplan‐Meier overall survival curves of glioma patients from different datasets. The dashed lines indicate the median overall survival of patients in different groups. The median expression values were used as a cut‐off. P values were calculated using paired two‐sided moderated Student's t test. (B) EGFL7 expression levels and subcellular location in U87‐MG and U251‐MG cells are demonstrated using a confocal microscopy (800 ×). The medium intensity red signals in the cytoplasm indicate EGFL7 expression levels, and the strong blue oval signals indicate the location of EGFL7 in the nucleus. (C) Relative proliferation rates of U87‐MG and U251‐MG cells after knocking down EGFL7 were measured using CCK‐8 assays. All data are represented as the mean ± SEM. (D) Dose‐response curves of U87‐MG and U251‐MG cells to selumetinib treatment, with an endpoint measurement at 72 h (mean ± SEM of 3 biological repeats). EGFR, epidermal growth factor receptor; EGFL7, EGF‐like domain multiple 7; DAPI, 4',6‐diamidino‐2‐phenylindole; CGGA, Chinese Glioma Genome Atlas; TCGA, The Cancer Genome Atlas; IC 50 , half‐maximal inhibitory concentration; CCK‐8, cell counting kit‐8; SEM, standard error of mean

    Techniques Used: Expressing, Confocal Microscopy, CCK-8 Assay, Concentration Assay, Cell Counting

    8) Product Images from "Analysis of Predictive Biomarkers in Patients With Lung Adenocarcinoma From Southern Brazil Reveals a Distinct Profile From Other Regions of the Country"

    Article Title: Analysis of Predictive Biomarkers in Patients With Lung Adenocarcinoma From Southern Brazil Reveals a Distinct Profile From Other Regions of the Country

    Journal: Journal of Global Oncology

    doi: 10.1200/JGO.19.00174

    Frequency of somatic mutations in EGFR, KRAS , and BRAF in lung adenocarcinoma tumors from patients in southern Brazil. (A) Female and male patients, (B) only female patients, and (C) only male patients. (*) Not detected using our next-generation sequencing panel. It does not exclude the presence of alterations in other driver genes.
    Figure Legend Snippet: Frequency of somatic mutations in EGFR, KRAS , and BRAF in lung adenocarcinoma tumors from patients in southern Brazil. (A) Female and male patients, (B) only female patients, and (C) only male patients. (*) Not detected using our next-generation sequencing panel. It does not exclude the presence of alterations in other driver genes.

    Techniques Used: Next-Generation Sequencing

    9) Product Images from "Estrogen Signaling via a Linear Pathway Involving Insulin-Like Growth Factor I Receptor, Matrix Metalloproteinases, and Epidermal Growth Factor Receptor to Activate Mitogen-Activated Protein Kinase in MCF-7 Breast Cancer Cells"

    Article Title: Estrogen Signaling via a Linear Pathway Involving Insulin-Like Growth Factor I Receptor, Matrix Metalloproteinases, and Epidermal Growth Factor Receptor to Activate Mitogen-Activated Protein Kinase in MCF-7 Breast Cancer Cells

    Journal:

    doi: 10.1210/en.2007-0240

    IGF-IR, EGFR, and HB-EGF involvement in E2-induced MAPK activation. A, Knockdown or blockade of IGF-IR and EGFR on E2-induced MAPK activation. MCF-7 cells were transiently transfected with nonspecific scrambled siRNA (−) or siRNA against IGF-IR
    Figure Legend Snippet: IGF-IR, EGFR, and HB-EGF involvement in E2-induced MAPK activation. A, Knockdown or blockade of IGF-IR and EGFR on E2-induced MAPK activation. MCF-7 cells were transiently transfected with nonspecific scrambled siRNA (−) or siRNA against IGF-IR

    Techniques Used: Activation Assay, Transfection

    E2 activated both IGF-IR and EGFR in MCF-7 cells. A, Levels of IGF-IR and EGFR expression in MCF-7 cells. Both MCF-7 and MDA-MB-231 cells were extracted from cells at 80% confluence and processed for assessment of IGF-IR andEGFRexpression using Western
    Figure Legend Snippet: E2 activated both IGF-IR and EGFR in MCF-7 cells. A, Levels of IGF-IR and EGFR expression in MCF-7 cells. Both MCF-7 and MDA-MB-231 cells were extracted from cells at 80% confluence and processed for assessment of IGF-IR andEGFRexpression using Western

    Techniques Used: Expressing, Multiple Displacement Amplification, Western Blot

    Linear activation of IGF-IR and EGFR is involved in E2-induced cell growth and cell death protection. A and B, Knockdown or blockade of IGF-IR and EGFR on ligand-induced cell growth. Cells were transiently transfected with nonspecific scrambled siRNA
    Figure Legend Snippet: Linear activation of IGF-IR and EGFR is involved in E2-induced cell growth and cell death protection. A and B, Knockdown or blockade of IGF-IR and EGFR on ligand-induced cell growth. Cells were transiently transfected with nonspecific scrambled siRNA

    Techniques Used: Activation Assay, Transfection

    E2-induced EGFR activation involves IGF-IR and MMP. A and B, E2-induced EGFR phosphorylation is dependent on both IGF-IR and MMP. Cells were pretreated with 1 µ m AG1024 and 10 µ m MMP2/9 inhibitor for 30 min (A) or transiently transfected
    Figure Legend Snippet: E2-induced EGFR activation involves IGF-IR and MMP. A and B, E2-induced EGFR phosphorylation is dependent on both IGF-IR and MMP. Cells were pretreated with 1 µ m AG1024 and 10 µ m MMP2/9 inhibitor for 30 min (A) or transiently transfected

    Techniques Used: Activation Assay, Transfection

    IGF-IR is an upstream molecule of EGFR. A, IGF-I increased the phosphorylation status of the EGFR. Quiescent MCF-7 cells were treated with vehicle, IGF-I, or EGF at doses indicated for 5 min. Lysates were immunoprecipitated with anti-EGFR antibodies.
    Figure Legend Snippet: IGF-IR is an upstream molecule of EGFR. A, IGF-I increased the phosphorylation status of the EGFR. Quiescent MCF-7 cells were treated with vehicle, IGF-I, or EGF at doses indicated for 5 min. Lysates were immunoprecipitated with anti-EGFR antibodies.

