phospho egfr tyr1068  (Cell Signaling Technology Inc)

 
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    Name:
    Phospho EGF Receptor Tyr1068 Antibody
    Description:
    The epidermal growth factor EGF receptor is a transmembrane tyrosine kinase that belongs to the HER ErbB protein family Ligand binding results in receptor dimerization autophosphorylation activation of downstream signaling internalization and lysosomal degradation 1 2 Phosphorylation of EGF receptor EGFR at Tyr845 in the kinase domain is implicated in stabilizing the activation loop maintaining the active state enzyme and providing a binding surface for substrate proteins 3 4 c Src is involved in phosphorylation of EGFR at Tyr845 5 The SH2 domain of PLCγ binds at phospho Tyr992 resulting in activation of PLCγ mediated downstream signaling 6 Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c Cbl leading to receptor ubiquitination and degradation following EGFR activation 7 8 The GRB2 adaptor protein binds activated EGFR at phospho Tyr1068 9 A pair of phosphorylated EGFR residues Tyr1148 and Tyr1173 provide a docking site for the Shc scaffold protein with both sites involved in MAP kinase signaling activation 2 Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity EGFR carboxy terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation 10
    Catalog Number:
    2234
    Price:
    None
    Category:
    Primary Antibodies
    Source:
    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1068 of human EGF receptor. Antibodies are purified by protein A and peptide affinity chromatography.
    Reactivity:
    Human Mouse Rat
    Applications:
    Western Blot, Immunohistochemistry
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    Structured Review

    Cell Signaling Technology Inc phospho egfr tyr1068
    The knockdown of GOLPH3 in T98G cells impairs ligand-induced activation of EGFR. ( A ) The indicated cells grown in 6-well plates were incubated with EGF for the indicated periods of time. Detergent-soluble extracts were prepared from cells and samples of proteins were analyzed by SDS-PAGE followed by immunoblotting using antibodies to detect the proteins indicated on the right, including antibodies specific to EGFR phosphorylated either at <t>Tyr1068</t> (p-EGFR-Y1068) or Tyr1086 (p-EGFR-Y1086). The immunoblot signal of anti-β-actin was used as a loading control. The position of molecular mass markers is indicated on the left. ( B , C ) Densitometry quantification of the ratio between the immunoblot signals for p-EGFR-Y1068 and total EGFR ( B ) or p-EGFR-Y1086 and total EGFR ( C ) from images as those shown in A. Bars represent the mean ± standard deviation ( n = 3; * p
    The epidermal growth factor EGF receptor is a transmembrane tyrosine kinase that belongs to the HER ErbB protein family Ligand binding results in receptor dimerization autophosphorylation activation of downstream signaling internalization and lysosomal degradation 1 2 Phosphorylation of EGF receptor EGFR at Tyr845 in the kinase domain is implicated in stabilizing the activation loop maintaining the active state enzyme and providing a binding surface for substrate proteins 3 4 c Src is involved in phosphorylation of EGFR at Tyr845 5 The SH2 domain of PLCγ binds at phospho Tyr992 resulting in activation of PLCγ mediated downstream signaling 6 Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c Cbl leading to receptor ubiquitination and degradation following EGFR activation 7 8 The GRB2 adaptor protein binds activated EGFR at phospho Tyr1068 9 A pair of phosphorylated EGFR residues Tyr1148 and Tyr1173 provide a docking site for the Shc scaffold protein with both sites involved in MAP kinase signaling activation 2 Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity EGFR carboxy terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation 10
    https://www.bioz.com/result/phospho egfr tyr1068/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phospho egfr tyr1068 - by Bioz Stars, 2021-05
    95/100 stars

    Images

    1) Product Images from "GOLPH3 Regulates EGFR in T98G Glioblastoma Cells by Modulating Its Glycosylation and Ubiquitylation"

    Article Title: GOLPH3 Regulates EGFR in T98G Glioblastoma Cells by Modulating Its Glycosylation and Ubiquitylation

