egfr Epitomics Search Results


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  • 80
    Millipore anti egfr mab
    Anti Egfr Mab, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher primary anti egfr antibody
    Primary Anti Egfr Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher n terminal epitope egfr
    <t>EGFR</t> deletion variants resulting from EGFR C-terminal domain exonic deletion (CTED) mutation have transforming potential (A) Schematic diagram of EGFR C-terminal exonic deletion mutations characterized in this study. Brown lines indicate exons splicing events whereas red lines indicate out-of-frame splicing. The total translated amino acid numbers of each CTED mutant and clinical incidence of each genomic alteration are indicated. For CTED1, CTED3, CTED6, and CTED7, exonic deletion results in inclusion of intron due to the loss of splicing acceptor site. For CTED2, CTED4, and CTED5, exonic deletion generates a frameshifted exon 28, with the addition of Asn (N) and Thr (T) followed by early termination. The number of amino acids added by inclusion of intron or frameshift of exon 28 are indicated with ( † ) and ( ‡ ) respectively, followed by + sign. Red asterisk (*) indicate the predicted intron-encoded stop codon and stop codons generated by frameshift and blue asterisk (*) indicate location of the EGFR stop codon. (B) NIH-3T3 cells stably expressing the indicated CTED mutant or WT EGFR were assayed for anchorage-independent growth in soft agar in the presence or absence of EGF. The bar graph depicts the number of colonies formed in soft agar (n=3, mean + SD). (C) Cell lysates prepared from NIH-3T3 cells expressing the indicated EGFR CTED mutants or WT EGFR were subjected to immunoblotting with antibodies against N-terminal <t>epitope</t> EGFR, C-terminal epitope EGFR, phospho-tyrosine (4G10), phospho-Stat3, phospho-Stat5, phospho-Akt, and β-actin.
    N Terminal Epitope Egfr, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Epitomics p egfr y1086
    <t>EGFR</t> deletion variants resulting from EGFR C-terminal domain exonic deletion (CTED) mutation have transforming potential (A) Schematic diagram of EGFR C-terminal exonic deletion mutations characterized in this study. Brown lines indicate exons splicing events whereas red lines indicate out-of-frame splicing. The total translated amino acid numbers of each CTED mutant and clinical incidence of each genomic alteration are indicated. For CTED1, CTED3, CTED6, and CTED7, exonic deletion results in inclusion of intron due to the loss of splicing acceptor site. For CTED2, CTED4, and CTED5, exonic deletion generates a frameshifted exon 28, with the addition of Asn (N) and Thr (T) followed by early termination. The number of amino acids added by inclusion of intron or frameshift of exon 28 are indicated with ( † ) and ( ‡ ) respectively, followed by + sign. Red asterisk (*) indicate the predicted intron-encoded stop codon and stop codons generated by frameshift and blue asterisk (*) indicate location of the EGFR stop codon. (B) NIH-3T3 cells stably expressing the indicated CTED mutant or WT EGFR were assayed for anchorage-independent growth in soft agar in the presence or absence of EGF. The bar graph depicts the number of colonies formed in soft agar (n=3, mean + SD). (C) Cell lysates prepared from NIH-3T3 cells expressing the indicated EGFR CTED mutants or WT EGFR were subjected to immunoblotting with antibodies against N-terminal <t>epitope</t> EGFR, C-terminal epitope EGFR, phospho-tyrosine (4G10), phospho-Stat3, phospho-Stat5, phospho-Akt, and β-actin.
    P Egfr Y1086, supplied by Epitomics, used in various techniques. Bioz Stars score: 78/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics total egfr
