Structured Review

Epitomics egfr
Egfr, supplied by Epitomics, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/egfr/product/Epitomics
Average 93 stars, based on 7 article reviews
Price from $9.99 to $1999.99
egfr - by Bioz Stars, 2020-01
93/100 stars

Images

Related Articles

Immunocytochemistry:

Article Title: Estrogen switches pure mucinous breast cancer to invasive lobular carcinoma with mucinous features
Article Snippet: Paragraph title: Immunocytochemistry (ICC) and antibodies ... Antibodies were: ER (Neomarkers, SP1) 1:100, PR (DAKO, 1294) 1:500, AR (Upstate, PG-21) 1:35, BrdU (BD Biosciences) 1:50, Her2 (Neomarkers, SP3) 1:50, CK5 (Novacastra, XM26) 1:100, CD10 (Epitomics, EP2998) 1:100, CK14 (Neomarkers) 1:200, CK18 (Calbiochem) 1:400, CK8/18 (Novocastra, 5D3) 1:100, CD117 (DAKO) 1:400, CD44 (Neomarkers 156-3C11) 1:200, EGFR (Epitomics E114) 1:12, E-Cadherin (DAKO) 1:25, p63 (Epitomics Y289) 1:250, Mammaglobin A (Abcam, 304-1A5) prediluted, Chromograinin A (Abcam) 1:60, Synaptophysin (Abcam) 1:100, Vimentin (Epitomics, SP20) 1:200, Vimentin (Abcam, V9) 1:50, α-SMA (Epitomics, E184) 1:400, p120 catenin (Epitomics, #2806) 1:250.

Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 79
    Epitomics antibody against egfr
    MCF‐7/TAM cells possessed increased levels of ER‐α36 and <t>EGFR,</t> together with reduced level of <t>ER‐α66.</t> (A). Western blotting analysis of the protein levels of ER‐α36, EGFR, ER‐α66, phosphorylated ERK1/2 and total ERK1/2 in MCF‐7 cells and MCF‐7/TAM cells. β‐actin was used as the loading control. All experiments were repeated at least three times, and the representative results are shown. (B C). Relative mRNA level of EGFR and ER‐α66 in MCF‐7/TAM cells was determined by real time qPCR. β‐actin gene was used as an endogenous control for normalization. Results showed are means ± SEM of three independent reactions.
    Antibody Against Egfr, supplied by Epitomics, used in various techniques. Bioz Stars score: 79/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/antibody against egfr/product/Epitomics
    Average 79 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    antibody against egfr - by Bioz Stars, 2020-01
    79/100 stars
      Buy from Supplier

    78
    Epitomics egfr pan rabbit monoclonal antibody
    SB431542, but not SIS, inhibited <t>EGFR</t> signaling in WT COCs. A, Egfr mRNA expression in COCs treated with DMSO, SB431542, or SIS for 20 h. B, Western blot analysis of EGFR, p-SMAD2, and <t>β-actin</t> (ACTB) in the same experimental groups as stated in panel A 20 h after culture. C, Changes of the levels of p-MAPK3/1 in the same experimental groups as stated in panel A after the initial 20-h culture and then treated with or without (control) AREG for 30 min. Groups indicated with different letters are significantly different, P
    Egfr Pan Rabbit Monoclonal Antibody, 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
    https://www.bioz.com/result/egfr pan rabbit monoclonal antibody/product/Epitomics
    Average 78 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    egfr pan rabbit monoclonal antibody - by Bioz Stars, 2020-01
    78/100 stars
      Buy from Supplier