    Techniques Used: Immunoprecipitation

    IGF-IR is an upstream molecule on EGFR-dependent MAPK activation. A, Effect of AG1478 and MMP2/9 inhibitor on IGF-I-induced MAPK activation in MCF-7 variants. Three variants of MCF-7 cells were pretreated with MMP2/9 inhibitor or AG1478 for 30 min and
    Figure Legend Snippet: IGF-IR is an upstream molecule on EGFR-dependent MAPK activation. A, Effect of AG1478 and MMP2/9 inhibitor on IGF-I-induced MAPK activation in MCF-7 variants. Three variants of MCF-7 cells were pretreated with MMP2/9 inhibitor or AG1478 for 30 min and

    Techniques Used: Activation Assay

    10) Product Images from "Activation of EGFR-DNA-PKcs pathway by IGFBP2 protects esophageal adenocarcinoma cells from acidic bile salts-induced DNA damage"

    Article Title: Activation of EGFR-DNA-PKcs pathway by IGFBP2 protects esophageal adenocarcinoma cells from acidic bile salts-induced DNA damage

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    doi: 10.1186/s13046-018-1021-y

    IGFBP2 is required for acidic bile salts-induced EGFR nuclear accumulation to activate DNA-PKcs in EAC cells. a , FLO1 cells were treated with acidic bile salts (ABS, pH 4, 200 μM) for 20 min and recovered for 0.5 h and 3 h. Cytoplasmic and nuclear fractions were analyzed using western blot analysis. Data shows that ABS induces IGFBP2 nuclear translocation as well as accumulation of p-EGFR. b , FLO1 cells with IGFBP2 knockdown (si-IGFBP2) and control cells were treated with ABS for 20 min and recovered for 0.5 h. Cytoplasmic and nuclear fractions were analyzed by using western blot analysis. Data displays attenuated nuclear accumulation of IGFBP2, p-EGFR, and p-DNA-PKcs, following knockdown of IGFBP2 and ABS treatment. c , FLO1 cells with IGFBP2 knockdown and control cells were treated with ABS for 20 min and recovered for 0.5 h. Immunofluorescence staining for IGFBP2 (red) and EGFR (green) was performed. DAPI (blue) was used to stain the nuclei. d , FLO1 cells were treated with EGFR tyrosine kinase inhibitor, gefitinib (10 μM) for 24 h. Then cells were exposed to ABS for 20 min and recovered for 0.5 h. Cytoplasmic and nuclear fractions were analyzed by using western blotting. e , OE33 cells with IGFBP2 overexpression were treated with and without EGFR tyrosine kinase inhibitor, gefitinib (10 μM) for 24 h. Then cells were treated with ABS for 20 min and recovered for 3 h. Cytoplasmic and nuclear fractions were analyzed by using western blotting
    Figure Legend Snippet: IGFBP2 is required for acidic bile salts-induced EGFR nuclear accumulation to activate DNA-PKcs in EAC cells. a , FLO1 cells were treated with acidic bile salts (ABS, pH 4, 200 μM) for 20 min and recovered for 0.5 h and 3 h. Cytoplasmic and nuclear fractions were analyzed using western blot analysis. Data shows that ABS induces IGFBP2 nuclear translocation as well as accumulation of p-EGFR. b , FLO1 cells with IGFBP2 knockdown (si-IGFBP2) and control cells were treated with ABS for 20 min and recovered for 0.5 h. Cytoplasmic and nuclear fractions were analyzed by using western blot analysis. Data displays attenuated nuclear accumulation of IGFBP2, p-EGFR, and p-DNA-PKcs, following knockdown of IGFBP2 and ABS treatment. c , FLO1 cells with IGFBP2 knockdown and control cells were treated with ABS for 20 min and recovered for 0.5 h. Immunofluorescence staining for IGFBP2 (red) and EGFR (green) was performed. DAPI (blue) was used to stain the nuclei. d , FLO1 cells were treated with EGFR tyrosine kinase inhibitor, gefitinib (10 μM) for 24 h. Then cells were exposed to ABS for 20 min and recovered for 0.5 h. Cytoplasmic and nuclear fractions were analyzed by using western blotting. e , OE33 cells with IGFBP2 overexpression were treated with and without EGFR tyrosine kinase inhibitor, gefitinib (10 μM) for 24 h. Then cells were treated with ABS for 20 min and recovered for 3 h. Cytoplasmic and nuclear fractions were analyzed by using western blotting

    Techniques Used: Western Blot, Translocation Assay, Immunofluorescence, Staining, Over Expression

    IGFBP2 forms a complex with EGFR and DNA-PKcs in the EAC cells in response to acidic bile salts. a (FLO1) and b (OE33) cells were treated with acidic bile salts (ABS, pH 4, 200 μM) for 20 min and then recovered for 0.5 h. Co-immunoprecipitation was performed using antibodies against EGFR, DNA-PKcs, and IGFBP2. Westering blot analysis was used to detect the indicated proteins. DNA-PKcs was not detected in IGFBP2 immunoprecipitation blots, possibly due to the large size of DNA-PKcs protein (450 kDa) that cannot be efficiently pulled down by the relatively small IGFBP2 (35 kDa). c , FLO1 cells with IGFBP2 knockdown (si-IGFBP2) and control cells were treated with ABS for 20 min and then recovered for 0.5 h. Co-immunoprecipitation was performed using an antibody against EGFR. Westering blot analysis was used to detect the indicated proteins. IgG was used as the negative control. UT, untreated with ABS
    Figure Legend Snippet: IGFBP2 forms a complex with EGFR and DNA-PKcs in the EAC cells in response to acidic bile salts. a (FLO1) and b (OE33) cells were treated with acidic bile salts (ABS, pH 4, 200 μM) for 20 min and then recovered for 0.5 h. Co-immunoprecipitation was performed using antibodies against EGFR, DNA-PKcs, and IGFBP2. Westering blot analysis was used to detect the indicated proteins. DNA-PKcs was not detected in IGFBP2 immunoprecipitation blots, possibly due to the large size of DNA-PKcs protein (450 kDa) that cannot be efficiently pulled down by the relatively small IGFBP2 (35 kDa). c , FLO1 cells with IGFBP2 knockdown (si-IGFBP2) and control cells were treated with ABS for 20 min and then recovered for 0.5 h. Co-immunoprecipitation was performed using an antibody against EGFR. Westering blot analysis was used to detect the indicated proteins. IgG was used as the negative control. UT, untreated with ABS