    <t>EGFR</t> deletion variants resulting from EGFR C-terminal domain exonic deletion (CTED) mutation have transforming potential (A) Schematic diagram of EGFR C-terminal exonic deletion mutations characterized in this study. Brown lines indicate exons splicing events whereas red lines indicate out-of-frame splicing. The total translated amino acid numbers of each CTED mutant and clinical incidence of each genomic alteration are indicated. For CTED1, CTED3, CTED6, and CTED7, exonic deletion results in inclusion of intron due to the loss of splicing acceptor site. For CTED2, CTED4, and CTED5, exonic deletion generates a frameshifted exon 28, with the addition of Asn (N) and Thr (T) followed by early termination. The number of amino acids added by inclusion of intron or frameshift of exon 28 are indicated with ( † ) and ( ‡ ) respectively, followed by + sign. Red asterisk (*) indicate the predicted intron-encoded stop codon and stop codons generated by frameshift and blue asterisk (*) indicate location of the EGFR stop codon. (B) NIH-3T3 cells stably expressing the indicated CTED mutant or WT EGFR were assayed for anchorage-independent growth in soft agar in the presence or absence of EGF. The bar graph depicts the number of colonies formed in soft agar (n=3, mean + SD). (C) Cell lysates prepared from NIH-3T3 cells expressing the indicated EGFR CTED mutants or WT EGFR were subjected to immunoblotting with antibodies against N-terminal <t>epitope</t> EGFR, C-terminal epitope EGFR, phospho-tyrosine (4G10), phospho-Stat3, phospho-Stat5, phospho-Akt, and β-actin.
    Total Egfr, supplied by Epitomics, used in various techniques. Bioz Stars score: 88/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics immunoblot analysis p egfr
    <t>EGFR</t> deletion variants resulting from EGFR C-terminal domain exonic deletion (CTED) mutation have transforming potential (A) Schematic diagram of EGFR C-terminal exonic deletion mutations characterized in this study. Brown lines indicate exons splicing events whereas red lines indicate out-of-frame splicing. The total translated amino acid numbers of each CTED mutant and clinical incidence of each genomic alteration are indicated. For CTED1, CTED3, CTED6, and CTED7, exonic deletion results in inclusion of intron due to the loss of splicing acceptor site. For CTED2, CTED4, and CTED5, exonic deletion generates a frameshifted exon 28, with the addition of Asn (N) and Thr (T) followed by early termination. The number of amino acids added by inclusion of intron or frameshift of exon 28 are indicated with ( † ) and ( ‡ ) respectively, followed by + sign. Red asterisk (*) indicate the predicted intron-encoded stop codon and stop codons generated by frameshift and blue asterisk (*) indicate location of the EGFR stop codon. (B) NIH-3T3 cells stably expressing the indicated CTED mutant or WT EGFR were assayed for anchorage-independent growth in soft agar in the presence or absence of EGF. The bar graph depicts the number of colonies formed in soft agar (n=3, mean + SD). (C) Cell lysates prepared from NIH-3T3 cells expressing the indicated EGFR CTED mutants or WT EGFR were subjected to immunoblotting with antibodies against N-terminal <t>epitope</t> EGFR, C-terminal epitope EGFR, phospho-tyrosine (4G10), phospho-Stat3, phospho-Stat5, phospho-Akt, and β-actin.
    Immunoblot Analysis P Egfr, supplied by Epitomics, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics egfr phospho py1173
    <t>EGFR</t> deletion variants resulting from EGFR C-terminal domain exonic deletion (CTED) mutation have transforming potential (A) Schematic diagram of EGFR C-terminal exonic deletion mutations characterized in this study. Brown lines indicate exons splicing events whereas red lines indicate out-of-frame splicing. The total translated amino acid numbers of each CTED mutant and clinical incidence of each genomic alteration are indicated. For CTED1, CTED3, CTED6, and CTED7, exonic deletion results in inclusion of intron due to the loss of splicing acceptor site. For CTED2, CTED4, and CTED5, exonic deletion generates a frameshifted exon 28, with the addition of Asn (N) and Thr (T) followed by early termination. The number of amino acids added by inclusion of intron or frameshift of exon 28 are indicated with ( † ) and ( ‡ ) respectively, followed by + sign. Red asterisk (*) indicate the predicted intron-encoded stop codon and stop codons generated by frameshift and blue asterisk (*) indicate location of the EGFR stop codon. (B) NIH-3T3 cells stably expressing the indicated CTED mutant or WT EGFR were assayed for anchorage-independent growth in soft agar in the presence or absence of EGF. The bar graph depicts the number of colonies formed in soft agar (n=3, mean + SD). (C) Cell lysates prepared from NIH-3T3 cells expressing the indicated EGFR CTED mutants or WT EGFR were subjected to immunoblotting with antibodies against N-terminal <t>epitope</t> EGFR, C-terminal epitope EGFR, phospho-tyrosine (4G10), phospho-Stat3, phospho-Stat5, phospho-Akt, and β-actin.
