egfr Epitomics Search Results


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  • 88
    Bethyl c 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.
    C Terminal Epitope Egfr, supplied by Bethyl, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    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: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Mimotopes egfr epitopes
    <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 Epitopes, supplied by Mimotopes, used in various techniques. Bioz Stars score: 86/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Epitomics egfr epitomics antibodies
    <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 Epitomics Antibodies, supplied by Epitomics, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Epitope Biotech immunogenic egfr encoded ctl epitope
    <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.
    Immunogenic Egfr Encoded Ctl Epitope, supplied by Epitope Biotech, used in various techniques. Bioz Stars score: 85/100, based on 5 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

    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