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms21228880

    The knockdown of GOLPH3 in T98G cells impairs ligand-induced activation of EGFR. ( A ) The indicated cells grown in 6-well plates were incubated with EGF for the indicated periods of time. Detergent-soluble extracts were prepared from cells and samples of proteins were analyzed by SDS-PAGE followed by immunoblotting using antibodies to detect the proteins indicated on the right, including antibodies specific to EGFR phosphorylated either at Tyr1068 (p-EGFR-Y1068) or Tyr1086 (p-EGFR-Y1086). The immunoblot signal of anti-β-actin was used as a loading control. The position of molecular mass markers is indicated on the left. ( B , C ) Densitometry quantification of the ratio between the immunoblot signals for p-EGFR-Y1068 and total EGFR ( B ) or p-EGFR-Y1086 and total EGFR ( C ) from images as those shown in A. Bars represent the mean ± standard deviation ( n = 3; * p
    Figure Legend Snippet: The knockdown of GOLPH3 in T98G cells impairs ligand-induced activation of EGFR. ( A ) The indicated cells grown in 6-well plates were incubated with EGF for the indicated periods of time. Detergent-soluble extracts were prepared from cells and samples of proteins were analyzed by SDS-PAGE followed by immunoblotting using antibodies to detect the proteins indicated on the right, including antibodies specific to EGFR phosphorylated either at Tyr1068 (p-EGFR-Y1068) or Tyr1086 (p-EGFR-Y1086). The immunoblot signal of anti-β-actin was used as a loading control. The position of molecular mass markers is indicated on the left. ( B , C ) Densitometry quantification of the ratio between the immunoblot signals for p-EGFR-Y1068 and total EGFR ( B ) or p-EGFR-Y1086 and total EGFR ( C ) from images as those shown in A. Bars represent the mean ± standard deviation ( n = 3; * p

    Techniques Used: Activation Assay, Incubation, SDS Page, Standard Deviation

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    Article Snippet: .. Cell lysates were analyzed by standard Western Blot using antibodies against (Tyr1068)-phosphorylated EGFR (#3777, Cell signaling technologies, USA) and Tubulin (rabbit anti-tubulin; #T3526, Sigma). .. For the visualization of EGF-functionalized nanophosphors uptake, VE11 cells were seeded into Lab-Tek chambered coverslips (Thermo Scientific, USA) to a final density of 1×104 cells/cm2 .