    79
    Epitomics polyclonal rabbit anti phosho egfr s695
    Distribution of epidermal growth factor and transferrin receptors in control and breast cancer tissue. Representative tissues were stained with (A) monoclonal rabbit <t>anti-phospho-EGFr</t> (pT693); <t>polyclonal</t> rabbit <t>anti-phosho-EGFr</t> (s695) (B) and monoclonal rabbit anti-CD71 (TFRC). (A) Weak staining of both EGFr (pT693) and EGFr (s659) was observed in the control breast tissue in contrast to strong staining observed in the invasive breast carcinoma tissue. (C) Control breast expressing transferrin receptor (red) (i) showed relatively equal amounts of expression in breast cancer (ii). Merged image: nucleus stained with DAPI (blue), EGFr and CD71 (red), β-actin (green). Images were acquired using an Olympus BX61 fluorescence microscope with automated FVII camera. Bar = 200μm, 100μm; x10, x20 magnification respectively.
    Polyclonal Rabbit Anti Phosho Egfr S695, supplied by Epitomics, used in various techniques. Bioz Stars score: 79/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal rabbit anti phosho egfr s695/product/Epitomics
    Average 79 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    polyclonal rabbit anti phosho egfr s695 - by Bioz Stars, 2020-01
    79/100 stars
      Buy from Supplier

    Image Search Results


    MCF‐7/TAM cells possessed increased levels of ER‐α36 and EGFR, together with reduced level of ER‐α66. (A). Western blotting analysis of the protein levels of ER‐α36, EGFR, ER‐α66, phosphorylated ERK1/2 and total ERK1/2 in MCF‐7 cells and MCF‐7/TAM cells. β‐actin was used as the loading control. All experiments were repeated at least three times, and the representative results are shown. (B C). Relative mRNA level of EGFR and ER‐α66 in MCF‐7/TAM cells was determined by real time qPCR. β‐actin gene was used as an endogenous control for normalization. Results showed are means ± SEM of three independent reactions.

    Journal: Molecular Oncology

    Article Title: Estrogen receptor‐α36 is involved in development of acquired tamoxifen resistance via regulating the growth status switch in breast cancer cells), Estrogen receptor‐α36 is involved in development of acquired tamoxifen resistance via regulating the growth status switch in breast cancer cells

    doi: 10.1016/j.molonc.2013.02.001

    Figure Lengend Snippet: MCF‐7/TAM cells possessed increased levels of ER‐α36 and EGFR, together with reduced level of ER‐α66. (A). Western blotting analysis of the protein levels of ER‐α36, EGFR, ER‐α66, phosphorylated ERK1/2 and total ERK1/2 in MCF‐7 cells and MCF‐7/TAM cells. β‐actin was used as the loading control. All experiments were repeated at least three times, and the representative results are shown. (B C). Relative mRNA level of EGFR and ER‐α66 in MCF‐7/TAM cells was determined by real time qPCR. β‐actin gene was used as an endogenous control for normalization. Results showed are means ± SEM of three independent reactions.

    Article Snippet: The antibody against EGFR and ER‐α66 was purchased from Epitomics, Inc. (Burlingame, CA, USA).

    Techniques: Western Blot, Real-time Polymerase Chain Reaction

    Inhibition of ER‐α36 with neutralizing anti‐ER‐α36 antibodies in MCF‐7/ER‐α36‐1 and MCF‐7/TAM cells. (A). MCF‐7/V cells and MCF‐7/ER‐α36‐1 cells were treated with 10 μg/ml anti‐ER‐α36 antibodies or equal control mouse IgG for 4 days. The survived cells were then harvested and the cell lysates were subjected to western blotting analysis. β‐actin was used as the loading control. All experiments were repeated at least three times, and the representative results are shown (B C). The mRNA level of EGFR and ER‐α66 in treated MCF‐7/V and MCF‐7/ER‐α36‐1 cells were analyzed by real time qPCR using β‐actin gene as an endogenous control. Results showed are means ± SEM of three independent reactions. (D). The colony forming efficiency of MCF‐7/ER‐α36‐1 cells treated with 1 μM TAM plus 10 μg/ml anti‐ER‐α36 antibodies or equivalent normal mouse IgG was examined using monolayer colony formation assay. Column: Means of three independent experiments; bars, SEM. (E). MCF‐7/TAM cells were treated with 30 μg/ml anti‐ER‐α36 antibodies or equivalent normal mouse IgG for 10 days. The survived cells were then harvested and the cell lysates were subjected to western blotting analysis. β‐actin was used as the loading control. Untreated parental MCF‐7 cells were used as a control. All experiments were repeated at least three times, and the representative results are shown. (F G). The mRNA level of EGFR and ER‐α66 in treated MCF‐7/TAM cells were analyzed by real time qPCR using β‐actin gene as an endogenous control. Untreated parental MCF‐7 cells were used as a control. Results showed are means ± SEM of three independent reactions. (H). The colony forming efficiency of MCF‐7/TAM cells treated with 1 μM TAM plus 30 μg/ml anti‐ER‐α36 antibodies or equivalent normal mouse IgG was examined using monolayer colony formation assay. Column: means of three independent experiments; bars, SEM.