    Techniques Used: Immunoprecipitation, Negative Control

    IGFBP2 is required for EGFR stabilization in FLO1 cells after acidic bile salts treatment. a , FLO1 cells with IGFBP2 knockdown (si-IGFBP2) and control cells (si-control) were treated with or without acidic bile salts (ABS, pH 4, 200 μM) and then recovered in full medium with cycloheximide (CHX, 50 μg/ml) for the indicated time points. Whole cell lysates were used for western blot analysis to determine the half-life time change of EGFR. b , Quantification of relative EGFR protein amounts at different time points (EGFR/β-actin). *** p
    Figure Legend Snippet: IGFBP2 is required for EGFR stabilization in FLO1 cells after acidic bile salts treatment. a , FLO1 cells with IGFBP2 knockdown (si-IGFBP2) and control cells (si-control) were treated with or without acidic bile salts (ABS, pH 4, 200 μM) and then recovered in full medium with cycloheximide (CHX, 50 μg/ml) for the indicated time points. Whole cell lysates were used for western blot analysis to determine the half-life time change of EGFR. b , Quantification of relative EGFR protein amounts at different time points (EGFR/β-actin). *** p

    Techniques Used: Western Blot

    IGFBP2 is required for acidic bile salts-induced EGFR and DNA-PKcs activation in EAC cells. a , FLO1 cells with IGFBP2 knockdown (si-IGFBP2) and control cells were treated with acidic bile salts (ABS, pH 4, 200 μM) for 20 min and then recovered for 0.5 h. Whole cell lysates were applied in western blot analysis to detect p-EGFR (Tyr1068) and p-DNA-PKcs (Thr2609). b , OE33 cells with IGFBP2 overexpressing and control cells were treated with ABS for 20 min and then recovered for 0.5 h. Whole cell lysates were used for western blot analysis to detect p-EGFR (Tyr1068) and p-DNA-PKcs (Thr2609). c and d , FLO1 cells with IGFBP2 knockdown and control cells were treated with ABS for 20 min and then recovered for 0.5 h. Immunofluorescence staining for p-DNA-PKcs (Thr2609) was performed. Quantification of positive p-DNA-PKcs cells was performed using image J and presented as a percentage of positive cells ( d ). *** p
    Figure Legend Snippet: IGFBP2 is required for acidic bile salts-induced EGFR and DNA-PKcs activation in EAC cells. a , FLO1 cells with IGFBP2 knockdown (si-IGFBP2) and control cells were treated with acidic bile salts (ABS, pH 4, 200 μM) for 20 min and then recovered for 0.5 h. Whole cell lysates were applied in western blot analysis to detect p-EGFR (Tyr1068) and p-DNA-PKcs (Thr2609). b , OE33 cells with IGFBP2 overexpressing and control cells were treated with ABS for 20 min and then recovered for 0.5 h. Whole cell lysates were used for western blot analysis to detect p-EGFR (Tyr1068) and p-DNA-PKcs (Thr2609). c and d , FLO1 cells with IGFBP2 knockdown and control cells were treated with ABS for 20 min and then recovered for 0.5 h. Immunofluorescence staining for p-DNA-PKcs (Thr2609) was performed. Quantification of positive p-DNA-PKcs cells was performed using image J and presented as a percentage of positive cells ( d ). *** p

    Techniques Used: Activation Assay, Western Blot, Immunofluorescence, Staining

    11) Product Images from "Pregnancy-upregulated nonubiquitous calmodulin kinase induces ligand-independent EGFR degradation"

    Article Title: Pregnancy-upregulated nonubiquitous calmodulin kinase induces ligand-independent EGFR degradation

    Journal:

    doi: 10.1152/ajpcell.00449.2007

    Upregulation of unliganded EGFR by small interfering (si)RNA-mediated knockdown of endogenous human Pnck in SK-BR-3 cells. A : upregulation of endogenous EGFR by Pnck siRNA. Subconfluent SK-BR-3 breast cancer cells were transfected with either control
    Figure Legend Snippet: Upregulation of unliganded EGFR by small interfering (si)RNA-mediated knockdown of endogenous human Pnck in SK-BR-3 cells. A : upregulation of endogenous EGFR by Pnck siRNA. Subconfluent SK-BR-3 breast cancer cells were transfected with either control

    Techniques Used: Transfection

    Ligand-independent EGFR downregulation by Pnck occurs by protea-lysosomal degradation, independent of EGFR tyrosine kinase activity. A : ligand-independent EGFR downregulation does not occur by transcriptional downregulation of the EGFR gene. Two sets
    Figure Legend Snippet: Ligand-independent EGFR downregulation by Pnck occurs by protea-lysosomal degradation, independent of EGFR tyrosine kinase activity. A : ligand-independent EGFR downregulation does not occur by transcriptional downregulation of the EGFR gene. Two sets

    Techniques Used: Activity Assay

    Ligand-independent EGFR downregulation by Pnck and dissection of MAP kinase signaling in Pnck-expressing HEK-293 cells. A : EGFR undergoes ligand-independent downregulation in HA-Pnck-expressing stable HEK-293 cells. Three dishes each of Neo and HA-Pnck
    Figure Legend Snippet: Ligand-independent EGFR downregulation by Pnck and dissection of MAP kinase signaling in Pnck-expressing HEK-293 cells. A : EGFR undergoes ligand-independent downregulation in HA-Pnck-expressing stable HEK-293 cells. Three dishes each of Neo and HA-Pnck