    Egfr Phospho Py1173, supplied by Epitomics, used in various techniques. Bioz Stars score: 78/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics egfr
    <t>EGFR</t> deletion variants resulting from EGFR C-terminal domain exonic deletion (CTED) mutation have transforming potential (A) Schematic diagram of EGFR C-terminal exonic deletion mutations characterized in this study. Brown lines indicate exons splicing events whereas red lines indicate out-of-frame splicing. The total translated amino acid numbers of each CTED mutant and clinical incidence of each genomic alteration are indicated. For CTED1, CTED3, CTED6, and CTED7, exonic deletion results in inclusion of intron due to the loss of splicing acceptor site. For CTED2, CTED4, and CTED5, exonic deletion generates a frameshifted exon 28, with the addition of Asn (N) and Thr (T) followed by early termination. The number of amino acids added by inclusion of intron or frameshift of exon 28 are indicated with ( † ) and ( ‡ ) respectively, followed by + sign. Red asterisk (*) indicate the predicted intron-encoded stop codon and stop codons generated by frameshift and blue asterisk (*) indicate location of the EGFR stop codon. (B) NIH-3T3 cells stably expressing the indicated CTED mutant or WT EGFR were assayed for anchorage-independent growth in soft agar in the presence or absence of EGF. The bar graph depicts the number of colonies formed in soft agar (n=3, mean + SD). (C) Cell lysates prepared from NIH-3T3 cells expressing the indicated EGFR CTED mutants or WT EGFR were subjected to immunoblotting with antibodies against N-terminal <t>epitope</t> EGFR, C-terminal epitope EGFR, phospho-tyrosine (4G10), phospho-Stat3, phospho-Stat5, phospho-Akt, and β-actin.
    Egfr, supplied by Epitomics, used in various techniques. Bioz Stars score: 93/100, based on 73 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics p egfr
    Potential mechanism by which NSCLC cells with wt <t>EGFR</t> display resistance to erlotinib. The up-regulation of ErbB ligands (TGF-α, EREG and NRG4) activates EGFR. Activation of RAF1-MEK1-ERK and <t>PKC/SNAI-AKT</t> up-regulates the downstream signaling
    P Egfr, supplied by Epitomics, used in various techniques. Bioz Stars score: 89/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics phospho egfr
    Potential mechanism by which NSCLC cells with wt <t>EGFR</t> display resistance to erlotinib. The up-regulation of ErbB ligands (TGF-α, EREG and NRG4) activates EGFR. Activation of RAF1-MEK1-ERK and <t>PKC/SNAI-AKT</t> up-regulates the downstream signaling
    Phospho Egfr, supplied by Epitomics, used in various techniques. Bioz Stars score: 88/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics p egfr s1046 7 antibody
    Potential mechanism by which NSCLC cells with wt <t>EGFR</t> display resistance to erlotinib. The up-regulation of ErbB ligands (TGF-α, EREG and NRG4) activates EGFR. Activation of RAF1-MEK1-ERK and <t>PKC/SNAI-AKT</t> up-regulates the downstream signaling
    P Egfr S1046 7 Antibody, supplied by Epitomics, used in various techniques. Bioz Stars score: 79/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics anti p egfr py1068
    Potential mechanism by which NSCLC cells with wt <t>EGFR</t> display resistance to erlotinib. The up-regulation of ErbB ligands (TGF-α, EREG and NRG4) activates EGFR. Activation of RAF1-MEK1-ERK and <t>PKC/SNAI-AKT</t> up-regulates the downstream signaling
    Anti P Egfr Py1068, supplied by Epitomics, used in various techniques. Bioz Stars score: 81/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics phospho egfr tyr1173
    Potential mechanism by which NSCLC cells with wt <t>EGFR</t> display resistance to erlotinib. The up-regulation of ErbB ligands (TGF-α, EREG and NRG4) activates EGFR. Activation of RAF1-MEK1-ERK and <t>PKC/SNAI-AKT</t> up-regulates the downstream signaling
    Phospho Egfr Tyr1173, supplied by Epitomics, used in various techniques. Bioz Stars score: 78/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore anti egfr antibody
