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  • 93
    Name:
    PLK Ser137 Biotinylated Peptide
    Description:
    This biotinylated peptide contains the residues surrounding serine 137 of PLK This peptide was generated for use as a substrate in heterogeneous or homogeneous kinase assays
    Catalog Number:
    1300
    Price:
    None
    Category:
    Experimental Controls
    Buy from Supplier


    Structured Review

    Cell Signaling Technology Inc fascin
    MST1 depletion causes morphological changes. a – d MST0-211H and H2452 cells were transfected with siNeg, siMST1, or siMST1+pcDNAMST1, analysed 48 h after transfection. Expression of MST1 was analysed by reverse transcription-quantitative real-time PCR (RT-qPCR) ( a ) and western blot ( b ), using glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an internal control. Quantification of number of cytoplasmic extensions and their size (µm) after <t>α-Tubulin</t> staining ( c ) and quantification of <t>Fascin</t> expression ( d ) by immunofluorescence and confocal microscopy in almost 200 cells using ImageJ software. Representative confocal pictures ( c , d ) are presented for cells stained for α-Tubulin (red), Fascin (green), and nuclei stained with 4′,6-diamidino-2-phenylindole (DAPI). For all histograms, error bars indicate the SEM of at least three independent experiments; * p
    This biotinylated peptide contains the residues surrounding serine 137 of PLK This peptide was generated for use as a substrate in heterogeneous or homogeneous kinase assays
    https://www.bioz.com/result/fascin/product/Cell Signaling Technology Inc
    Average 93 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    fascin - by Bioz Stars, 2020-07
    93/100 stars

    Images

    1) Product Images from "MST1/Hippo promoter gene methylation predicts poor survival in patients with malignant pleural mesothelioma in the IFCT-GFPC-0701 MAPS Phase 3 trial"

    Article Title: MST1/Hippo promoter gene methylation predicts poor survival in patients with malignant pleural mesothelioma in the IFCT-GFPC-0701 MAPS Phase 3 trial

    Journal: British Journal of Cancer

    doi: 10.1038/s41416-019-0379-8

    MST1 depletion causes morphological changes. a – d MST0-211H and H2452 cells were transfected with siNeg, siMST1, or siMST1+pcDNAMST1, analysed 48 h after transfection. Expression of MST1 was analysed by reverse transcription-quantitative real-time PCR (RT-qPCR) ( a ) and western blot ( b ), using glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an internal control. Quantification of number of cytoplasmic extensions and their size (µm) after α-Tubulin staining ( c ) and quantification of Fascin expression ( d ) by immunofluorescence and confocal microscopy in almost 200 cells using ImageJ software. Representative confocal pictures ( c , d ) are presented for cells stained for α-Tubulin (red), Fascin (green), and nuclei stained with 4′,6-diamidino-2-phenylindole (DAPI). For all histograms, error bars indicate the SEM of at least three independent experiments; * p
    Figure Legend Snippet: MST1 depletion causes morphological changes. a – d MST0-211H and H2452 cells were transfected with siNeg, siMST1, or siMST1+pcDNAMST1, analysed 48 h after transfection. Expression of MST1 was analysed by reverse transcription-quantitative real-time PCR (RT-qPCR) ( a ) and western blot ( b ), using glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an internal control. Quantification of number of cytoplasmic extensions and their size (µm) after α-Tubulin staining ( c ) and quantification of Fascin expression ( d ) by immunofluorescence and confocal microscopy in almost 200 cells using ImageJ software. Representative confocal pictures ( c , d ) are presented for cells stained for α-Tubulin (red), Fascin (green), and nuclei stained with 4′,6-diamidino-2-phenylindole (DAPI). For all histograms, error bars indicate the SEM of at least three independent experiments; * p

    Techniques Used: Transfection, Expressing, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, Western Blot, Staining, Immunofluorescence, Confocal Microscopy, Software

    2) Product Images from "Melatonin Represses Metastasis in Her2-postive Human Breast Cancer Cells by Suppressing RSK2 Expression"

    Article Title: Melatonin Represses Metastasis in Her2-postive Human Breast Cancer Cells by Suppressing RSK2 Expression