    Journal: Molecular Oncology

    Article Title: Estrogen receptor‐α36 is involved in development of acquired tamoxifen resistance via regulating the growth status switch in breast cancer cells), Estrogen receptor‐α36 is involved in development of acquired tamoxifen resistance via regulating the growth status switch in breast cancer cells

    doi: 10.1016/j.molonc.2013.02.001

    Figure Lengend Snippet: Inhibition of ER‐α36 with neutralizing anti‐ER‐α36 antibodies in MCF‐7/ER‐α36‐1 and MCF‐7/TAM cells. (A). MCF‐7/V cells and MCF‐7/ER‐α36‐1 cells were treated with 10 μg/ml anti‐ER‐α36 antibodies or equal control mouse IgG for 4 days. The survived cells were then harvested and the cell lysates were subjected to western blotting analysis. β‐actin was used as the loading control. All experiments were repeated at least three times, and the representative results are shown (B C). The mRNA level of EGFR and ER‐α66 in treated MCF‐7/V and MCF‐7/ER‐α36‐1 cells were analyzed by real time qPCR using β‐actin gene as an endogenous control. Results showed are means ± SEM of three independent reactions. (D). The colony forming efficiency of MCF‐7/ER‐α36‐1 cells treated with 1 μM TAM plus 10 μg/ml anti‐ER‐α36 antibodies or equivalent normal mouse IgG was examined using monolayer colony formation assay. Column: Means of three independent experiments; bars, SEM. (E). MCF‐7/TAM cells were treated with 30 μg/ml anti‐ER‐α36 antibodies or equivalent normal mouse IgG for 10 days. The survived cells were then harvested and the cell lysates were subjected to western blotting analysis. β‐actin was used as the loading control. Untreated parental MCF‐7 cells were used as a control. All experiments were repeated at least three times, and the representative results are shown. (F G). The mRNA level of EGFR and ER‐α66 in treated MCF‐7/TAM cells were analyzed by real time qPCR using β‐actin gene as an endogenous control. Untreated parental MCF‐7 cells were used as a control. Results showed are means ± SEM of three independent reactions. (H). The colony forming efficiency of MCF‐7/TAM cells treated with 1 μM TAM plus 30 μg/ml anti‐ER‐α36 antibodies or equivalent normal mouse IgG was examined using monolayer colony formation assay. Column: means of three independent experiments; bars, SEM.

    Article Snippet: The antibody against EGFR and ER‐α66 was purchased from Epitomics, Inc. (Burlingame, CA, USA).

    Techniques: Inhibition, Western Blot, Real-time Polymerase Chain Reaction, Colony Assay

    Overexpressing ER‐α36 in MCF‐7 cells up‐regulated EGFR expression and down‐regulated ER‐α66 expression. (A). Western blotting analysis of the protein levels of ER‐α36, EGFR, ER‐α66, phosphorylated ERK1/2 and total ERK1/2 in MCF‐7/V cells and MCF‐7/ER‐α36 cells. β‐actin was used as the loading control. All experiments were repeated at least three times, and the representative results are shown. (B C). Relative mRNA level of EGFR and ER‐α66 in MCF‐7/ER‐α36 cells was determined by real time qPCR. β‐actin gene was used as an endogenous control for normalization. Results showed are means ± SEM of three independent reactions.