    Potential mechanism by which NSCLC cells with wt <t>EGFR</t> display resistance to erlotinib. The up-regulation of ErbB ligands (TGF-α, EREG and NRG4) activates EGFR. Activation of RAF1-MEK1-ERK and <t>PKC/SNAI-AKT</t> up-regulates the downstream signaling
    Anti Egfr Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 187 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics rabbit anti phospho tyr1068 p egfr
    Potential mechanism by which NSCLC cells with wt <t>EGFR</t> display resistance to erlotinib. The up-regulation of ErbB ligands (TGF-α, EREG and NRG4) activates EGFR. Activation of RAF1-MEK1-ERK and <t>PKC/SNAI-AKT</t> up-regulates the downstream signaling
    Rabbit Anti Phospho Tyr1068 P Egfr, supplied by Epitomics, used in various techniques. Bioz Stars score: 81/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Boster Bio anti egfr
    Potential mechanism by which NSCLC cells with wt <t>EGFR</t> display resistance to erlotinib. The up-regulation of ErbB ligands (TGF-α, EREG and NRG4) activates EGFR. Activation of RAF1-MEK1-ERK and <t>PKC/SNAI-AKT</t> up-regulates the downstream signaling
    Anti Egfr, supplied by Boster Bio, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Abcam phosphorylated her1
    a Extended dosing study investigating seven i.v. weekly administrations of an efficacious dose (3 mg/kg) and a less-efficacious (0.3 mg/kg) dose of RG7116 in FaDu xenograft mice (FaDu_008). RG7116 given as a three-weekly cycle (two doses in total) was also investigated. b Dose-dependent efficacy up to Day 39 was seen as in the previous study and tumor growth inhibition with 3 mg/kg RG7116 given as a three-weekly cycle was similar to weekly dosing. Mice in the 0.3 mg/kg group were rechallenged ( black arrow ) with 5 mg/kg on Day 39 resulting in tumor growth inhibition for two further assessments; however, tumor regrowth was observed in all dosing groups from Day 50. c RG7116 trough concentrations from the first to third administrations again showed accumulation only with the higher dose. Inhibition of HER3 ( d ) and AKT ( e ) phosphorylation was also seen with weekly dosing at the efficacious dose (3 mg/kg) but not with the lower dose (0.3 mg/kg). Following a single 3 mg/kg dose (representing a three-weekly schedule), initial inhibition of HER3 phosphorylation was seen to diminish by Day 14 and 21. f Upregulation of <t>HER1</t> (~2.1-fold) and HER2 (~1.3-fold) mRNA was seen 96 h after FaDu xenograft mice ( n = 5) were administered 1.0 mg/kg RG7116 in a separate study, and this was associated with upregulation of HER1 and HER2 protein. g To compare the single animals, 20 µg total protein lysate was loaded per lane (lanes 101–110 are vehicle and 201–210 are the RG7116-treated animals). At Day 52, inhibition of HER3 phosphorylation was maintained in RG7116-treated mice, and expressed HER1 was seen to be phosphorylated compared to vehicle control. HER2 and pHER2 were not changed (data not shown). SEM standard error of the mean, SD standard deviation
    Phosphorylated Her1, supplied by Abcam, used in various techniques. Bioz Stars score: 79/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    R&D Systems pmoles recombinant human egfr fc hegfr fusion protein
    Binding specificity of <t>anti-EGFR</t> aptamers. The N62 pool and aptamers E03, E04, and E07 were assayed in triplicate by filtration for binding to <t>hEGFR,</t> mEGFR, hErbB2, and hIgG1. Average values and standard deviations are shown. Binding assays were carried out either in the absence (left) or presence (right) of DTT. A no protein control was also carried through the procedure. Percent binding was relative to the total RNA added.
    Pmoles Recombinant Human Egfr Fc Hegfr Fusion Protein, supplied by R&D Systems, used in various techniques. Bioz Stars score: 78/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics mouse polyclonal anti phospho egfr
    Binding specificity of <t>anti-EGFR</t> aptamers. The N62 pool and aptamers E03, E04, and E07 were assayed in triplicate by filtration for binding to <t>hEGFR,</t> mEGFR, hErbB2, and hIgG1. Average values and standard deviations are shown. Binding assays were carried out either in the absence (left) or presence (right) of DTT. A no protein control was also carried through the procedure. Percent binding was relative to the total RNA added.