    Journal: Molecular cancer research : MCR

    doi: 10.1158/1541-7786.MCR-16-0158

    Inhibition of the Erk, Rsk2, Creb, Stat3 and Fascin signaling pathways in Her2-positive breast cancer cells by melatonin and the Erk1/2 inhibitor UO126. ( A) SKBR-3 and MCF-7 Her2.1 breast cancer cells were grown in DMEM supplemented with 10% FBS and the effects of MLT (10 −8 M), UO126 (100 ng/ml), or the combination of MLT and UO126 on the expression of total and phospho-active Erk, Rsk2, Creb, Stat3, and total Fascin, were determined by immune (Western)-blot analysis as described in Materials and Methods. ( B ) SKBR-3 breast cancer cells were grown in DMEM supplemented with 10% FBS and stably transfected with the CA-RSK2 consruct and the effects of MLT (10 −8 M), UO126 (100 ng/ml), or the combination of MLT and UO126 on the expression of total and phospho-active Rsk2, Creb, Stat3, and total Fascin, were determined by immune (Western)-blot analysis as described in Materials and Methods.
    Figure Legend Snippet: Inhibition of the Erk, Rsk2, Creb, Stat3 and Fascin signaling pathways in Her2-positive breast cancer cells by melatonin and the Erk1/2 inhibitor UO126. ( A) SKBR-3 and MCF-7 Her2.1 breast cancer cells were grown in DMEM supplemented with 10% FBS and the effects of MLT (10 −8 M), UO126 (100 ng/ml), or the combination of MLT and UO126 on the expression of total and phospho-active Erk, Rsk2, Creb, Stat3, and total Fascin, were determined by immune (Western)-blot analysis as described in Materials and Methods. ( B ) SKBR-3 breast cancer cells were grown in DMEM supplemented with 10% FBS and stably transfected with the CA-RSK2 consruct and the effects of MLT (10 −8 M), UO126 (100 ng/ml), or the combination of MLT and UO126 on the expression of total and phospho-active Rsk2, Creb, Stat3, and total Fascin, were determined by immune (Western)-blot analysis as described in Materials and Methods.

    Techniques Used: Inhibition, Expressing, Western Blot, Stable Transfection, Transfection

    Expression of Erk1/2, Rsk2, Creb, Stat3 and Fascin signaling nodes and their suppression by melatonin in MCF-7, MCF-7 Her2.1 , and SKBR-3 breast cancer cells. ( A) Expression of total (t) and phospho (p)-activated Erk, Rsk2, Creb, Stat3 and total Fascin in parental MCF-7, MCF-7 Her2.1 , and SKBR-3 breast cancer cells. (B and C) SKBR-3 and MCF- 7Her2.1 breast cancer cells were serum starved for 24 h and the dose-response effects of melatonin (MLT) treatment (10 −6 to 10 −10 M, for 1 hour) on the expression of total and phospho-active Erk and Rsk2 by Western-blot analysis as described in Materials and Methods. ( D and E) SKBR-3 and MCF-7 Her2.1 breast cancer cells were serum starved for 24 h and the time-course effects (15, 30, 60 min) of MLT treatment (10 −8 M) on the expression of total and phospho-active Erk and Rsk2 were examined by Western blot analysis. ( F) SKBR-3 and MCF-7 Her2.1 breast cancer cells were serum starved for 24 h and the ability of the MLT-receptor antagonist Luzindole (LUZ) at a concentration of 10 −6 M to block the effects MLT treatment (10 −8 M, for 1 h) on the expression of total and phospho-active Erk and Rsk2 was examined by Western blot analysis. Graphical data represents the mean ± standard deviation of 3 independent experiments.
    Figure Legend Snippet: Expression of Erk1/2, Rsk2, Creb, Stat3 and Fascin signaling nodes and their suppression by melatonin in MCF-7, MCF-7 Her2.1 , and SKBR-3 breast cancer cells. ( A) Expression of total (t) and phospho (p)-activated Erk, Rsk2, Creb, Stat3 and total Fascin in parental MCF-7, MCF-7 Her2.1 , and SKBR-3 breast cancer cells. (B and C) SKBR-3 and MCF- 7Her2.1 breast cancer cells were serum starved for 24 h and the dose-response effects of melatonin (MLT) treatment (10 −6 to 10 −10 M, for 1 hour) on the expression of total and phospho-active Erk and Rsk2 by Western-blot analysis as described in Materials and Methods. ( D and E) SKBR-3 and MCF-7 Her2.1 breast cancer cells were serum starved for 24 h and the time-course effects (15, 30, 60 min) of MLT treatment (10 −8 M) on the expression of total and phospho-active Erk and Rsk2 were examined by Western blot analysis. ( F) SKBR-3 and MCF-7 Her2.1 breast cancer cells were serum starved for 24 h and the ability of the MLT-receptor antagonist Luzindole (LUZ) at a concentration of 10 −6 M to block the effects MLT treatment (10 −8 M, for 1 h) on the expression of total and phospho-active Erk and Rsk2 was examined by Western blot analysis. Graphical data represents the mean ± standard deviation of 3 independent experiments.