    Techniques Used: Dissection, Expressing

    Inhibition of total tyrosine, EGFR, and Shc tyrosine phosphorylation by Pnck. A : inhibition of EGF-induced tyrosine phosphorylation in HA-Pnck expressing HEK-293 cells ( lanes 1 – 6 ). Neo ( lanes 1 – 3 ) and HA-Pnck HEK-293 ( lanes 4 –
    Figure Legend Snippet: Inhibition of total tyrosine, EGFR, and Shc tyrosine phosphorylation by Pnck. A : inhibition of EGF-induced tyrosine phosphorylation in HA-Pnck expressing HEK-293 cells ( lanes 1 – 6 ). Neo ( lanes 1 – 3 ) and HA-Pnck HEK-293 ( lanes 4 –

    Techniques Used: Inhibition, Expressing

    Related Articles

    Immunostaining:

    Article Title: Time-gated FRET nanoassemblies for rapid and sensitive intra- and extracellular fluorescence imaging
    Article Snippet: .. Extracellular Tb-to-QD FRET using immunostaining To demonstrate the feasibility of extracellular Tb-to-QD FRET biosensing by immunostaining with different kinds of antibodies, we used cetuximab and matuzumab antibodies and EgA1 and EgB4 single-domain VH H (variable domain of heavy chain) antibodies (nanobodies) that recognize different epitopes of EGFR ( , ). eBioscience eFluor 650NC QDs emitting at 650 nm (QD650) were surface-functionalized with cetuximab and EgB4, and ultraviolet-visible (UV-Vis) absorption spectroscopy revealed that the average degrees of labeling (DOLs) were approximately 6.8 cetuximab per QD650 and 18.1 EgB4 per QD650. ..

    Spectroscopy:

    Article Title: Time-gated FRET nanoassemblies for rapid and sensitive intra- and extracellular fluorescence imaging
    Article Snippet: .. Extracellular Tb-to-QD FRET using immunostaining To demonstrate the feasibility of extracellular Tb-to-QD FRET biosensing by immunostaining with different kinds of antibodies, we used cetuximab and matuzumab antibodies and EgA1 and EgB4 single-domain VH H (variable domain of heavy chain) antibodies (nanobodies) that recognize different epitopes of EGFR ( , ). eBioscience eFluor 650NC QDs emitting at 650 nm (QD650) were surface-functionalized with cetuximab and EgB4, and ultraviolet-visible (UV-Vis) absorption spectroscopy revealed that the average degrees of labeling (DOLs) were approximately 6.8 cetuximab per QD650 and 18.1 EgB4 per QD650. ..

    Labeling:

    Article Title: Time-gated FRET nanoassemblies for rapid and sensitive intra- and extracellular fluorescence imaging
    Article Snippet: .. Extracellular Tb-to-QD FRET using immunostaining To demonstrate the feasibility of extracellular Tb-to-QD FRET biosensing by immunostaining with different kinds of antibodies, we used cetuximab and matuzumab antibodies and EgA1 and EgB4 single-domain VH H (variable domain of heavy chain) antibodies (nanobodies) that recognize different epitopes of EGFR ( , ). eBioscience eFluor 650NC QDs emitting at 650 nm (QD650) were surface-functionalized with cetuximab and EgB4, and ultraviolet-visible (UV-Vis) absorption spectroscopy revealed that the average degrees of labeling (DOLs) were approximately 6.8 cetuximab per QD650 and 18.1 EgB4 per QD650. ..

    Formalin-fixed Paraffin-Embedded:

    Article Title: Appropriateness of Using Patient-Derived Xenograft Models for Pharmacologic Evaluation of Novel Therapies for Esophageal/Gastro-Esophageal Junction Cancers
    Article Snippet: .. FFPE tissue sections were stained with antibodies against p53 (clone DO-7, Vector Laboratories, Burlington,Canada, dilution:1:250), p16INK4a (mtm laboratories AG, Heidelberg,Germany; not- diluted), Ki-67 (Clone SP6, NEOmarkers, Rockford,USA, dilution:1:500), EGFR (Clone 31G7, Zymed, San Fransisco,USA, dilution:1:100), Her-2/neu (clone A0485, Dako, Burlington,Canada, dilution:1:25), HIF-1α (clone 54, BD Biosciences, Franklin Lakes,USA, dilution:1:50) and CD31 (clone PECAM1, Santa Cruz,USA, dilution:1:1000). .. A staining index was used to evaluate CD31 and HIF-1α expression using Aperio ImageScope viewer.

    Staining:

    Article Title: Appropriateness of Using Patient-Derived Xenograft Models for Pharmacologic Evaluation of Novel Therapies for Esophageal/Gastro-Esophageal Junction Cancers
    Article Snippet: .. FFPE tissue sections were stained with antibodies against p53 (clone DO-7, Vector Laboratories, Burlington,Canada, dilution:1:250), p16INK4a (mtm laboratories AG, Heidelberg,Germany; not- diluted), Ki-67 (Clone SP6, NEOmarkers, Rockford,USA, dilution:1:500), EGFR (Clone 31G7, Zymed, San Fransisco,USA, dilution:1:100), Her-2/neu (clone A0485, Dako, Burlington,Canada, dilution:1:25), HIF-1α (clone 54, BD Biosciences, Franklin Lakes,USA, dilution:1:50) and CD31 (clone PECAM1, Santa Cruz,USA, dilution:1:1000). .. A staining index was used to evaluate CD31 and HIF-1α expression using Aperio ImageScope viewer.

    Next-Generation Sequencing:

    Article Title: Analysis of Predictive Biomarkers in Patients With Lung Adenocarcinoma From Southern Brazil Reveals a Distinct Profile From Other Regions of the Country
    Article Snippet: Of the 799 NSCLC samples that were received by the Precision Medicine Program of the HCPA, 619 (77.4%) were considered suitable for NGS analysis on the basis of tumor cell content, DNA amount, and purity. .. Molecular Analysis by NGS Molecular analysis of the EGFR, KRAS, NRAS, and BRAF genes was performed with an NGS platform (Ion Torrent PGM, server version 5.0; ThermoFisher Scientific, Waltham, MA). .. We used an AmpliSeqTM customized panel (ThermoFisher Scientific) to identify mutations in the EGFR gene (exons 18 to 21), KRAS (exons 2 and 3), NRAS (exons 2 and 3), and BRAF (exons 11 and 15).