    Mouse Polyclonal Anti Phospho Egfr, supplied by Epitomics, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics rabbit polyclonal anti phospho egfr py1068 antibody
    Binding specificity of <t>anti-EGFR</t> aptamers. The N62 pool and aptamers E03, E04, and E07 were assayed in triplicate by filtration for binding to <t>hEGFR,</t> mEGFR, hErbB2, and hIgG1. Average values and standard deviations are shown. Binding assays were carried out either in the absence (left) or presence (right) of DTT. A no protein control was also carried through the procedure. Percent binding was relative to the total RNA added.
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    Epitomics rabbit monoclonal anti egfr antibody
    Binding specificity of <t>anti-EGFR</t> aptamers. The N62 pool and aptamers E03, E04, and E07 were assayed in triplicate by filtration for binding to <t>hEGFR,</t> mEGFR, hErbB2, and hIgG1. Average values and standard deviations are shown. Binding assays were carried out either in the absence (left) or presence (right) of DTT. A no protein control was also carried through the procedure. Percent binding was relative to the total RNA added.
    Rabbit Monoclonal Anti Egfr Antibody, supplied by Epitomics, used in various techniques. Bioz Stars score: 80/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics monoclonal rabbit anti phospho egfr pt693
    Binding specificity of <t>anti-EGFR</t> aptamers. The N62 pool and aptamers E03, E04, and E07 were assayed in triplicate by filtration for binding to <t>hEGFR,</t> mEGFR, hErbB2, and hIgG1. Average values and standard deviations are shown. Binding assays were carried out either in the absence (left) or presence (right) of DTT. A no protein control was also carried through the procedure. Percent binding was relative to the total RNA added.
    Monoclonal Rabbit Anti Phospho Egfr Pt693, supplied by Epitomics, used in various techniques. Bioz Stars score: 80/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Epitomics rabbit monoclonal anti human egfr ab
    Binding specificity of <t>anti-EGFR</t> aptamers. The N62 pool and aptamers E03, E04, and E07 were assayed in triplicate by filtration for binding to <t>hEGFR,</t> mEGFR, hErbB2, and hIgG1. Average values and standard deviations are shown. Binding assays were carried out either in the absence (left) or presence (right) of DTT. A no protein control was also carried through the procedure. Percent binding was relative to the total RNA added.
    Rabbit Monoclonal Anti Human Egfr Ab, supplied by Epitomics, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    EGFR deletion variants resulting from EGFR C-terminal domain exonic deletion (CTED) mutation have transforming potential (A) Schematic diagram of EGFR C-terminal exonic deletion mutations characterized in this study. Brown lines indicate exons splicing events whereas red lines indicate out-of-frame splicing. The total translated amino acid numbers of each CTED mutant and clinical incidence of each genomic alteration are indicated. For CTED1, CTED3, CTED6, and CTED7, exonic deletion results in inclusion of intron due to the loss of splicing acceptor site. For CTED2, CTED4, and CTED5, exonic deletion generates a frameshifted exon 28, with the addition of Asn (N) and Thr (T) followed by early termination. The number of amino acids added by inclusion of intron or frameshift of exon 28 are indicated with ( † ) and ( ‡ ) respectively, followed by + sign. Red asterisk (*) indicate the predicted intron-encoded stop codon and stop codons generated by frameshift and blue asterisk (*) indicate location of the EGFR stop codon. (B) NIH-3T3 cells stably expressing the indicated CTED mutant or WT EGFR were assayed for anchorage-independent growth in soft agar in the presence or absence of EGF. The bar graph depicts the number of colonies formed in soft agar (n=3, mean + SD). (C) Cell lysates prepared from NIH-3T3 cells expressing the indicated EGFR CTED mutants or WT EGFR were subjected to immunoblotting with antibodies against N-terminal epitope EGFR, C-terminal epitope EGFR, phospho-tyrosine (4G10), phospho-Stat3, phospho-Stat5, phospho-Akt, and β-actin.