    Techniques Used: Expressing, Western Blot, Concentration Assay, Blocking Assay, Standard Deviation

    3) Product Images from "Fascin induces melanoma tumorigenesis and stemness through regulating the Hippo pathway"

    Article Title: Fascin induces melanoma tumorigenesis and stemness through regulating the Hippo pathway

    Journal: Cell Communication and Signaling : CCS

    doi: 10.1186/s12964-018-0250-1

    Fascin regulatesTAZ protein stability. a Quantitative RT-PCR analysis of TAZ mRNA level in WM793 control and WM793 fascin KO cells following culture in medium without/with serum overnight. b Western blot analysis of TAZ expression in WM793 control and WM793 fascin KO cells treated with cycloheximide (CHX). c Quantification of panel B represents TAZ degradation rate in WM793 control and WM793 fascin KO cells. d Immunoblotting analysis of WM793 control and WM793 fascin KO cells after serum starvation overnight and treatment with MG132 (1 μM) for indicated times. e Western blot analysis of WM793 control and WM793 fascin KO cells following serum starvation overnight and then treatment with GSK-3β inhibitor CHIR0091 (2 μM) for 12 h
    Figure Legend Snippet: Fascin regulatesTAZ protein stability. a Quantitative RT-PCR analysis of TAZ mRNA level in WM793 control and WM793 fascin KO cells following culture in medium without/with serum overnight. b Western blot analysis of TAZ expression in WM793 control and WM793 fascin KO cells treated with cycloheximide (CHX). c Quantification of panel B represents TAZ degradation rate in WM793 control and WM793 fascin KO cells. d Immunoblotting analysis of WM793 control and WM793 fascin KO cells after serum starvation overnight and treatment with MG132 (1 μM) for indicated times. e Western blot analysis of WM793 control and WM793 fascin KO cells following serum starvation overnight and then treatment with GSK-3β inhibitor CHIR0091 (2 μM) for 12 h

    Techniques Used: Quantitative RT-PCR, Western Blot, Expressing

    Fascin interacts with MST2 and reduces MST2 homodimeration and p-LATS. a WM793 fascin KO cells were reintroduced with fascin-WT and fascin-S39E plasmids. Western blot analysis was performed using indicated antibodies. b HEK293T cells were transfected with the indicated plasmids. Following incubation for 48 h, cell lysates were immunoprecipitated with Flag (M2) antibody and then immunoblotted with GFP antibody. c In vitro translated [ 35 S]-MST2-full length (FL), MST2(1-313aa) and MST2(314-491aa) truncated proteins were incubated with GST and GST-fascin fusion proteins. After wash, protein complex was eluted and then separated on 10% SDS-PAGE and exposed to phospho-imager (Amersham) for autoradiography. d HEK293T cells were transfected with indicated plasmids. Cell lysates were immunoprecipitated with Flag (M2) antibody and then immunoblotted with GFP antibody. e A proposed model of TAZ regulation by Fascin. Fascin binds to MST2 and inhibits MST2 homodimer formation and kinase activity, which results in inhibition of LATS1/2 activation and TAZ phosphorylation, and thus inhibits TAZ degradation
    Figure Legend Snippet: Fascin interacts with MST2 and reduces MST2 homodimeration and p-LATS. a WM793 fascin KO cells were reintroduced with fascin-WT and fascin-S39E plasmids. Western blot analysis was performed using indicated antibodies. b HEK293T cells were transfected with the indicated plasmids. Following incubation for 48 h, cell lysates were immunoprecipitated with Flag (M2) antibody and then immunoblotted with GFP antibody. c In vitro translated [ 35 S]-MST2-full length (FL), MST2(1-313aa) and MST2(314-491aa) truncated proteins were incubated with GST and GST-fascin fusion proteins. After wash, protein complex was eluted and then separated on 10% SDS-PAGE and exposed to phospho-imager (Amersham) for autoradiography. d HEK293T cells were transfected with indicated plasmids. Cell lysates were immunoprecipitated with Flag (M2) antibody and then immunoblotted with GFP antibody. e A proposed model of TAZ regulation by Fascin. Fascin binds to MST2 and inhibits MST2 homodimer formation and kinase activity, which results in inhibition of LATS1/2 activation and TAZ phosphorylation, and thus inhibits TAZ degradation