    Immunohistochemistry:

    Article Title: Proteomics identifies EGF‐like domain multiple 7 as a potential therapeutic target for epidermal growth factor receptor‐positive glioma, et al. Proteomics identifies EGF‐like domain multiple 7 as a potential therapeutic target for epidermal growth factor receptor‐positive glioma
    Article Snippet: Sections were put in 10 mmol/L citrate antigen‐unmasking solution (pH 6.0) heating in oven at 90°C for 15 min. All sections were incubated with 10% fetal bovine serum (FBS) (Thermo Fisher Scientific) at 37°C for 10 min. Next, sections were incubated with primary antibodies (1:100 dilution) overnight at 4°C, followed by incubation with biotin‐labeled secondary antibodies (1:100 dilution) for 1 h at 37°C and then incubated with 3,3’‐diaminobenzidine substrate solution (Zhongshan Bio Corp, Zhongshan, Guangdong, China), counterstained with hematoxylin (Zhongshan Bio Corp), and visualized under a light microscope. .. The antibodies used in IHC included antibodies against EGF‐like domain multiple 7 (EGFL7) (sc‐373898, dilution 1:100, Santa Cruz Biotechnology, Dallas, TX, USA), EGFR (MA5‐13070, dilution 1:100, Invitrogen, Waltham, MA, USA), marker of proliferation Ki67 (KI67) (ab15580, dilution 1:200, Abcam, Cambridge, MA, USA), phosphorylated extracellular signal‐regulated kinase (p‐ERK)1/2 (ab214362, dilution 1:200, Abcam), and phosphorylated pyruvate kinase M1/2 (p‐PKM1/2) (#3827, dilution 1:200, Cell Signaling Technology, Danvers, MA, USA). .. The staining intensity was scored on a scale of 0 to 3 (0, negative; 1, slightly positive; 2, moderately positive; 3, intensely positive) by two experienced pathologists without knowledge of the diagnosis.

    Article Title: 18F-fludrodeoxyglucose maximal standardized uptake value and metabolic tumor burden are associated with major chemotherapy-related tumor markers in NSCLC patients
    Article Snippet: The SUV was calculated with respect to total body weight according to the formula: SUV = Tumor activity concentration Injected dose/body weight .. Immunohistochemical analysis Protein expressions of EGFR, p53, and ERCC1 were evaluated on representative full sections of biopsy samples using the respective monoclonal antibodies: EGFR, ZM-0083, clone: 31G7, dilution 1:100 (Thermo Fisher Scientific, Waltham, MA, USA); p53, ZM-0408, clone: BP53.12, dilution 1:50 (Thermo Fisher Scientific); ERCC1, ZM-0138, clone: 4 F9, dilution 1:50 (Thermo Fisher Scientific). .. Intensity of staining was scored as the following: 0 (no staining), 1 (weak staining), 2 (intermediate staining), and 3 (strong staining).

    Marker:

    Article Title: Proteomics identifies EGF‐like domain multiple 7 as a potential therapeutic target for epidermal growth factor receptor‐positive glioma, et al. Proteomics identifies EGF‐like domain multiple 7 as a potential therapeutic target for epidermal growth factor receptor‐positive glioma
    Article Snippet: Sections were put in 10 mmol/L citrate antigen‐unmasking solution (pH 6.0) heating in oven at 90°C for 15 min. All sections were incubated with 10% fetal bovine serum (FBS) (Thermo Fisher Scientific) at 37°C for 10 min. Next, sections were incubated with primary antibodies (1:100 dilution) overnight at 4°C, followed by incubation with biotin‐labeled secondary antibodies (1:100 dilution) for 1 h at 37°C and then incubated with 3,3’‐diaminobenzidine substrate solution (Zhongshan Bio Corp, Zhongshan, Guangdong, China), counterstained with hematoxylin (Zhongshan Bio Corp), and visualized under a light microscope. .. The antibodies used in IHC included antibodies against EGF‐like domain multiple 7 (EGFL7) (sc‐373898, dilution 1:100, Santa Cruz Biotechnology, Dallas, TX, USA), EGFR (MA5‐13070, dilution 1:100, Invitrogen, Waltham, MA, USA), marker of proliferation Ki67 (KI67) (ab15580, dilution 1:200, Abcam, Cambridge, MA, USA), phosphorylated extracellular signal‐regulated kinase (p‐ERK)1/2 (ab214362, dilution 1:200, Abcam), and phosphorylated pyruvate kinase M1/2 (p‐PKM1/2) (#3827, dilution 1:200, Cell Signaling Technology, Danvers, MA, USA). .. The staining intensity was scored on a scale of 0 to 3 (0, negative; 1, slightly positive; 2, moderately positive; 3, intensely positive) by two experienced pathologists without knowledge of the diagnosis.