    Journal: Oncotarget

    Article Title: Constitutive asymmetric dimerization drives oncogenic activation of epidermal growth factor receptor carboxyl-terminal deletion mutants

    doi:

    Figure Lengend Snippet: EGFR deletion variants resulting from EGFR C-terminal domain exonic deletion (CTED) mutation have transforming potential (A) Schematic diagram of EGFR C-terminal exonic deletion mutations characterized in this study. Brown lines indicate exons splicing events whereas red lines indicate out-of-frame splicing. The total translated amino acid numbers of each CTED mutant and clinical incidence of each genomic alteration are indicated. For CTED1, CTED3, CTED6, and CTED7, exonic deletion results in inclusion of intron due to the loss of splicing acceptor site. For CTED2, CTED4, and CTED5, exonic deletion generates a frameshifted exon 28, with the addition of Asn (N) and Thr (T) followed by early termination. The number of amino acids added by inclusion of intron or frameshift of exon 28 are indicated with ( † ) and ( ‡ ) respectively, followed by + sign. Red asterisk (*) indicate the predicted intron-encoded stop codon and stop codons generated by frameshift and blue asterisk (*) indicate location of the EGFR stop codon. (B) NIH-3T3 cells stably expressing the indicated CTED mutant or WT EGFR were assayed for anchorage-independent growth in soft agar in the presence or absence of EGF. The bar graph depicts the number of colonies formed in soft agar (n=3, mean + SD). (C) Cell lysates prepared from NIH-3T3 cells expressing the indicated EGFR CTED mutants or WT EGFR were subjected to immunoblotting with antibodies against N-terminal epitope EGFR, C-terminal epitope EGFR, phospho-tyrosine (4G10), phospho-Stat3, phospho-Stat5, phospho-Akt, and β-actin.

    Article Snippet: The membrane was probed with the antibodies against either N-terminal epitope EGFR (Thermo Scientific), C-terminal epitope EGFR (Bethyl), 4G10 (Millipore), β-actin, Stat3, p-Stat3, Akt, p-Akt, p-Stat5 or p-Shc (Cell Signaling Technology).

    Techniques: Mutagenesis, Generated, Stable Transfection, Expressing

    Potential mechanism by which NSCLC cells with wt EGFR display resistance to erlotinib. The up-regulation of ErbB ligands (TGF-α, EREG and NRG4) activates EGFR. Activation of RAF1-MEK1-ERK and PKC/SNAI-AKT up-regulates the downstream signaling

    Journal: International Journal of Clinical and Experimental Pathology

    Article Title: RAF1-MEK1-ERK/AKT axis may confer NSCLC cell lines resistance to erlotinib

    doi:

    Figure Lengend Snippet: Potential mechanism by which NSCLC cells with wt EGFR display resistance to erlotinib. The up-regulation of ErbB ligands (TGF-α, EREG and NRG4) activates EGFR. Activation of RAF1-MEK1-ERK and PKC/SNAI-AKT up-regulates the downstream signaling

    Article Snippet: Immunoblotting of Abs specific for GAPDH (Abmart, 080922), EGFR (Abclonal, A0227), p-EGFR (Santa cruz, SC-12351, pY1173), p-EGFR (Epitomics, #1139-S, pY1086), AKT (Santa Cruz, sc-8312), p-AKT (Santa Cruz, SC-7985-R, pS473), ERK (Abclonal, A0228) and p-ERK (Cell signaling, #9106S, pT202/204) were detected using HRP-conjugated anti-mouse (Promega) or anti-rabbit (Promega) and visualized by chemiluminescence detection system (Millipore, WBKLS0500).