    Techniques Used: Western Blot, Transfection, Incubation, Immunoprecipitation, In Vitro, SDS Page, Autoradiography, Activity Assay, Inhibition, Activation Assay

    Fascin regulates melanoma sphere formation through TAZ. a WM793 cells were infected with control or TAZ shRNAs. Expression of TAZ was analyzed by Western blot. b Quantification of sphere numbers in control and TAZ knockdown WM793 cells. Data represented as mean ± SD; n = 3 (*** P
    Figure Legend Snippet: Fascin regulates melanoma sphere formation through TAZ. a WM793 cells were infected with control or TAZ shRNAs. Expression of TAZ was analyzed by Western blot. b Quantification of sphere numbers in control and TAZ knockdown WM793 cells. Data represented as mean ± SD; n = 3 (*** P

    Techniques Used: Infection, Expressing, Western Blot

    Fascin regulates TAZ protein level independent of its actin-bundling activity. a WM793 fascin KO cells were starved for 12 h and then cultured with/without FBS and then subjected to Western blot analysis with indicated antibodies. b WM793 fascin KO cells were reintroduced with fascin-WT and fascin-S39E and Western blot analysis was performed using indicated antibodies
    Figure Legend Snippet: Fascin regulates TAZ protein level independent of its actin-bundling activity. a WM793 fascin KO cells were starved for 12 h and then cultured with/without FBS and then subjected to Western blot analysis with indicated antibodies. b WM793 fascin KO cells were reintroduced with fascin-WT and fascin-S39E and Western blot analysis was performed using indicated antibodies

    Techniques Used: Activity Assay, Cell Culture, Western Blot

    4) Product Images from "Fascin induces melanoma tumorigenesis and stemness through regulating the Hippo pathway"

    Article Title: Fascin induces melanoma tumorigenesis and stemness through regulating the Hippo pathway

    Journal: Cell Communication and Signaling : CCS

    doi: 10.1186/s12964-018-0250-1

    Fascin regulatesTAZ protein stability. a Quantitative RT-PCR analysis of TAZ mRNA level in WM793 control and WM793 fascin KO cells following culture in medium without/with serum overnight. b Western blot analysis of TAZ expression in WM793 control and WM793 fascin KO cells treated with cycloheximide (CHX). c Quantification of panel B represents TAZ degradation rate in WM793 control and WM793 fascin KO cells. d Immunoblotting analysis of WM793 control and WM793 fascin KO cells after serum starvation overnight and treatment with MG132 (1 μM) for indicated times. e Western blot analysis of WM793 control and WM793 fascin KO cells following serum starvation overnight and then treatment with GSK-3β inhibitor CHIR0091 (2 μM) for 12 h
    Figure Legend Snippet: Fascin regulatesTAZ protein stability. a Quantitative RT-PCR analysis of TAZ mRNA level in WM793 control and WM793 fascin KO cells following culture in medium without/with serum overnight. b Western blot analysis of TAZ expression in WM793 control and WM793 fascin KO cells treated with cycloheximide (CHX). c Quantification of panel B represents TAZ degradation rate in WM793 control and WM793 fascin KO cells. d Immunoblotting analysis of WM793 control and WM793 fascin KO cells after serum starvation overnight and treatment with MG132 (1 μM) for indicated times. e Western blot analysis of WM793 control and WM793 fascin KO cells following serum starvation overnight and then treatment with GSK-3β inhibitor CHIR0091 (2 μM) for 12 h