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    Thermo Fisher egfr wild type cell lines
    ZWM026 induces different death way of cells and exerts synergistic effect combined with cisplatin. (A, B) Activities of ZWM026 against cleaved-PARP, LC3B and phosphor-PKCα/βII in <t>H1975</t> and A549 cell lines. Cells were treated with ZWM026 and gefitinib at indicated concentration for 48 hours. The resulting extracts were probed with the indicated antibodies. (C) Efficacy comparisons of ZWM026 and PKC412 against <t>phosphor-EGFR</t> and phosphor-PKCα/βII in constructed NIH-3T3 stably expressed EGFR-L858R/T790M and EGFR-WT. Cells were treated with the compounds for 30 minutes and lysed as described methods. (D) ZWM026 in combination with cisplatin induces the synergistic inhibition of proliferation. We examined the effects of ZWM026 and cisplatin, either alone or in combination, on growth inhibition of H1975 cells by the MTT assay (The CI value was calculated according to the CompuSyn software). The CI > 1 is antagonistic, CI = 1 is additive and CI
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    92
    Thermo Fisher monoclonal egfr mouse antibody
    Immunohistochemical stain of lung adenocarcinoma. Control pan-cytokeratin antibody stains all tissue samples regardless of <t>EGFR</t> mutation status. Case 1 . A sample with wild-type EGFR was not stained with total EGFR, L858R and delE746-A750 antibodies. Case 2 . A sample with delE746-A750 was stained with both total EGFR and delE746-A750 specific antibody. Case 3. A sample with L858R was stained with both total EGFR and L858R specific antibody. Case 4. A sample with wild-type EGFR was stained with moderate intensity of total EGFR and mild intensity of L858R specific antibody.
    Monoclonal Egfr Mouse Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/monoclonal egfr mouse antibody/product/Thermo Fisher
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    monoclonal egfr mouse antibody - by Bioz Stars, 2021-05
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    92
    Thermo Fisher snp egfr c 16170352 20
    rs884419 as a potential cis -acting <t>EGFR</t> regulator. (A) Genomic context for SNPs analyzed; red, rs884419; yellow, all others. (B) LD plot for SNPs in/near EGFR gene. Color intensity is proportional to LD strength between SNP pairs. (C) MatInspector-predicted
    Snp Egfr C 16170352 20, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/snp egfr c 16170352 20/product/Thermo Fisher
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    snp egfr c 16170352 20 - by Bioz Stars, 2021-05
    92/100 stars
      Buy from Supplier


    Image Search Results


    ZWM026 induces different death way of cells and exerts synergistic effect combined with cisplatin. (A, B) Activities of ZWM026 against cleaved-PARP, LC3B and phosphor-PKCα/βII in H1975 and A549 cell lines. Cells were treated with ZWM026 and gefitinib at indicated concentration for 48 hours. The resulting extracts were probed with the indicated antibodies. (C) Efficacy comparisons of ZWM026 and PKC412 against phosphor-EGFR and phosphor-PKCα/βII in constructed NIH-3T3 stably expressed EGFR-L858R/T790M and EGFR-WT. Cells were treated with the compounds for 30 minutes and lysed as described methods. (D) ZWM026 in combination with cisplatin induces the synergistic inhibition of proliferation. We examined the effects of ZWM026 and cisplatin, either alone or in combination, on growth inhibition of H1975 cells by the MTT assay (The CI value was calculated according to the CompuSyn software). The CI > 1 is antagonistic, CI = 1 is additive and CI

    Journal: American Journal of Cancer Research

    Article Title: A novel multi-target inhibitor harboring selectivity of inhibiting EGFR T790M sparing wild-type EGFR

    doi:

    Figure Lengend Snippet: ZWM026 induces different death way of cells and exerts synergistic effect combined with cisplatin. (A, B) Activities of ZWM026 against cleaved-PARP, LC3B and phosphor-PKCα/βII in H1975 and A549 cell lines. Cells were treated with ZWM026 and gefitinib at indicated concentration for 48 hours. The resulting extracts were probed with the indicated antibodies. (C) Efficacy comparisons of ZWM026 and PKC412 against phosphor-EGFR and phosphor-PKCα/βII in constructed NIH-3T3 stably expressed EGFR-L858R/T790M and EGFR-WT. Cells were treated with the compounds for 30 minutes and lysed as described methods. (D) ZWM026 in combination with cisplatin induces the synergistic inhibition of proliferation. We examined the effects of ZWM026 and cisplatin, either alone or in combination, on growth inhibition of H1975 cells by the MTT assay (The CI value was calculated according to the CompuSyn software). The CI > 1 is antagonistic, CI = 1 is additive and CI

    Article Snippet: EGFR mutant NSCLC cell lines NCI-H1975 (L858R/T790M) and HCC827 (del E746_A750), and EGFR wild-type cell lines including NCI-H3122, NCI-H1299 and PC14 were cultured in RPMI-1640 (Life Technologies).

    Techniques: Concentration Assay, Construct, Stable Transfection, Inhibition, MTT Assay, Software

    AKT, TSC2, mTOR and S6 are required for UV-induced AKT cascade activation. (A and B) HaCaT cells were exposed to different dosages of UV radiation (0, 5, 15, 30, 60, 120 mJ/cm 2 ) for 30 min and for different durations of 30 mJ/cm 2 UV respectively. p-EGFR (Tyr1068), p-AKT (Ser473), p-4E-BP1 (Ser65) were detected by western blotting. (C) HaCaT cells were pretreated with 20 μM niacin, followed by UV radiation (0, 15, 30, 60 mJ/cm 2 ), then stained with the JC-1 probe and imaged by fluorescent microscope. The individual red and green average fluorescence intensities are expressed as the ratio of green to red fluorescence. An increase on the fluorescence green/red ratio indicates a shift increase in mitochondrial depolarization as an early apoptosis label. HaCaT cells were pre-treated with (D) the EGFR inhibitor, PD153035 (PD, 1 μM); (E) with the PI3K/AKT inhibitor LY294002 (LY, 10 μM) and mTOR inhibitor rapamycin (Rapa, 100 nM), for 1 h, with UV (30 mJ/cm 2 ) radiation and cultured for 15, 30 and 60 min. (F) Cells were transfected with Tuberin/TSC2 siRNAII (100 nM) for 48 h prior to UV radiation (30 mJ/cm 2 ), for 30 or 60 min. p-EGFR (Tyr1068), p-AKT (Ser473), p-AKT (Thr308), p-TSC2 (Thr1462), p-mTOR (Ser2448), p-S6K (Thr389), p-S6 (Ser235/236), p-4E-BP1 (Ser65) and total AKT antibody were used by western blotting. All experiments were repeated at least three times and similar results were obtained.