    Techniques: Activation Assay

    The activation status of EGFR/ERK/AKT in 3 NSCLC cell lines. U1752, Calu-6 and NCI-H292 cells were applied to western blotting for EGFR, p-EGFR (Y1173), p-EGFR (Y1086), ERK, p-ERK (T202/204), AKT, p-AKT (S473). GAPDH was used as input control.

    Journal: International Journal of Clinical and Experimental Pathology

    Article Title: RAF1-MEK1-ERK/AKT axis may confer NSCLC cell lines resistance to erlotinib

    doi:

    Figure Lengend Snippet: The activation status of EGFR/ERK/AKT in 3 NSCLC cell lines. U1752, Calu-6 and NCI-H292 cells were applied to western blotting for EGFR, p-EGFR (Y1173), p-EGFR (Y1086), ERK, p-ERK (T202/204), AKT, p-AKT (S473). GAPDH was used as input control.

    Article Snippet: Immunoblotting of Abs specific for GAPDH (Abmart, 080922), EGFR (Abclonal, A0227), p-EGFR (Santa cruz, SC-12351, pY1173), p-EGFR (Epitomics, #1139-S, pY1086), AKT (Santa Cruz, sc-8312), p-AKT (Santa Cruz, SC-7985-R, pS473), ERK (Abclonal, A0228) and p-ERK (Cell signaling, #9106S, pT202/204) were detected using HRP-conjugated anti-mouse (Promega) or anti-rabbit (Promega) and visualized by chemiluminescence detection system (Millipore, WBKLS0500).

    Techniques: Activation Assay, Western Blot

    a Extended dosing study investigating seven i.v. weekly administrations of an efficacious dose (3 mg/kg) and a less-efficacious (0.3 mg/kg) dose of RG7116 in FaDu xenograft mice (FaDu_008). RG7116 given as a three-weekly cycle (two doses in total) was also investigated. b Dose-dependent efficacy up to Day 39 was seen as in the previous study and tumor growth inhibition with 3 mg/kg RG7116 given as a three-weekly cycle was similar to weekly dosing. Mice in the 0.3 mg/kg group were rechallenged ( black arrow ) with 5 mg/kg on Day 39 resulting in tumor growth inhibition for two further assessments; however, tumor regrowth was observed in all dosing groups from Day 50. c RG7116 trough concentrations from the first to third administrations again showed accumulation only with the higher dose. Inhibition of HER3 ( d ) and AKT ( e ) phosphorylation was also seen with weekly dosing at the efficacious dose (3 mg/kg) but not with the lower dose (0.3 mg/kg). Following a single 3 mg/kg dose (representing a three-weekly schedule), initial inhibition of HER3 phosphorylation was seen to diminish by Day 14 and 21. f Upregulation of HER1 (~2.1-fold) and HER2 (~1.3-fold) mRNA was seen 96 h after FaDu xenograft mice ( n = 5) were administered 1.0 mg/kg RG7116 in a separate study, and this was associated with upregulation of HER1 and HER2 protein. g To compare the single animals, 20 µg total protein lysate was loaded per lane (lanes 101–110 are vehicle and 201–210 are the RG7116-treated animals). At Day 52, inhibition of HER3 phosphorylation was maintained in RG7116-treated mice, and expressed HER1 was seen to be phosphorylated compared to vehicle control. HER2 and pHER2 were not changed (data not shown). SEM standard error of the mean, SD standard deviation

