phosphorylation phospho erk  (Thermo Fisher)


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    Structured Review

    Thermo Fisher phosphorylation phospho erk
    Knockdown of <t>ANO6</t> inhibited the activation of <t>ERK</t> signaling. After T98G and U87MG cells transfection with ANO6-KD 1 or ANO6-KD2, ( A and B ) the protein expression level of ERK and phospho-ERK was detected by Western blot assay; ( C ) the protein expression levels of ANO6 and ERK were detected by Western blot assay in cytoplasm and cell nucleus of T98G cells; ( D and E ) Histograms were used to represent statistical results of the protein expression levels of ANO6 and ERK in cytoplasm and cell nucleus of T98G cells; ( F ) the protein expression levels of ANO6 and ERK were detected by Western blot assay in cytoplasm and cell nucleus of U87MG cells. ( G and H ) Histograms were used to represent statistical results of the protein expression levels of ANO6 and ERK in cytoplasm and cell nucleus of U87MG cells; β-actin was used as a load control for cytoplasm. LaminB was used as a load control for cell nucleus. Data are presented as the mean ± standard deviation. ** p
    Phosphorylation Phospho Erk, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phosphorylation phospho erk/product/Thermo Fisher
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phosphorylation phospho erk - by Bioz Stars, 2020-09
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    1) Product Images from "ANO6 promotes cell proliferation and invasion in glioma through regulating the ERK signaling pathway"

    Article Title: ANO6 promotes cell proliferation and invasion in glioma through regulating the ERK signaling pathway

    Journal: OncoTargets and therapy

    doi: 10.2147/OTT.S211725

    Knockdown of ANO6 inhibited the activation of ERK signaling. After T98G and U87MG cells transfection with ANO6-KD 1 or ANO6-KD2, ( A and B ) the protein expression level of ERK and phospho-ERK was detected by Western blot assay; ( C ) the protein expression levels of ANO6 and ERK were detected by Western blot assay in cytoplasm and cell nucleus of T98G cells; ( D and E ) Histograms were used to represent statistical results of the protein expression levels of ANO6 and ERK in cytoplasm and cell nucleus of T98G cells; ( F ) the protein expression levels of ANO6 and ERK were detected by Western blot assay in cytoplasm and cell nucleus of U87MG cells. ( G and H ) Histograms were used to represent statistical results of the protein expression levels of ANO6 and ERK in cytoplasm and cell nucleus of U87MG cells; β-actin was used as a load control for cytoplasm. LaminB was used as a load control for cell nucleus. Data are presented as the mean ± standard deviation. ** p
    Figure Legend Snippet: Knockdown of ANO6 inhibited the activation of ERK signaling. After T98G and U87MG cells transfection with ANO6-KD 1 or ANO6-KD2, ( A and B ) the protein expression level of ERK and phospho-ERK was detected by Western blot assay; ( C ) the protein expression levels of ANO6 and ERK were detected by Western blot assay in cytoplasm and cell nucleus of T98G cells; ( D and E ) Histograms were used to represent statistical results of the protein expression levels of ANO6 and ERK in cytoplasm and cell nucleus of T98G cells; ( F ) the protein expression levels of ANO6 and ERK were detected by Western blot assay in cytoplasm and cell nucleus of U87MG cells. ( G and H ) Histograms were used to represent statistical results of the protein expression levels of ANO6 and ERK in cytoplasm and cell nucleus of U87MG cells; β-actin was used as a load control for cytoplasm. LaminB was used as a load control for cell nucleus. Data are presented as the mean ± standard deviation. ** p

    Techniques Used: Activation Assay, Transfection, Expressing, Western Blot, Standard Deviation

    ERK inhibitor inhibited the proliferation and invasion of ANO6 overexpression cells. After SHG-44 cells transfection with ANO6 plasmid was treated with PD98059, ( A ) the cell viability was detected by MTT assay; ( B and C ) the ability of cell proliferation was detected by colony formation; ( D and E ) the ability of invasion was detected by transwell assay. Data are presented as the mean ± standard deviation. ** p
    Figure Legend Snippet: ERK inhibitor inhibited the proliferation and invasion of ANO6 overexpression cells. After SHG-44 cells transfection with ANO6 plasmid was treated with PD98059, ( A ) the cell viability was detected by MTT assay; ( B and C ) the ability of cell proliferation was detected by colony formation; ( D and E ) the ability of invasion was detected by transwell assay. Data are presented as the mean ± standard deviation. ** p