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    Cell Signaling Technology Inc mouse anti phospho egfr
    Apoptosis in human GBM neurospheres containing GSCs treated with cetuximab-IONPs Transport of <t>EGFR</t> to the cytoskeletal structures . Neurospheres were treated with free IONPs (0.2 mg/ml), cetuximab-IONPs (0.2 mg/ml), control vehicle, or cetuximab alone (50 μg/ml) and expression of apoptotic proteins was evaluated by Western blotting. Elevated levels of cleaved caspase 3 and cleaved PARP were found in neurospheres N08-74 and N08-30 after treatment with cetuximab-IONPs for 3 (A, left) and in neurospheres N08-74 for 14 hs (A, right). Treatment with cetuximab-IONPs was most effective in inducing cleavage of caspase 3 and PARP although some caspase 3 cleavage was also induced by free IONPs in N08-30. In neurospheres N08-1002, induction of caspase 3 and PARP cleavage, and decreased phosphorylation of ERK 44/42 was found after 3 h treatment with cetuximab-IONPs and cetuximab alone, both in the presence and absence of EGF and FGF, caspase 3 was used as a control (B, top). Treatment with cetuximab-IONPs (but not the control conjugated antibody) increased cleavage of PARP in neurospheres N08-1002 whereas no cleavage was observed in NHPC (B, bottom). (C) N08-30 neurospheres were treated as above for 5 hs, lysates were subcellularly fractionated, and analyzed by Western blotting. Elevated levels of <t>wtEGFR</t> were found in the cytoskeletal fraction after cells were treated with cetuximab-IONPs. (D) U87MG and U87MGwtEGFR human GBM cell lines were treated with free IONPs, cetuximab-IONPs, or cetuximab alone. Apoptosis, as indicated by activation of caspase 3 cleavage, was seen only in the U87MGwtEGFR cell line treated with cetuximab-IONPs.
    Mouse Anti Phospho Egfr, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse anti phospho egfr/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    99
    Cell Signaling Technology Inc anti phospho egfr
    NTS autocrine and paracrine regulation enhanced <t>EGFR,</t> <t>HER2,</t> and HER3 basal expression and activation in human breast cancer cell lines (A) HER2 and HER3 immunohistochemistry performed on paraffin embedded tumors from mice xenograph with MCF-7, NTS-l or NTS-h. 200X magnification and computer enlargement of specific areas. (B) Breast cancer cells MCF-7, NTS-l and NTS-h, with the histograms representing intensity-based quantification of Western blot bands of basal total protein, EGFR, HER2, and HER3, using Morpho Expert software (Explora Nova, France). Values are expressed as the percentage of the control MCF-7 cells and are the mean ± SEM of 5 to 7 independent experiments. (C) Representative western blot analyses of EGFR, HER2, HER3 and ERK 1/2 total protein from MCF-7 and NTS-l cells treated with 5x10 −6 M SR 48692. (D) EGFR, HER2, and HER3 immunolabeling in MCF-7 and NTS-l cells treated after 48h of seeding. (E) Breast cancer cells MCF-7 and NTS-l, with the histograms representing intensity-based quantification of Western blot bands of phosphorylated protein, EGFR, HER2, and HER3. Values are expressed as the percentage of the control MCF-7 cells and are the mean ± SEM of 5 to 7 independent experiments. (F) Representative western blot analyses of Phospho EGFR, phosphoHER2, and Phospho HER3 protein from MCF-7 and NTS-l cells treated with DMSO or 5x10 −6 M SR 48692 for 48h.
    Anti Phospho Egfr, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho egfr/product/Cell Signaling Technology Inc
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti phospho egfr - by Bioz Stars, 2021-05
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    Image Search Results


    Apoptosis in human GBM neurospheres containing GSCs treated with cetuximab-IONPs Transport of EGFR to the cytoskeletal structures . Neurospheres were treated with free IONPs (0.2 mg/ml), cetuximab-IONPs (0.2 mg/ml), control vehicle, or cetuximab alone (50 μg/ml) and expression of apoptotic proteins was evaluated by Western blotting. Elevated levels of cleaved caspase 3 and cleaved PARP were found in neurospheres N08-74 and N08-30 after treatment with cetuximab-IONPs for 3 (A, left) and in neurospheres N08-74 for 14 hs (A, right). Treatment with cetuximab-IONPs was most effective in inducing cleavage of caspase 3 and PARP although some caspase 3 cleavage was also induced by free IONPs in N08-30. In neurospheres N08-1002, induction of caspase 3 and PARP cleavage, and decreased phosphorylation of ERK 44/42 was found after 3 h treatment with cetuximab-IONPs and cetuximab alone, both in the presence and absence of EGF and FGF, caspase 3 was used as a control (B, top). Treatment with cetuximab-IONPs (but not the control conjugated antibody) increased cleavage of PARP in neurospheres N08-1002 whereas no cleavage was observed in NHPC (B, bottom). (C) N08-30 neurospheres were treated as above for 5 hs, lysates were subcellularly fractionated, and analyzed by Western blotting. Elevated levels of wtEGFR were found in the cytoskeletal fraction after cells were treated with cetuximab-IONPs. (D) U87MG and U87MGwtEGFR human GBM cell lines were treated with free IONPs, cetuximab-IONPs, or cetuximab alone. Apoptosis, as indicated by activation of caspase 3 cleavage, was seen only in the U87MGwtEGFR cell line treated with cetuximab-IONPs.