    Journal: International Journal of Molecular Medicine

    Article Title: Niacin protects against UVB radiation-induced apoptosis in cultured human skin keratinocytes

    doi: 10.3892/ijmm.2012.886

    Figure Lengend Snippet: AKT, TSC2, mTOR and S6 are required for UV-induced AKT cascade activation. (A and B) HaCaT cells were exposed to different dosages of UV radiation (0, 5, 15, 30, 60, 120 mJ/cm 2 ) for 30 min and for different durations of 30 mJ/cm 2 UV respectively. p-EGFR (Tyr1068), p-AKT (Ser473), p-4E-BP1 (Ser65) were detected by western blotting. (C) HaCaT cells were pretreated with 20 μM niacin, followed by UV radiation (0, 15, 30, 60 mJ/cm 2 ), then stained with the JC-1 probe and imaged by fluorescent microscope. The individual red and green average fluorescence intensities are expressed as the ratio of green to red fluorescence. An increase on the fluorescence green/red ratio indicates a shift increase in mitochondrial depolarization as an early apoptosis label. HaCaT cells were pre-treated with (D) the EGFR inhibitor, PD153035 (PD, 1 μM); (E) with the PI3K/AKT inhibitor LY294002 (LY, 10 μM) and mTOR inhibitor rapamycin (Rapa, 100 nM), for 1 h, with UV (30 mJ/cm 2 ) radiation and cultured for 15, 30 and 60 min. (F) Cells were transfected with Tuberin/TSC2 siRNAII (100 nM) for 48 h prior to UV radiation (30 mJ/cm 2 ), for 30 or 60 min. p-EGFR (Tyr1068), p-AKT (Ser473), p-AKT (Thr308), p-TSC2 (Thr1462), p-mTOR (Ser2448), p-S6K (Thr389), p-S6 (Ser235/236), p-4E-BP1 (Ser65) and total AKT antibody were used by western blotting. All experiments were repeated at least three times and similar results were obtained.

    Article Snippet: The EGFR inhibitor, PD153035 was purchased from Invitrogen (Carlsbad, CA, USA).

    Techniques: Activation Assay, Western Blot, Staining, Microscopy, Fluorescence, Cell Culture, Transfection

    Immunohistochemical stain of lung adenocarcinoma. Control pan-cytokeratin antibody stains all tissue samples regardless of EGFR mutation status. Case 1 . A sample with wild-type EGFR was not stained with total EGFR, L858R and delE746-A750 antibodies. Case 2 . A sample with delE746-A750 was stained with both total EGFR and delE746-A750 specific antibody. Case 3. A sample with L858R was stained with both total EGFR and L858R specific antibody. Case 4. A sample with wild-type EGFR was stained with moderate intensity of total EGFR and mild intensity of L858R specific antibody.

    Journal: PLoS ONE

    Article Title: Including Total EGFR Staining in Scoring Improves EGFR Mutations Detection by Mutation-Specific Antibodies and EGFR TKIs Response Prediction

    doi: 10.1371/journal.pone.0023303

    Figure Lengend Snippet: Immunohistochemical stain of lung adenocarcinoma. Control pan-cytokeratin antibody stains all tissue samples regardless of EGFR mutation status. Case 1 . A sample with wild-type EGFR was not stained with total EGFR, L858R and delE746-A750 antibodies. Case 2 . A sample with delE746-A750 was stained with both total EGFR and delE746-A750 specific antibody. Case 3. A sample with L858R was stained with both total EGFR and L858R specific antibody. Case 4. A sample with wild-type EGFR was stained with moderate intensity of total EGFR and mild intensity of L858R specific antibody.

    Article Snippet: We also performed IHC staining for total EGFR protein using the monoclonal EGFR mouse antibody (clone 31G7, dilution 1∶150, Invitrogen, CA).

    Techniques: Immunohistochemistry, Staining, Mutagenesis

    Receiver–operator characteristic (ROC) curve of EGFR mutation-specific antibodies IHC in predicting L858R or E746-A750. (A) AUC for the logistic regression model based on L858R Q score and total EGFR expression Q score was higher than that for L858R intensity only (0.891 vs. 0.853; p = 0.036). (B) the logistic regression model based on delE746-A750 Q score and total EGFR expression intensity had a trend of higher AUC than that for delE746-A750 intensity only (0.969 vs. 0.958; p = 0.087). AUC: area under the ROC curve.

    Journal: PLoS ONE

    Article Title: Including Total EGFR Staining in Scoring Improves EGFR Mutations Detection by Mutation-Specific Antibodies and EGFR TKIs Response Prediction

    doi: 10.1371/journal.pone.0023303

    Figure Lengend Snippet: Receiver–operator characteristic (ROC) curve of EGFR mutation-specific antibodies IHC in predicting L858R or E746-A750. (A) AUC for the logistic regression model based on L858R Q score and total EGFR expression Q score was higher than that for L858R intensity only (0.891 vs. 0.853; p = 0.036). (B) the logistic regression model based on delE746-A750 Q score and total EGFR expression intensity had a trend of higher AUC than that for delE746-A750 intensity only (0.969 vs. 0.958; p = 0.087). AUC: area under the ROC curve.

    Article Snippet: We also performed IHC staining for total EGFR protein using the monoclonal EGFR mouse antibody (clone 31G7, dilution 1∶150, Invitrogen, CA).

    Techniques: Mutagenesis, Immunohistochemistry, Expressing

    rs884419 as a potential cis -acting EGFR regulator. (A) Genomic context for SNPs analyzed; red, rs884419; yellow, all others. (B) LD plot for SNPs in/near EGFR gene. Color intensity is proportional to LD strength between SNP pairs. (C) MatInspector-predicted

    Journal: The Journal of urology

    Article Title: The EGFR Polymorphism rs884419 is Associated with Freedom from Recurrence in Patients with Resected Prostate Cancer

    doi: 10.1016/j.juro.2009.12.098

    Figure Lengend Snippet: rs884419 as a potential cis -acting EGFR regulator. (A) Genomic context for SNPs analyzed; red, rs884419; yellow, all others. (B) LD plot for SNPs in/near EGFR gene. Color intensity is proportional to LD strength between SNP pairs. (C) MatInspector-predicted

    Article Snippet: Allelic discrimination of these EGFR polymorphisms was performed using Taqman® SNP genotyping assays (Applied Biosystems, assay IDs: C_335819_10 [rs3735064], C_2678606_10 [rs7780270], C_16170352_20 [rs11543848], C_321872_10 [rs11976696], C_2678667_10 [rs9642391], C_7610424_10 [rs845560], C_7610434_10 [rs845562], and C_8304143_10 [rs884419]), and the following reagents for rs7808697: Forward primer, 5’-CTC CAT CCA TGT TCT TGC AAA GTA C-3’; Reverse primer, 5’-GAC AGA CTG GAT AAA GAA AAT TGT GGT ACA-3’; and the allele-specific probes 5’-VIC-CTT TTG TGG CTA CCT AGT G-3’ and 5’-FAM- TTG TGG CTG CCT AGT G-3’.