    Techniques Used: Over Expression, Transfection, Plasmid Preparation, MTT Assay, Transwell Assay, Standard Deviation

    Related Articles

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    Article Title: ANO6 promotes cell proliferation and invasion in glioma through regulating the ERK signaling pathway
    Article Snippet: .. The antibodies are as follows: ANO6 (1:1000, catPA5-69345, ThermoFisher, California, USA), ERK (1:1000, cat#13–6200, ThermoFisher, California, USA), phosphorylation (phospho)-ERK (1:500, cat#44-680G, ThermoFisher, California, USA), LaminB (1:2000, cat#PA5-66473, ThermoFisher, California, USA), β-actin (1:5000, cat#MA5-15739, ThermoFisher, California, USA). .. Colony formation assay Cells were plated in 6-well culture plates at 100 cells/well.

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    Thermo Fisher erk phosphorylation
    EDA- or EDB-containing fibronectin increase integrin signaling, whereas silencing them diminishes signaling. A , expression of FN-EDA or FN-EDB in osteoblasts enhances <t>FAK,</t> AKT, and <t>ERK</t> phosphorylation compared with cells transfected with the control construct lacking the EDA and the EDB domains ( FN ) (biological replicates for FAK: n = 14/14/14 in 3 experiments; AKT: n = 13/16/16 in 6 experiments; and ERK: n = 16/16/16 in 5 experiments). B , exposing osteoblasts to rFN-EDA or rFN-EDB similarly enhances FAK, AKT, and ERK phosphorylation compared with the control construct ( rFN ) lacking both EDA and EDB domains (biological replicates for FAK: n = 8/6/4; AKT: n = 11/8/8; and ERK: n = 12/8/8 in 4 experiments). Cells were exposed to 200 ng/ml recombinant proteins produced as outlined under “Experimental procedures” for 15 min after culture in serum-free medium for 8 h. C , silencing EDA- or EDB-containing fibronectin using siRNA diminished integrin-mediated signaling (biological replicates for FAK: n = 5/8/8; AKT: n = 6/8/8; and ERK: n = 7/8/8 each in 2 experiments). Osteoblasts were transfected and cultured for 2 days in medium containing fibronectin-depleted FCS, and cell lysates were collected in A and C . Results are expressed as mean ± S.D. ( error bars ). *, p
    Erk Phosphorylation, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 3 article reviews
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    Thermo Fisher mek erk phosphorylation assay cells
    EDA- or EDB-containing fibronectin increase integrin signaling, whereas silencing them diminishes signaling. A , expression of FN-EDA or FN-EDB in osteoblasts enhances <t>FAK,</t> AKT, and <t>ERK</t> phosphorylation compared with cells transfected with the control construct lacking the EDA and the EDB domains ( FN ) (biological replicates for FAK: n = 14/14/14 in 3 experiments; AKT: n = 13/16/16 in 6 experiments; and ERK: n = 16/16/16 in 5 experiments). B , exposing osteoblasts to rFN-EDA or rFN-EDB similarly enhances FAK, AKT, and ERK phosphorylation compared with the control construct ( rFN ) lacking both EDA and EDB domains (biological replicates for FAK: n = 8/6/4; AKT: n = 11/8/8; and ERK: n = 12/8/8 in 4 experiments). Cells were exposed to 200 ng/ml recombinant proteins produced as outlined under “Experimental procedures” for 15 min after culture in serum-free medium for 8 h. C , silencing EDA- or EDB-containing fibronectin using siRNA diminished integrin-mediated signaling (biological replicates for FAK: n = 5/8/8; AKT: n = 6/8/8; and ERK: n = 7/8/8 each in 2 experiments). Osteoblasts were transfected and cultured for 2 days in medium containing fibronectin-depleted FCS, and cell lysates were collected in A and C . Results are expressed as mean ± S.D. ( error bars ). *, p
    Mek Erk Phosphorylation Assay Cells, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mek erk phosphorylation assay cells/product/Thermo Fisher
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mek erk phosphorylation assay cells - by Bioz Stars, 2020-09
    93/100 stars
      Buy from Supplier