    Journal: Oncotarget

    Article Title: Targeted therapy of glioblastoma stem-like cells and tumor non-stem cells using cetuximab-conjugated iron-oxide nanoparticles

    doi:

    Figure Lengend Snippet: Apoptosis in human GBM neurospheres containing GSCs treated with cetuximab-IONPs Transport of EGFR to the cytoskeletal structures . Neurospheres were treated with free IONPs (0.2 mg/ml), cetuximab-IONPs (0.2 mg/ml), control vehicle, or cetuximab alone (50 μg/ml) and expression of apoptotic proteins was evaluated by Western blotting. Elevated levels of cleaved caspase 3 and cleaved PARP were found in neurospheres N08-74 and N08-30 after treatment with cetuximab-IONPs for 3 (A, left) and in neurospheres N08-74 for 14 hs (A, right). Treatment with cetuximab-IONPs was most effective in inducing cleavage of caspase 3 and PARP although some caspase 3 cleavage was also induced by free IONPs in N08-30. In neurospheres N08-1002, induction of caspase 3 and PARP cleavage, and decreased phosphorylation of ERK 44/42 was found after 3 h treatment with cetuximab-IONPs and cetuximab alone, both in the presence and absence of EGF and FGF, caspase 3 was used as a control (B, top). Treatment with cetuximab-IONPs (but not the control conjugated antibody) increased cleavage of PARP in neurospheres N08-1002 whereas no cleavage was observed in NHPC (B, bottom). (C) N08-30 neurospheres were treated as above for 5 hs, lysates were subcellularly fractionated, and analyzed by Western blotting. Elevated levels of wtEGFR were found in the cytoskeletal fraction after cells were treated with cetuximab-IONPs. (D) U87MG and U87MGwtEGFR human GBM cell lines were treated with free IONPs, cetuximab-IONPs, or cetuximab alone. Apoptosis, as indicated by activation of caspase 3 cleavage, was seen only in the U87MGwtEGFR cell line treated with cetuximab-IONPs.

    Article Snippet: Primary antibodies used were: mouse anti-β-actin (1:1000, Sigma); rabbit anti-cleaved caspase 3 (1:1000, CellSignaling); rabbit anti-caspase 3 (1:1000, CellSignaling); rabbit anti-cleaved caspase 9 (1:1000, CellSignaling); rabbit anti-caspase 9 (1:1000, CellSignaling); rabbit anti-CD133 (1:1000, CellSignaling); rabbit anti-EGFRvIII (1:1000, GenScript Corp.); mouse anti-phospho-EGFR (Tyr1068, 1:1000, CellSignalling); rabbit anti-wtEGFR (1:1000, Santa Cruz Biotechnology); rabbit anti-phospho-ERK44/42 (1:1000, CellSignaling); rabbit anti-ERK44/42 (1:1000, CellSignaling); mouse anti-GFAP (1:1000, CellSignaling); rabbit anti-Nanog (1:1000, CellSignaling); mouse anti-Nestin (1:500, Abcam); rabbit anti-Olig 2 (1:100, Milipore); rabbit anti-cleaved PARP (1:1000, CellSignaling); rabbit anti-PARP (1:1000, CellSignaling); rabbit anti-Sox2 (1:1000, CellSignaling); mouse anti-β3-tubulin (1:1000, Milipore); and rabbit anti-Vimentin (1:1000, CellSignaling).

    Techniques: Expressing, Western Blot, Activation Assay

    Therapeutic activity of combined inhibition of EGFR, HER3, and the PI3K-Akt pathway in TNBC preclinical models

    Journal: Science signaling

    Article Title: Antagonism of EGFR and HER3 Enhances the Response to Inhibitors of the PI3K-Akt Pathway in Triple-Negative Breast Cancer

    doi: 10.1126/scisignal.2005125

    Figure Lengend Snippet: Therapeutic activity of combined inhibition of EGFR, HER3, and the PI3K-Akt pathway in TNBC preclinical models

    Article Snippet: Membranes were blocked for 1 hour in 5% nonfat dry milk in tris-buffered saline (TBS)–Tween and then hybridized using the following primary antibodies in 5% bovine serum albumin (BSA) TBS-Tween: phospho-Akt (Ser473 ), phospho-Akt (Thr308 ), Akt, phospho-S6 (Ser 240/4 ), phospho-S6 (Ser 235/6 ), S6, phospho-ERK (Thr202 /Tyr204 ), ERK, phospho-EGFR (Tyr1068 ), EGFR, phospho-HER3 (Tyr1289 ), and HER3 (1:500 to 1:1000; Cell Signaling Technology). b-Actin was used as a loading control (1:5000; Sigma), also in 5% BSA TBS-Tween.