    Journal: Cancer Chemotherapy and Pharmacology

    Article Title: Preclinical pharmacokinetics, pharmacodynamics, and efficacy of RG7116: a novel humanized, glycoengineered anti-HER3 antibody

    doi: 10.1007/s00280-015-2697-8

    Figure Lengend Snippet: a Extended dosing study investigating seven i.v. weekly administrations of an efficacious dose (3 mg/kg) and a less-efficacious (0.3 mg/kg) dose of RG7116 in FaDu xenograft mice (FaDu_008). RG7116 given as a three-weekly cycle (two doses in total) was also investigated. b Dose-dependent efficacy up to Day 39 was seen as in the previous study and tumor growth inhibition with 3 mg/kg RG7116 given as a three-weekly cycle was similar to weekly dosing. Mice in the 0.3 mg/kg group were rechallenged ( black arrow ) with 5 mg/kg on Day 39 resulting in tumor growth inhibition for two further assessments; however, tumor regrowth was observed in all dosing groups from Day 50. c RG7116 trough concentrations from the first to third administrations again showed accumulation only with the higher dose. Inhibition of HER3 ( d ) and AKT ( e ) phosphorylation was also seen with weekly dosing at the efficacious dose (3 mg/kg) but not with the lower dose (0.3 mg/kg). Following a single 3 mg/kg dose (representing a three-weekly schedule), initial inhibition of HER3 phosphorylation was seen to diminish by Day 14 and 21. f Upregulation of HER1 (~2.1-fold) and HER2 (~1.3-fold) mRNA was seen 96 h after FaDu xenograft mice ( n = 5) were administered 1.0 mg/kg RG7116 in a separate study, and this was associated with upregulation of HER1 and HER2 protein. g To compare the single animals, 20 µg total protein lysate was loaded per lane (lanes 101–110 are vehicle and 201–210 are the RG7116-treated animals). At Day 52, inhibition of HER3 phosphorylation was maintained in RG7116-treated mice, and expressed HER1 was seen to be phosphorylated compared to vehicle control. HER2 and pHER2 were not changed (data not shown). SEM standard error of the mean, SD standard deviation

    Article Snippet: Western Blot analyses Tissue was immediately lysed using Triton Lysis Buffer (1 % Triton-X-100; 10 µg/mL aprotinin; 0.4 mM orthovanadate; 1 mM phenylmethylsulfonyl fluoride), and lysates were denatured in NuPAGE Sample Reducing Agent at 70 °C for 10 min. SDS–PAGE and Western blotting were conducted as described previously [ ] using 20 μg protein per lane measured using a bicinchoninic acid assay and antibodies specific for HER1 (Upstate/Millipore, #06-847), HER2 (Dako, #A485), HER3 (clone C-17, Santa Cruz, #sc-285), phosphorylated HER1 (pHER1, clone ID Y39; Epitomics/Abcam, #ab32086), or pHER3 (clone 21D3 [Tyr1289 ], Cell Signaling Technologies, #4791).

    Techniques: Mouse Assay, Inhibition, Standard Deviation

    Binding specificity of anti-EGFR aptamers. The N62 pool and aptamers E03, E04, and E07 were assayed in triplicate by filtration for binding to hEGFR, mEGFR, hErbB2, and hIgG1. Average values and standard deviations are shown. Binding assays were carried out either in the absence (left) or presence (right) of DTT. A no protein control was also carried through the procedure. Percent binding was relative to the total RNA added.

    Journal: PLoS ONE

    Article Title: Inhibition of Cell Proliferation by an Anti-EGFR Aptamer

    doi: 10.1371/journal.pone.0020299

    Figure Lengend Snippet: Binding specificity of anti-EGFR aptamers. The N62 pool and aptamers E03, E04, and E07 were assayed in triplicate by filtration for binding to hEGFR, mEGFR, hErbB2, and hIgG1. Average values and standard deviations are shown. Binding assays were carried out either in the absence (left) or presence (right) of DTT. A no protein control was also carried through the procedure. Percent binding was relative to the total RNA added.

    Article Snippet: About 2 nmoles RNA and 90 pmoles recombinant human EGFR-Fc (hEGFR) fusion protein (R & D Systems, Minneapolis, MN) were used for each round of selection in a reaction volume of 100 µL.

    Techniques: Binding Assay, Filtration