    Journal: Molecular Oncology

    Article Title: Estrogen receptor‐α36 is involved in development of acquired tamoxifen resistance via regulating the growth status switch in breast cancer cells), Estrogen receptor‐α36 is involved in development of acquired tamoxifen resistance via regulating the growth status switch in breast cancer cells

    doi: 10.1016/j.molonc.2013.02.001

    Figure Lengend Snippet: Overexpressing ER‐α36 in MCF‐7 cells up‐regulated EGFR expression and down‐regulated ER‐α66 expression. (A). Western blotting analysis of the protein levels of ER‐α36, EGFR, ER‐α66, phosphorylated ERK1/2 and total ERK1/2 in MCF‐7/V cells and MCF‐7/ER‐α36 cells. β‐actin was used as the loading control. All experiments were repeated at least three times, and the representative results are shown. (B C). Relative mRNA level of EGFR and ER‐α66 in MCF‐7/ER‐α36 cells was determined by real time qPCR. β‐actin gene was used as an endogenous control for normalization. Results showed are means ± SEM of three independent reactions.

    Article Snippet: The antibody against EGFR and ER‐α66 was purchased from Epitomics, Inc. (Burlingame, CA, USA).

    Techniques: Expressing, Western Blot, Real-time Polymerase Chain Reaction

    EGFR/ERK signaling participated in the down‐regulation of ER‐α66 in MCF‐7/ER‐α36‐1 cells. (A B). MCF‐7/V and MCF‐7/ER‐α36‐1 cells were starved in serum free medium for 12 h and then treated with 5 μM AG1478 or equivalent vehicle for 1 h. The survived cells were then harvested and the cell lysates were subjected to western blotting analysis. β‐actin was used as the loading control. Data shown were representative of three separate experiments. (C). The mRNA level of ER‐α66 in AG1478 treated MCF‐7/V and MCF‐7/ER‐α36‐1 cells was analyzed by real time qPCR using β‐actin gene as an endogenous control. Results showed are means ± SEM of three independent reactions. (D). MCF‐7/ER‐α36‐1 cells were starved in serum free medium for 12 h and then treated with 50 μM PD098059 or equivalent vehicle for 1 h. The survived cells were then harvested and the cell lysates were subjected to western blotting analysis. β‐actin was used as the loading control. Data shown were representative of three separate experiments. (E). The mRNA level of ER‐α66 in PD098059 treated MCF‐7/ER‐α36‐1 cells was analyzed by real time qPCR using β‐actin gene as an endogenous control. Results showed are means ± SEM of three independent reactions. (F). MCF‐7/ER‐α36‐1 cells were transiently transfected with empty vector or pcDNA3.1+ER‐α66. The cell lysates were then subjected to Western blot analysis. β‐actin was used as the loading control. Data shown were representative of three separate experiments. (G). The mRNA level of EGFR in transiently transfected cells was analyzed by real time qPCR using β‐actin gene as an endogenous control. Results showed are means ± SEM of three independent reactions.

    Journal: Molecular Oncology

    Article Title: Estrogen receptor‐α36 is involved in development of acquired tamoxifen resistance via regulating the growth status switch in breast cancer cells), Estrogen receptor‐α36 is involved in development of acquired tamoxifen resistance via regulating the growth status switch in breast cancer cells

    doi: 10.1016/j.molonc.2013.02.001

    Figure Lengend Snippet: EGFR/ERK signaling participated in the down‐regulation of ER‐α66 in MCF‐7/ER‐α36‐1 cells. (A B). MCF‐7/V and MCF‐7/ER‐α36‐1 cells were starved in serum free medium for 12 h and then treated with 5 μM AG1478 or equivalent vehicle for 1 h. The survived cells were then harvested and the cell lysates were subjected to western blotting analysis. β‐actin was used as the loading control. Data shown were representative of three separate experiments. (C). The mRNA level of ER‐α66 in AG1478 treated MCF‐7/V and MCF‐7/ER‐α36‐1 cells was analyzed by real time qPCR using β‐actin gene as an endogenous control. Results showed are means ± SEM of three independent reactions. (D). MCF‐7/ER‐α36‐1 cells were starved in serum free medium for 12 h and then treated with 50 μM PD098059 or equivalent vehicle for 1 h. The survived cells were then harvested and the cell lysates were subjected to western blotting analysis. β‐actin was used as the loading control. Data shown were representative of three separate experiments. (E). The mRNA level of ER‐α66 in PD098059 treated MCF‐7/ER‐α36‐1 cells was analyzed by real time qPCR using β‐actin gene as an endogenous control. Results showed are means ± SEM of three independent reactions. (F). MCF‐7/ER‐α36‐1 cells were transiently transfected with empty vector or pcDNA3.1+ER‐α66. The cell lysates were then subjected to Western blot analysis. β‐actin was used as the loading control. Data shown were representative of three separate experiments. (G). The mRNA level of EGFR in transiently transfected cells was analyzed by real time qPCR using β‐actin gene as an endogenous control. Results showed are means ± SEM of three independent reactions.