    Techniques Used: Quantitative RT-PCR, Western Blot, Expressing

    Fascin interacts with MST2 and reduces MST2 homodimeration and p-LATS. a WM793 fascin KO cells were reintroduced with fascin-WT and fascin-S39E plasmids. Western blot analysis was performed using indicated antibodies. b HEK293T cells were transfected with the indicated plasmids. Following incubation for 48 h, cell lysates were immunoprecipitated with Flag (M2) antibody and then immunoblotted with GFP antibody. c In vitro translated [ 35 S]-MST2-full length (FL), MST2(1-313aa) and MST2(314-491aa) truncated proteins were incubated with GST and GST-fascin fusion proteins. After wash, protein complex was eluted and then separated on 10% SDS-PAGE and exposed to phospho-imager (Amersham) for autoradiography. d HEK293T cells were transfected with indicated plasmids. Cell lysates were immunoprecipitated with Flag (M2) antibody and then immunoblotted with GFP antibody. e A proposed model of TAZ regulation by Fascin. Fascin binds to MST2 and inhibits MST2 homodimer formation and kinase activity, which results in inhibition of LATS1/2 activation and TAZ phosphorylation, and thus inhibits TAZ degradation
    Figure Legend Snippet: Fascin interacts with MST2 and reduces MST2 homodimeration and p-LATS. a WM793 fascin KO cells were reintroduced with fascin-WT and fascin-S39E plasmids. Western blot analysis was performed using indicated antibodies. b HEK293T cells were transfected with the indicated plasmids. Following incubation for 48 h, cell lysates were immunoprecipitated with Flag (M2) antibody and then immunoblotted with GFP antibody. c In vitro translated [ 35 S]-MST2-full length (FL), MST2(1-313aa) and MST2(314-491aa) truncated proteins were incubated with GST and GST-fascin fusion proteins. After wash, protein complex was eluted and then separated on 10% SDS-PAGE and exposed to phospho-imager (Amersham) for autoradiography. d HEK293T cells were transfected with indicated plasmids. Cell lysates were immunoprecipitated with Flag (M2) antibody and then immunoblotted with GFP antibody. e A proposed model of TAZ regulation by Fascin. Fascin binds to MST2 and inhibits MST2 homodimer formation and kinase activity, which results in inhibition of LATS1/2 activation and TAZ phosphorylation, and thus inhibits TAZ degradation

    Techniques Used: Western Blot, Transfection, Incubation, Immunoprecipitation, In Vitro, SDS Page, Autoradiography, Activity Assay, Inhibition, Activation Assay

    Fascin regulates melanoma sphere formation through TAZ. a WM793 cells were infected with control or TAZ shRNAs. Expression of TAZ was analyzed by Western blot. b Quantification of sphere numbers in control and TAZ knockdown WM793 cells. Data represented as mean ± SD; n = 3 (*** P
    Figure Legend Snippet: Fascin regulates melanoma sphere formation through TAZ. a WM793 cells were infected with control or TAZ shRNAs. Expression of TAZ was analyzed by Western blot. b Quantification of sphere numbers in control and TAZ knockdown WM793 cells. Data represented as mean ± SD; n = 3 (*** P

    Techniques Used: Infection, Expressing, Western Blot

    Fascin regulates TAZ protein level independent of its actin-bundling activity. a WM793 fascin KO cells were starved for 12 h and then cultured with/without FBS and then subjected to Western blot analysis with indicated antibodies. b WM793 fascin KO cells were reintroduced with fascin-WT and fascin-S39E and Western blot analysis was performed using indicated antibodies
    Figure Legend Snippet: Fascin regulates TAZ protein level independent of its actin-bundling activity. a WM793 fascin KO cells were starved for 12 h and then cultured with/without FBS and then subjected to Western blot analysis with indicated antibodies. b WM793 fascin KO cells were reintroduced with fascin-WT and fascin-S39E and Western blot analysis was performed using indicated antibodies

    Techniques Used: Activity Assay, Cell Culture, Western Blot

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    Immunofluorescence:

    Article Title: The loss of the kinases SadA and SadB results in early neuronal apoptosis and a reduced number of progenitors
    Article Snippet: .. Antibodies The following antibodies were used for immunofluorescence staining: rabbit anti-Brsk1 (C-terminal epitope; Cell Signaling #5935, 1:100), rabbit anti-Brsk1 (N-terminal epitope; Atlas Antibodies, HPA061719, 1:200), rabbit anti-Brsk2 (N-terminal epitope; Cell Signaling #5460, 1:100), rabbit anti-phospho-SadA/B (1:500), rabbit anti-cleaved caspase-3 (Cell Signaling, #9661, 1:200), rabb it anti-phospho-Ser139- γ H2A.X (Abcam, #ab11174, 1:100), mouse anti-Ki67 (Cell Signaling, #9449, 1:300), rabbit anti-Pax6 (Biolegend, #901301, 1:200), mouse anti-PH3 (Cell Signaling, #9706,1:300), mouse anti-PCNA (Millipore # MAB424), mouse anti-nestin (BD Biosciences, #611658, 1:200), rabbit anti-NF medium chain (Abcam, #ab64300, 1:200), mouse anti-NF medium chain (2H3, DSHB, 1:4), rabbit anti-Tbr1 (Abcam, #31940, 1:400), rat anti-Ctip2 (Abcam, #ab18465), SMI-312 (Abcam, #24574, 1:1000), rabbit anti-Tbr2 (Abcam, #23345, 1:400), mouse Tau-1 (Chemicon, #MAB3420; 1:500), mouse anti-MAP2 (Chemicon, #AB5622; 1:1000) and goat secondary antibodies labeled with Alexa 488 or 594 (Molecular Probes, 1:800). .. The rabbit anti-phospho-Sad antibody was raised against the peptide KGDSLLEpTSCGSPHY and affinity purified (Davids Biotechnology).

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    Cell Signaling Technology Inc fascin
    MST1 depletion causes morphological changes. a – d MST0-211H and H2452 cells were transfected with siNeg, siMST1, or siMST1+pcDNAMST1, analysed 48 h after transfection. Expression of MST1 was analysed by reverse transcription-quantitative real-time PCR (RT-qPCR) ( a ) and western blot ( b ), using glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an internal control. Quantification of number of cytoplasmic extensions and their size (µm) after <t>α-Tubulin</t> staining ( c ) and quantification of <t>Fascin</t> expression ( d ) by immunofluorescence and confocal microscopy in almost 200 cells using ImageJ software. Representative confocal pictures ( c , d ) are presented for cells stained for α-Tubulin (red), Fascin (green), and nuclei stained with 4′,6-diamidino-2-phenylindole (DAPI). For all histograms, error bars indicate the SEM of at least three independent experiments; * p
    Fascin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    MST1 depletion causes morphological changes. a – d MST0-211H and H2452 cells were transfected with siNeg, siMST1, or siMST1+pcDNAMST1, analysed 48 h after transfection. Expression of MST1 was analysed by reverse transcription-quantitative real-time PCR (RT-qPCR) ( a ) and western blot ( b ), using glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an internal control. Quantification of number of cytoplasmic extensions and their size (µm) after α-Tubulin staining ( c ) and quantification of Fascin expression ( d ) by immunofluorescence and confocal microscopy in almost 200 cells using ImageJ software. Representative confocal pictures ( c , d ) are presented for cells stained for α-Tubulin (red), Fascin (green), and nuclei stained with 4′,6-diamidino-2-phenylindole (DAPI). For all histograms, error bars indicate the SEM of at least three independent experiments; * p

    Journal: British Journal of Cancer

    Article Title: MST1/Hippo promoter gene methylation predicts poor survival in patients with malignant pleural mesothelioma in the IFCT-GFPC-0701 MAPS Phase 3 trial

    doi: 10.1038/s41416-019-0379-8

    Figure Lengend Snippet: MST1 depletion causes morphological changes. a – d MST0-211H and H2452 cells were transfected with siNeg, siMST1, or siMST1+pcDNAMST1, analysed 48 h after transfection. Expression of MST1 was analysed by reverse transcription-quantitative real-time PCR (RT-qPCR) ( a ) and western blot ( b ), using glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an internal control. Quantification of number of cytoplasmic extensions and their size (µm) after α-Tubulin staining ( c ) and quantification of Fascin expression ( d ) by immunofluorescence and confocal microscopy in almost 200 cells using ImageJ software. Representative confocal pictures ( c , d ) are presented for cells stained for α-Tubulin (red), Fascin (green), and nuclei stained with 4′,6-diamidino-2-phenylindole (DAPI). For all histograms, error bars indicate the SEM of at least three independent experiments; * p

    Article Snippet: The primary antibodies were YAP (Cell Signaling, 1/150), TAZ (Cell Signaling, 1/150), alpha-tubulin (Sigma Aldrich, 1/300), actin (Cell Signaling, 1/300), Fascin (Cell Signaling, 1/300) or cytochrome C (BD Biosciences, 1/50).

    Techniques: Transfection, Expressing, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, Western Blot, Staining, Immunofluorescence, Confocal Microscopy, Software