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    EDA- or EDB-containing fibronectin increase integrin signaling, whereas silencing them diminishes signaling. A , expression of FN-EDA or FN-EDB in osteoblasts enhances FAK, AKT, and ERK phosphorylation compared with cells transfected with the control construct lacking the EDA and the EDB domains ( FN ) (biological replicates for FAK: n = 14/14/14 in 3 experiments; AKT: n = 13/16/16 in 6 experiments; and ERK: n = 16/16/16 in 5 experiments). B , exposing osteoblasts to rFN-EDA or rFN-EDB similarly enhances FAK, AKT, and ERK phosphorylation compared with the control construct ( rFN ) lacking both EDA and EDB domains (biological replicates for FAK: n = 8/6/4; AKT: n = 11/8/8; and ERK: n = 12/8/8 in 4 experiments). Cells were exposed to 200 ng/ml recombinant proteins produced as outlined under “Experimental procedures” for 15 min after culture in serum-free medium for 8 h. C , silencing EDA- or EDB-containing fibronectin using siRNA diminished integrin-mediated signaling (biological replicates for FAK: n = 5/8/8; AKT: n = 6/8/8; and ERK: n = 7/8/8 each in 2 experiments). Osteoblasts were transfected and cultured for 2 days in medium containing fibronectin-depleted FCS, and cell lysates were collected in A and C . Results are expressed as mean ± S.D. ( error bars ). *, p

    Journal: The Journal of Biological Chemistry

    Article Title: Fibronectins containing extradomain A or B enhance osteoblast differentiation via distinct integrins

    doi: 10.1074/jbc.M116.739987

    Figure Lengend Snippet: EDA- or EDB-containing fibronectin increase integrin signaling, whereas silencing them diminishes signaling. A , expression of FN-EDA or FN-EDB in osteoblasts enhances FAK, AKT, and ERK phosphorylation compared with cells transfected with the control construct lacking the EDA and the EDB domains ( FN ) (biological replicates for FAK: n = 14/14/14 in 3 experiments; AKT: n = 13/16/16 in 6 experiments; and ERK: n = 16/16/16 in 5 experiments). B , exposing osteoblasts to rFN-EDA or rFN-EDB similarly enhances FAK, AKT, and ERK phosphorylation compared with the control construct ( rFN ) lacking both EDA and EDB domains (biological replicates for FAK: n = 8/6/4; AKT: n = 11/8/8; and ERK: n = 12/8/8 in 4 experiments). Cells were exposed to 200 ng/ml recombinant proteins produced as outlined under “Experimental procedures” for 15 min after culture in serum-free medium for 8 h. C , silencing EDA- or EDB-containing fibronectin using siRNA diminished integrin-mediated signaling (biological replicates for FAK: n = 5/8/8; AKT: n = 6/8/8; and ERK: n = 7/8/8 each in 2 experiments). Osteoblasts were transfected and cultured for 2 days in medium containing fibronectin-depleted FCS, and cell lysates were collected in A and C . Results are expressed as mean ± S.D. ( error bars ). *, p

    Article Snippet: For analysis of FAK, AKT, and ERK phosphorylation, cells were transfected (TurboFect, Thermo Fisher) according to the manufacturer's instructions with the different constructs or siRNAs and harvested for protein analysis after culturing for 2 days in medium containing fibronectin-depleted FCS.