    Article Snippet: The antibody against EGFR and ER‐α66 was purchased from Epitomics, Inc. (Burlingame, CA, USA).

    Techniques: Western Blot, Real-time Polymerase Chain Reaction, Transfection, Plasmid Preparation

    Knock‐down of ER‐α36 in MCF‐7/TAM cells resulted in decreased EGFR mRNA and protein expression, together with increased ER‐α66 mRNA expression. (A). Western blotting analysis of the protein levels of EGFR and ER‐α66 in MCF‐7/TAM‐V cells and MCF‐7/TAM‐mi36‐2 cells. β‐actin was used as the loading control. All experiments were repeated at least three times, and the representative results are shown. (B C). Relative mRNA level of EGFR and ER‐α66 in MCF‐7/TAM‐mi36‐2 cells was determined by real time qPCR. β‐actin gene was used as an endogenous control for normalization. Results showed are means ± SEM of three independent reactions.

    Journal: Molecular Oncology

    Article Title: Estrogen receptor‐α36 is involved in development of acquired tamoxifen resistance via regulating the growth status switch in breast cancer cells), Estrogen receptor‐α36 is involved in development of acquired tamoxifen resistance via regulating the growth status switch in breast cancer cells

    doi: 10.1016/j.molonc.2013.02.001

    Figure Lengend Snippet: Knock‐down of ER‐α36 in MCF‐7/TAM cells resulted in decreased EGFR mRNA and protein expression, together with increased ER‐α66 mRNA expression. (A). Western blotting analysis of the protein levels of EGFR and ER‐α66 in MCF‐7/TAM‐V cells and MCF‐7/TAM‐mi36‐2 cells. β‐actin was used as the loading control. All experiments were repeated at least three times, and the representative results are shown. (B C). Relative mRNA level of EGFR and ER‐α66 in MCF‐7/TAM‐mi36‐2 cells was determined by real time qPCR. β‐actin gene was used as an endogenous control for normalization. Results showed are means ± SEM of three independent reactions.

    Article Snippet: The antibody against EGFR and ER‐α66 was purchased from Epitomics, Inc. (Burlingame, CA, USA).

    Techniques: Expressing, Western Blot, Real-time Polymerase Chain Reaction

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

    Journal: Molecular Endocrinology

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

    doi: 10.1210/me.2009-0497

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

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

    Techniques: Expressing, Western Blot

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

    Journal: Molecular Endocrinology

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

    doi: 10.1210/me.2009-0497

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

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

    Techniques: Western Blot

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

    Journal: Molecular Endocrinology

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

    doi: 10.1210/me.2009-0497

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

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

    Techniques: Recombinant, Expressing, Western Blot

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

    Journal: Molecular Endocrinology

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

    doi: 10.1210/me.2009-0497

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

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

    Techniques: Western Blot

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

    Journal: Molecular Endocrinology

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

    doi: 10.1210/me.2009-0497

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

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

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

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

    Journal: Cancer research

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

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

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

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

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

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

    Journal: Cancer research

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

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

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

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

    Techniques: Expressing, Stable Transfection, Transfection, Western Blot

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

    Journal: Cancer research

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

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

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

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

    Techniques: Immunoprecipitation, Western Blot, Plasmid Preparation

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

    Journal: American Journal of Translational Research

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

    doi:

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

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

    Techniques: Staining, Expressing, Fluorescence, Microscopy

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

    Journal: American Journal of Translational Research

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

    doi:

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

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

    Techniques: Staining, Fluorescence, Microscopy