    Techniques: Activity Assay, Inhibition

    HER3 expression and response to anti-EGFR therapy in TNBC patients

    Journal: Science signaling

    Article Title: Antagonism of EGFR and HER3 Enhances the Response to Inhibitors of the PI3K-Akt Pathway in Triple-Negative Breast Cancer

    doi: 10.1126/scisignal.2005125

    Figure Lengend Snippet: HER3 expression and response to anti-EGFR therapy in TNBC patients

    Article Snippet: Membranes were blocked for 1 hour in 5% nonfat dry milk in tris-buffered saline (TBS)–Tween and then hybridized using the following primary antibodies in 5% bovine serum albumin (BSA) TBS-Tween: phospho-Akt (Ser473 ), phospho-Akt (Thr308 ), Akt, phospho-S6 (Ser 240/4 ), phospho-S6 (Ser 235/6 ), S6, phospho-ERK (Thr202 /Tyr204 ), ERK, phospho-EGFR (Tyr1068 ), EGFR, phospho-HER3 (Tyr1289 ), and HER3 (1:500 to 1:1000; Cell Signaling Technology). b-Actin was used as a loading control (1:5000; Sigma), also in 5% BSA TBS-Tween.

    Techniques: Expressing

    NTS autocrine and paracrine regulation enhanced EGFR, HER2, and HER3 basal expression and activation in human breast cancer cell lines (A) HER2 and HER3 immunohistochemistry performed on paraffin embedded tumors from mice xenograph with MCF-7, NTS-l or NTS-h. 200X magnification and computer enlargement of specific areas. (B) Breast cancer cells MCF-7, NTS-l and NTS-h, with the histograms representing intensity-based quantification of Western blot bands of basal total protein, EGFR, HER2, and HER3, using Morpho Expert software (Explora Nova, France). Values are expressed as the percentage of the control MCF-7 cells and are the mean ± SEM of 5 to 7 independent experiments. (C) Representative western blot analyses of EGFR, HER2, HER3 and ERK 1/2 total protein from MCF-7 and NTS-l cells treated with 5x10 −6 M SR 48692. (D) EGFR, HER2, and HER3 immunolabeling in MCF-7 and NTS-l cells treated after 48h of seeding. (E) Breast cancer cells MCF-7 and NTS-l, with the histograms representing intensity-based quantification of Western blot bands of phosphorylated protein, EGFR, HER2, and HER3. Values are expressed as the percentage of the control MCF-7 cells and are the mean ± SEM of 5 to 7 independent experiments. (F) Representative western blot analyses of Phospho EGFR, phosphoHER2, and Phospho HER3 protein from MCF-7 and NTS-l cells treated with DMSO or 5x10 −6 M SR 48692 for 48h.

    Journal: Oncotarget

    Article Title: Activation of EGFR, HER2 and HER3 by neurotensin/neurotensin receptor 1 renders breast tumors aggressive yet highly responsive to lapatinib and metformin in mice

    doi:

    Figure Lengend Snippet: NTS autocrine and paracrine regulation enhanced EGFR, HER2, and HER3 basal expression and activation in human breast cancer cell lines (A) HER2 and HER3 immunohistochemistry performed on paraffin embedded tumors from mice xenograph with MCF-7, NTS-l or NTS-h. 200X magnification and computer enlargement of specific areas. (B) Breast cancer cells MCF-7, NTS-l and NTS-h, with the histograms representing intensity-based quantification of Western blot bands of basal total protein, EGFR, HER2, and HER3, using Morpho Expert software (Explora Nova, France). Values are expressed as the percentage of the control MCF-7 cells and are the mean ± SEM of 5 to 7 independent experiments. (C) Representative western blot analyses of EGFR, HER2, HER3 and ERK 1/2 total protein from MCF-7 and NTS-l cells treated with 5x10 −6 M SR 48692. (D) EGFR, HER2, and HER3 immunolabeling in MCF-7 and NTS-l cells treated after 48h of seeding. (E) Breast cancer cells MCF-7 and NTS-l, with the histograms representing intensity-based quantification of Western blot bands of phosphorylated protein, EGFR, HER2, and HER3. Values are expressed as the percentage of the control MCF-7 cells and are the mean ± SEM of 5 to 7 independent experiments. (F) Representative western blot analyses of Phospho EGFR, phosphoHER2, and Phospho HER3 protein from MCF-7 and NTS-l cells treated with DMSO or 5x10 −6 M SR 48692 for 48h.

    Article Snippet: Total anti-EGFR (1:500), anti-phospho-EGFR (1:500), anti-phospho-HER2 (1:500), anti-HER3 (1:2000), anti-phospho-HER3 (1:1000), anti-ERK 1/2 (1:2000) were from Cell Signaling Technology®.

    Techniques: Expressing, Activation Assay, Immunohistochemistry, Mouse Assay, Western Blot, Software, Immunolabeling

    NTS/NTSR1 expressing tumors response to EGFR/HER2 inhibitor treatments (A) NTS-h cells were inoculated in the left mammary gland of the mice. Here is shown an example of a mouse from each group after 23 days of treatment. (B) Tumor growths generated by NTS-h cells treated for 23 days with sesame oil 6% DMSO, or 75 mg/kg lapatinib, or 200 mg/kg metformin, or both. At day one, 7 mice per group were randomized on tumors size reaching approximately 95 mm 3 .

    Journal: Oncotarget

    Article Title: Activation of EGFR, HER2 and HER3 by neurotensin/neurotensin receptor 1 renders breast tumors aggressive yet highly responsive to lapatinib and metformin in mice

    doi:

    Figure Lengend Snippet: NTS/NTSR1 expressing tumors response to EGFR/HER2 inhibitor treatments (A) NTS-h cells were inoculated in the left mammary gland of the mice. Here is shown an example of a mouse from each group after 23 days of treatment. (B) Tumor growths generated by NTS-h cells treated for 23 days with sesame oil 6% DMSO, or 75 mg/kg lapatinib, or 200 mg/kg metformin, or both. At day one, 7 mice per group were randomized on tumors size reaching approximately 95 mm 3 .

    Article Snippet: Total anti-EGFR (1:500), anti-phospho-EGFR (1:500), anti-phospho-HER2 (1:500), anti-HER3 (1:2000), anti-phospho-HER3 (1:1000), anti-ERK 1/2 (1:2000) were from Cell Signaling Technology®.

    Techniques: Expressing, Mouse Assay, Generated

    Synergy between NTS and EGF to activate EGFR, HER2, and HER3 (A) Breast cancer cells NTS-l or MCF-7, with the histograms representing intensity- based quantification of Western blot bands of phosphorylated protein, EGFR, HER2, and HER3 treated for 10 min with 10ng/ml EGF. Values are expressed as the percentage of the EGF treated MCF-7 cells and are the mean ± SEM of 5 independent experiments. (B) Representative Western blot analyses of phosphoEGFR, phosphoHER2, phosphoHER3 and actin from MCF-7 and NTS-l cells treated or not with 10ng/ml EFG for 10 min.

    Journal: Oncotarget

    Article Title: Activation of EGFR, HER2 and HER3 by neurotensin/neurotensin receptor 1 renders breast tumors aggressive yet highly responsive to lapatinib and metformin in mice

    doi:

    Figure Lengend Snippet: Synergy between NTS and EGF to activate EGFR, HER2, and HER3 (A) Breast cancer cells NTS-l or MCF-7, with the histograms representing intensity- based quantification of Western blot bands of phosphorylated protein, EGFR, HER2, and HER3 treated for 10 min with 10ng/ml EGF. Values are expressed as the percentage of the EGF treated MCF-7 cells and are the mean ± SEM of 5 independent experiments. (B) Representative Western blot analyses of phosphoEGFR, phosphoHER2, phosphoHER3 and actin from MCF-7 and NTS-l cells treated or not with 10ng/ml EFG for 10 min.

    Article Snippet: Total anti-EGFR (1:500), anti-phospho-EGFR (1:500), anti-phospho-HER2 (1:500), anti-HER3 (1:2000), anti-phospho-HER3 (1:1000), anti-ERK 1/2 (1:2000) were from Cell Signaling Technology®.

    Techniques: Western Blot

    Mig-6 prompts H1299, A549 sensitivity to gefitinib by regulating EGFR/ERK pathway. A. H1299 and A549 cells were transfected with pcDNA3 vector-, or pcDNA3-Mig-6 over-expression vector-, for 24 h, then 10 μM gefitinib was added, cell proliferation rates were detected by CCK-8 assay for five days; B. H1299 and A549 cells were transfected with pcDNA3 vector-, or pcDNA3-Mig-6 over-expression vector-, for 24 h, then 10 μM gefitinib were added another 24 h before detected. The percentage of apoptotic cells is expressed as the mean + SD of three independent experiments. * P

    Journal: International Journal of Clinical and Experimental Pathology

    Article Title: Mig-6 overcomes gefitinib resistance by inhibiting EGFR/ERK pathway in non-small cell lung cancer cell lines

    doi:

    Figure Lengend Snippet: Mig-6 prompts H1299, A549 sensitivity to gefitinib by regulating EGFR/ERK pathway. A. H1299 and A549 cells were transfected with pcDNA3 vector-, or pcDNA3-Mig-6 over-expression vector-, for 24 h, then 10 μM gefitinib was added, cell proliferation rates were detected by CCK-8 assay for five days; B. H1299 and A549 cells were transfected with pcDNA3 vector-, or pcDNA3-Mig-6 over-expression vector-, for 24 h, then 10 μM gefitinib were added another 24 h before detected. The percentage of apoptotic cells is expressed as the mean + SD of three independent experiments. * P

    Article Snippet: After transferring, the polyvinylidene fluoride (PVDF) membranes (Millipore, Billerica, MA, USA) were incubated overnight at 4°C with the following antibodies Mig-6 (1: 1000; protein tech), β-actin (1: 000; Santa Cruz Biotechnology, Santa Cruz, CA), anti-phospho-ERK, anti-phospho-EGFR (1: 1000; Cell Signaling Technology, Danvers, MA).

    Techniques: Transfection, Plasmid Preparation, Over Expression, CCK-8 Assay

    Mig-6 reverses gefitinib-resistance through inhibiting EGFR/ERK pathway. A. PC9/AB11 was transfected with PC (pcDNA3 vector) or Mig-6, after 24 h, cells were treated with 1 μM gefitinib, cell proliferation rates were measured by CCK8 assay 24 h later; B. PC9/AB11 was transfected with PC (pcDNA3 vector) or Mig-6, after 24 h, cells were treated with 1 μM gefitinib, levels of p-EGFR and p-ERK were measured by western blot 24 h later.

    Journal: International Journal of Clinical and Experimental Pathology

    Article Title: Mig-6 overcomes gefitinib resistance by inhibiting EGFR/ERK pathway in non-small cell lung cancer cell lines

    doi:

    Figure Lengend Snippet: Mig-6 reverses gefitinib-resistance through inhibiting EGFR/ERK pathway. A. PC9/AB11 was transfected with PC (pcDNA3 vector) or Mig-6, after 24 h, cells were treated with 1 μM gefitinib, cell proliferation rates were measured by CCK8 assay 24 h later; B. PC9/AB11 was transfected with PC (pcDNA3 vector) or Mig-6, after 24 h, cells were treated with 1 μM gefitinib, levels of p-EGFR and p-ERK were measured by western blot 24 h later.

    Article Snippet: After transferring, the polyvinylidene fluoride (PVDF) membranes (Millipore, Billerica, MA, USA) were incubated overnight at 4°C with the following antibodies Mig-6 (1: 1000; protein tech), β-actin (1: 000; Santa Cruz Biotechnology, Santa Cruz, CA), anti-phospho-ERK, anti-phospho-EGFR (1: 1000; Cell Signaling Technology, Danvers, MA).

    Techniques: Transfection, Plasmid Preparation, CCK-8 Assay, Western Blot