    Techniques: Expressing, Transfection, Construct, Recombinant, Produced, Cell Culture

    Knockdown of ANO6 inhibited the activation of ERK signaling. After T98G and U87MG cells transfection with ANO6-KD 1 or ANO6-KD2, ( A and B ) the protein expression level of ERK and phospho-ERK was detected by Western blot assay; ( C ) the protein expression levels of ANO6 and ERK were detected by Western blot assay in cytoplasm and cell nucleus of T98G cells; ( D and E ) Histograms were used to represent statistical results of the protein expression levels of ANO6 and ERK in cytoplasm and cell nucleus of T98G cells; ( F ) the protein expression levels of ANO6 and ERK were detected by Western blot assay in cytoplasm and cell nucleus of U87MG cells. ( G and H ) Histograms were used to represent statistical results of the protein expression levels of ANO6 and ERK in cytoplasm and cell nucleus of U87MG cells; β-actin was used as a load control for cytoplasm. LaminB was used as a load control for cell nucleus. Data are presented as the mean ± standard deviation. ** p

    Journal: OncoTargets and therapy

    Article Title: ANO6 promotes cell proliferation and invasion in glioma through regulating the ERK signaling pathway

    doi: 10.2147/OTT.S211725

    Figure Lengend Snippet: Knockdown of ANO6 inhibited the activation of ERK signaling. After T98G and U87MG cells transfection with ANO6-KD 1 or ANO6-KD2, ( A and B ) the protein expression level of ERK and phospho-ERK was detected by Western blot assay; ( C ) the protein expression levels of ANO6 and ERK were detected by Western blot assay in cytoplasm and cell nucleus of T98G cells; ( D and E ) Histograms were used to represent statistical results of the protein expression levels of ANO6 and ERK in cytoplasm and cell nucleus of T98G cells; ( F ) the protein expression levels of ANO6 and ERK were detected by Western blot assay in cytoplasm and cell nucleus of U87MG cells. ( G and H ) Histograms were used to represent statistical results of the protein expression levels of ANO6 and ERK in cytoplasm and cell nucleus of U87MG cells; β-actin was used as a load control for cytoplasm. LaminB was used as a load control for cell nucleus. Data are presented as the mean ± standard deviation. ** p

    Article Snippet: The antibodies are as follows: ANO6 (1:1000, cat#PA5-69345, ThermoFisher, California, USA), ERK (1:1000, cat#13–6200, ThermoFisher, California, USA), phosphorylation (phospho)-ERK (1:500, cat#44-680G, ThermoFisher, California, USA), LaminB (1:2000, cat#PA5-66473, ThermoFisher, California, USA), β-actin (1:5000, cat#MA5-15739, ThermoFisher, California, USA).

    Techniques: Activation Assay, Transfection, Expressing, Western Blot, Standard Deviation

    ERK inhibitor inhibited the proliferation and invasion of ANO6 overexpression cells. After SHG-44 cells transfection with ANO6 plasmid was treated with PD98059, ( A ) the cell viability was detected by MTT assay; ( B and C ) the ability of cell proliferation was detected by colony formation; ( D and E ) the ability of invasion was detected by transwell assay. Data are presented as the mean ± standard deviation. ** p

    Journal: OncoTargets and therapy

    Article Title: ANO6 promotes cell proliferation and invasion in glioma through regulating the ERK signaling pathway

    doi: 10.2147/OTT.S211725

    Figure Lengend Snippet: ERK inhibitor inhibited the proliferation and invasion of ANO6 overexpression cells. After SHG-44 cells transfection with ANO6 plasmid was treated with PD98059, ( A ) the cell viability was detected by MTT assay; ( B and C ) the ability of cell proliferation was detected by colony formation; ( D and E ) the ability of invasion was detected by transwell assay. Data are presented as the mean ± standard deviation. ** p

    Article Snippet: The antibodies are as follows: ANO6 (1:1000, cat#PA5-69345, ThermoFisher, California, USA), ERK (1:1000, cat#13–6200, ThermoFisher, California, USA), phosphorylation (phospho)-ERK (1:500, cat#44-680G, ThermoFisher, California, USA), LaminB (1:2000, cat#PA5-66473, ThermoFisher, California, USA), β-actin (1:5000, cat#MA5-15739, ThermoFisher, California, USA).

    Techniques: Over Expression, Transfection, Plasmid Preparation, MTT Assay, Transwell Assay, Standard Deviation