    Techniques:

    Impact of Genotype for EGFR SNPs on Recurrence and Survival Outcomes in Prostate Cancer

    Journal: The Journal of urology

    Article Title: The EGFR Polymorphism rs884419 is Associated with Freedom from Recurrence in Patients with Resected Prostate Cancer

    doi: 10.1016/j.juro.2009.12.098

    Figure Lengend Snippet: Impact of Genotype for EGFR SNPs on Recurrence and Survival Outcomes in Prostate Cancer

    Article Snippet: Allelic discrimination of these EGFR polymorphisms was performed using Taqman® SNP genotyping assays (Applied Biosystems, assay IDs: C_335819_10 [rs3735064], C_2678606_10 [rs7780270], C_16170352_20 [rs11543848], C_321872_10 [rs11976696], C_2678667_10 [rs9642391], C_7610424_10 [rs845560], C_7610434_10 [rs845562], and C_8304143_10 [rs884419]), and the following reagents for rs7808697: Forward primer, 5’-CTC CAT CCA TGT TCT TGC AAA GTA C-3’; Reverse primer, 5’-GAC AGA CTG GAT AAA GAA AAT TGT GGT ACA-3’; and the allele-specific probes 5’-VIC-CTT TTG TGG CTA CCT AGT G-3’ and 5’-FAM- TTG TGG CTG CCT AGT G-3’.

    Techniques:

    Impact of Genotype for EGFR SNPs on Recurrence and Survival Outcomes in Prostate Cancer

    Journal: The Journal of urology

    Article Title: The EGFR Polymorphism rs884419 is Associated with Freedom from Recurrence in Patients with Resected Prostate Cancer

    doi: 10.1016/j.juro.2009.12.098

    Figure Lengend Snippet: Impact of Genotype for EGFR SNPs on Recurrence and Survival Outcomes in Prostate Cancer

    Article Snippet: Allelic discrimination of these EGFR polymorphisms was performed using Taqman® SNP genotyping assays (Applied Biosystems, assay IDs: C_335819_10 [rs3735064], C_2678606_10 [rs7780270], C_16170352_20 [rs11543848], C_321872_10 [rs11976696], C_2678667_10 [rs9642391], C_7610424_10 [rs845560], C_7610434_10 [rs845562], and C_8304143_10 [rs884419]), and the following reagents for rs7808697: Forward primer, 5’-CTC CAT CCA TGT TCT TGC AAA GTA C-3’; Reverse primer, 5’-GAC AGA CTG GAT AAA GAA AAT TGT GGT ACA-3’; and the allele-specific probes 5’-VIC-CTT TTG TGG CTA CCT AGT G-3’ and 5’-FAM- TTG TGG CTG CCT AGT G-3’.

    Techniques:

    Kaplan-Meier estimates of freedom from recurrence (FFR) following radical prostatectomy as treatment for localized prostate cancer. (A) FFR curves were plotted for the individual EGFR rs884419 genotypes. (B) FFR curves were plotted to test whether allele

    Journal: The Journal of urology

    Article Title: The EGFR Polymorphism rs884419 is Associated with Freedom from Recurrence in Patients with Resected Prostate Cancer

    doi: 10.1016/j.juro.2009.12.098

    Figure Lengend Snippet: Kaplan-Meier estimates of freedom from recurrence (FFR) following radical prostatectomy as treatment for localized prostate cancer. (A) FFR curves were plotted for the individual EGFR rs884419 genotypes. (B) FFR curves were plotted to test whether allele

    Article Snippet: Allelic discrimination of these EGFR polymorphisms was performed using Taqman® SNP genotyping assays (Applied Biosystems, assay IDs: C_335819_10 [rs3735064], C_2678606_10 [rs7780270], C_16170352_20 [rs11543848], C_321872_10 [rs11976696], C_2678667_10 [rs9642391], C_7610424_10 [rs845560], C_7610434_10 [rs845562], and C_8304143_10 [rs884419]), and the following reagents for rs7808697: Forward primer, 5’-CTC CAT CCA TGT TCT TGC AAA GTA C-3’; Reverse primer, 5’-GAC AGA CTG GAT AAA GAA AAT TGT GGT ACA-3’; and the allele-specific probes 5’-VIC-CTT TTG TGG CTA CCT AGT G-3’ and 5’-FAM- TTG TGG CTG CCT AGT G-3’.

    Techniques:

    EGFR rs884419 SNP Genotype Predicts FFR Independently of Tumor Grade, PSA Levels, and Surgical Margin Status

    Journal: The Journal of urology

    Article Title: The EGFR Polymorphism rs884419 is Associated with Freedom from Recurrence in Patients with Resected Prostate Cancer

    doi: 10.1016/j.juro.2009.12.098

    Figure Lengend Snippet: EGFR rs884419 SNP Genotype Predicts FFR Independently of Tumor Grade, PSA Levels, and Surgical Margin Status

    Article Snippet: Allelic discrimination of these EGFR polymorphisms was performed using Taqman® SNP genotyping assays (Applied Biosystems, assay IDs: C_335819_10 [rs3735064], C_2678606_10 [rs7780270], C_16170352_20 [rs11543848], C_321872_10 [rs11976696], C_2678667_10 [rs9642391], C_7610424_10 [rs845560], C_7610434_10 [rs845562], and C_8304143_10 [rs884419]), and the following reagents for rs7808697: Forward primer, 5’-CTC CAT CCA TGT TCT TGC AAA GTA C-3’; Reverse primer, 5’-GAC AGA CTG GAT AAA GAA AAT TGT GGT ACA-3’; and the allele-specific probes 5’-VIC-CTT TTG TGG CTA CCT AGT G-3’ and 5’-FAM- TTG TGG CTG CCT AGT G-3’.

    Techniques: