anti rabbit fitc  (Millipore)


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    Structured Review

    Millipore anti rabbit fitc
    Fig. 1. p53 relocalizes into NBs. ( A ) SaOS-2 cells were microinjected with either 10 ng/µl pcDNA3p53wt (b–d), pRcCMVp53K386R (f–h) or pNLS-βgal (i–k) together with 30 ng/µl pGFPSUMO-1 and 50 ng/µl pcDNA3HAhUbc9. p53 staining was analysed using a rabbit antiserum, while the localization of βgal-NLS was detected by a monoclonal anti-β-galactosidase antibody. Primary antibodies and GFP–SUMO-1 staining were revealed by incubation with <t>TRITC-conjugated</t> secondary antibodies or by the intrinsic green fluorescence of GFP, respectively. Merging of the two colours results in a yellow signal, corresponding to colocalized proteins. (a and e) Staining of p53 wt and K386R, respectively, in the absence of coexpressed GFP–SUMO-1 and HA-hUbc9. ( B ) SaOS-2 cells (a–c) microinjected with 10 ng/µl pcDNA3p53wt and 30 ng/µl pcDNA3PML3 were analysed for p53 expression as above and for PML staining using the anti-PML monoclonal antibody PG-M3 followed by incubation with an <t>FITC-conjugated</t> secondary antibody. U2OS cells (d–f) were microinjected with pcDNA3PML3, and localization of endogenous p53 and overexpressed PML3 was examined as above. ( C ) LOVO cells were treated with UV light and As 2 O 3 and expression of endogenous p53 was detected by a mixture of DO-1 and 1801 monoclonal antibodies followed by incubation with a TRITC-conjugated secondary antibody (a and c). Endogenous PML3 staining was revealed with a rabbit polyclonal serum specific for PML3 and FITC-conjugated secondary antibody (b and c).
    Anti Rabbit Fitc, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti rabbit fitc/product/Millipore
    Average 99 stars, based on 20 article reviews
    Price from $9.99 to $1999.99
    anti rabbit fitc - by Bioz Stars, 2020-07
    99/100 stars

    Images

    1) Product Images from "Regulation of p53 activity in nuclear bodies by a specific PML isoform"

    Article Title: Regulation of p53 activity in nuclear bodies by a specific PML isoform

    Journal: The EMBO Journal

    doi: 10.1093/emboj/19.22.6185

    Fig. 1. p53 relocalizes into NBs. ( A ) SaOS-2 cells were microinjected with either 10 ng/µl pcDNA3p53wt (b–d), pRcCMVp53K386R (f–h) or pNLS-βgal (i–k) together with 30 ng/µl pGFPSUMO-1 and 50 ng/µl pcDNA3HAhUbc9. p53 staining was analysed using a rabbit antiserum, while the localization of βgal-NLS was detected by a monoclonal anti-β-galactosidase antibody. Primary antibodies and GFP–SUMO-1 staining were revealed by incubation with TRITC-conjugated secondary antibodies or by the intrinsic green fluorescence of GFP, respectively. Merging of the two colours results in a yellow signal, corresponding to colocalized proteins. (a and e) Staining of p53 wt and K386R, respectively, in the absence of coexpressed GFP–SUMO-1 and HA-hUbc9. ( B ) SaOS-2 cells (a–c) microinjected with 10 ng/µl pcDNA3p53wt and 30 ng/µl pcDNA3PML3 were analysed for p53 expression as above and for PML staining using the anti-PML monoclonal antibody PG-M3 followed by incubation with an FITC-conjugated secondary antibody. U2OS cells (d–f) were microinjected with pcDNA3PML3, and localization of endogenous p53 and overexpressed PML3 was examined as above. ( C ) LOVO cells were treated with UV light and As 2 O 3 and expression of endogenous p53 was detected by a mixture of DO-1 and 1801 monoclonal antibodies followed by incubation with a TRITC-conjugated secondary antibody (a and c). Endogenous PML3 staining was revealed with a rabbit polyclonal serum specific for PML3 and FITC-conjugated secondary antibody (b and c).
    Figure Legend Snippet: Fig. 1. p53 relocalizes into NBs. ( A ) SaOS-2 cells were microinjected with either 10 ng/µl pcDNA3p53wt (b–d), pRcCMVp53K386R (f–h) or pNLS-βgal (i–k) together with 30 ng/µl pGFPSUMO-1 and 50 ng/µl pcDNA3HAhUbc9. p53 staining was analysed using a rabbit antiserum, while the localization of βgal-NLS was detected by a monoclonal anti-β-galactosidase antibody. Primary antibodies and GFP–SUMO-1 staining were revealed by incubation with TRITC-conjugated secondary antibodies or by the intrinsic green fluorescence of GFP, respectively. Merging of the two colours results in a yellow signal, corresponding to colocalized proteins. (a and e) Staining of p53 wt and K386R, respectively, in the absence of coexpressed GFP–SUMO-1 and HA-hUbc9. ( B ) SaOS-2 cells (a–c) microinjected with 10 ng/µl pcDNA3p53wt and 30 ng/µl pcDNA3PML3 were analysed for p53 expression as above and for PML staining using the anti-PML monoclonal antibody PG-M3 followed by incubation with an FITC-conjugated secondary antibody. U2OS cells (d–f) were microinjected with pcDNA3PML3, and localization of endogenous p53 and overexpressed PML3 was examined as above. ( C ) LOVO cells were treated with UV light and As 2 O 3 and expression of endogenous p53 was detected by a mixture of DO-1 and 1801 monoclonal antibodies followed by incubation with a TRITC-conjugated secondary antibody (a and c). Endogenous PML3 staining was revealed with a rabbit polyclonal serum specific for PML3 and FITC-conjugated secondary antibody (b and c).

    Techniques Used: Staining, Incubation, Fluorescence, Expressing

    2) Product Images from "Neutrophil Extracellular Traps Identification in Tegumentary Lesions of Patients with Paracoccidioidomycosis and Different Patterns of NETs Generation In Vitro"

    Article Title: Neutrophil Extracellular Traps Identification in Tegumentary Lesions of Patients with Paracoccidioidomycosis and Different Patterns of NETs Generation In Vitro

    Journal: PLoS Neglected Tropical Diseases

    doi: 10.1371/journal.pntd.0004037

    Confocal microscopy of NETs identified in skin lesions of patients with PCM. Tissue was stained with DAPI (A), labeled with anti-elastase antibody followed by FITC-conjugated secondary antibody (B) and anti-histone H1 secondary antibody followed by Texas Red (C). In the last frame, the overlapping images (D). The highlights show the process of NETs formation. (Bar size 10μm).
    Figure Legend Snippet: Confocal microscopy of NETs identified in skin lesions of patients with PCM. Tissue was stained with DAPI (A), labeled with anti-elastase antibody followed by FITC-conjugated secondary antibody (B) and anti-histone H1 secondary antibody followed by Texas Red (C). In the last frame, the overlapping images (D). The highlights show the process of NETs formation. (Bar size 10μm).

    Techniques Used: Confocal Microscopy, Staining, Labeling

    Confocal microscopy of NETs identified in skin lesions of patients with PCM. Tissue was stained with DAPI (A), labeled with anti-elastase antibody followed by FITC-conjugated secondary antibody (B) and anti-histone H1 secondary antibody followed by Texas Red (C). In the last frame, the overlapping images (D). (Bar size 15μm).
    Figure Legend Snippet: Confocal microscopy of NETs identified in skin lesions of patients with PCM. Tissue was stained with DAPI (A), labeled with anti-elastase antibody followed by FITC-conjugated secondary antibody (B) and anti-histone H1 secondary antibody followed by Texas Red (C). In the last frame, the overlapping images (D). (Bar size 15μm).

    Techniques Used: Confocal Microscopy, Staining, Labeling

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    Article Snippet: .. Antibodies against p11 and p36 were obtained from Transduction Laboratories, a Tsg101-specific monoclonal antibody was obtained from Santa Cruz, an anti-tubulin antibody was obtained from Sigma, and an anti-p24 monoclonal antibody was obtained from Chemicon. .. The M2 anti-FLAG antibody (Sigma) was used for detecting tagged AHSV-6 NS3.

    other:

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    Article Snippet: Phenazine methosulfate and anti-tubulin antibody were obtained from Sigma.

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    Millipore anti tubulin antibody
    Growth kinetics of MERS-CoV-WT, -CD, and -mt and accumulation of viral proteins and RNA in infected Vero cells. (A) Vero cells were infected with MERS-CoV-WT (WT), MERS-CoV-CD (CD), or MERS-CoV-mt (mt) at an MOI of 0.01 (left panel) or 3 (right panel). Culture supernatants were collected at the indicated times, and virus titers were determined by plaque assay in Vero cells. The results represent the averages of three independent experiments. Each bar represents the mean (± the standard deviation) for three samples. (B) Vero cells were infected with each of the three viruses at an MOI of 3. At indicated times postinfection, total proteins were extracted and Western blot analysis was performed to detect the S, M, N, nsp1, and <t>tubulin</t> by using anti-MERS-CoV S, M, N, nsp1, and tubulin antibody, respectively. (C) Vero cells were infected with each of the three viruses at an MOI of 3. At the indicated times, total RNAs were extracted. The viral mRNAs were detected by Northern blotting using a probe that binds to the 3′ end of the MERS-CoV genome. The 28S and 18S rRNAs were detected by ethidium bromide staining.
    Anti Tubulin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 231 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Millipore goat anti rabbit igg fitc conjugated
    Alcohol Induces HDAC2 Protein and this Effect is Inhibited by TSA After reaching confluency, SK-N-MC were pre-incubated with TSA for 2 hours, then treated with EtOH (0.1%) for 48 hours. In figure 3a, 10 µg of protein were analyzed using western blot with primary anti-HDAC2 and secondary <t>anti-IgG-HRP</t> antibodies. GAPDH was used as a loading control. Data presented show a representative blot indicating modulation of HDAC2 protein expression and a bar graph representing the mean ± SE of % densitometry values of HDAC2 protein levels (% control) of three independent experiments. # represents significance compared to control. * represents significance compared to EtOH treatment. For the flow cytometry experiments, 1 × 10 6 cells were fixed and permeabilized prior to intracellular staining with primary anti-HDAC2 and secondary <t>anti-IgG-FITC</t> antibody. Data presented in figure 3b show a representative histogram overlay of the gated cells. The bar graph represents the mean ± SE of % of gated cells expressing HDAC2. 10000 events were analyzed per sample. The gray and black histograms represent the unlabeled and secondary antibody controls respectively; the green histogram is the untreated control (~52%), blue represents EtOH (~69 %), purple represents TSA (~45%), and orange represents TSA + EtOH (~49%) treated cells. Data are representative of three independent experiments.
    Goat Anti Rabbit Igg Fitc Conjugated, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti rabbit igg fitc conjugated/product/Millipore
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    Image Search Results


    Growth kinetics of MERS-CoV-WT, -CD, and -mt and accumulation of viral proteins and RNA in infected Vero cells. (A) Vero cells were infected with MERS-CoV-WT (WT), MERS-CoV-CD (CD), or MERS-CoV-mt (mt) at an MOI of 0.01 (left panel) or 3 (right panel). Culture supernatants were collected at the indicated times, and virus titers were determined by plaque assay in Vero cells. The results represent the averages of three independent experiments. Each bar represents the mean (± the standard deviation) for three samples. (B) Vero cells were infected with each of the three viruses at an MOI of 3. At indicated times postinfection, total proteins were extracted and Western blot analysis was performed to detect the S, M, N, nsp1, and tubulin by using anti-MERS-CoV S, M, N, nsp1, and tubulin antibody, respectively. (C) Vero cells were infected with each of the three viruses at an MOI of 3. At the indicated times, total RNAs were extracted. The viral mRNAs were detected by Northern blotting using a probe that binds to the 3′ end of the MERS-CoV genome. The 28S and 18S rRNAs were detected by ethidium bromide staining.

    Journal: Journal of Virology

    Article Title: The Endonucleolytic RNA Cleavage Function of nsp1 of Middle East Respiratory Syndrome Coronavirus Promotes the Production of Infectious Virus Particles in Specific Human Cell Lines

    doi: 10.1128/JVI.01157-18

    Figure Lengend Snippet: Growth kinetics of MERS-CoV-WT, -CD, and -mt and accumulation of viral proteins and RNA in infected Vero cells. (A) Vero cells were infected with MERS-CoV-WT (WT), MERS-CoV-CD (CD), or MERS-CoV-mt (mt) at an MOI of 0.01 (left panel) or 3 (right panel). Culture supernatants were collected at the indicated times, and virus titers were determined by plaque assay in Vero cells. The results represent the averages of three independent experiments. Each bar represents the mean (± the standard deviation) for three samples. (B) Vero cells were infected with each of the three viruses at an MOI of 3. At indicated times postinfection, total proteins were extracted and Western blot analysis was performed to detect the S, M, N, nsp1, and tubulin by using anti-MERS-CoV S, M, N, nsp1, and tubulin antibody, respectively. (C) Vero cells were infected with each of the three viruses at an MOI of 3. At the indicated times, total RNAs were extracted. The viral mRNAs were detected by Northern blotting using a probe that binds to the 3′ end of the MERS-CoV genome. The 28S and 18S rRNAs were detected by ethidium bromide staining.

    Article Snippet: Anti-myc antibody (Millipore), anti-tubulin antibody (Calbiochem), or antibodies against each of MERS-CoV protein described above were used as primary antibodies.

    Techniques: Infection, Plaque Assay, Standard Deviation, Western Blot, Northern Blot, Staining

    Accumulation of viral proteins and RNA in infected 293/CD26 cells. (A) 293/CD26 cells were either mock infected (Mock) or infected with MERS-CoV-WT (WT), MERS-CoV-CD (CD), or MERS-CoV-mt (mt) at an MOI of 3. At indicated times postinfection, total proteins were extracted (A) or total RNAs were extracted (B and C). (A) Western blot analysis was performed to detect the S, M, N, nsp1, and tubulin. (B) The viral mRNAs were detected by Northern blotting using a probe that binds to the 3′ end of the MERS-CoV genome, and the 28S and 18S rRNAs were detected by ethidium bromide staining. (C) The amounts of genomic RNA and subgenomic mRNA 8 were quantified by qRT-PCR, and expression levels were normalized to levels of 18s rRNA. Each bar represents the mean (± the standard deviation) for three wells.

    Journal: Journal of Virology

    Article Title: The Endonucleolytic RNA Cleavage Function of nsp1 of Middle East Respiratory Syndrome Coronavirus Promotes the Production of Infectious Virus Particles in Specific Human Cell Lines

    doi: 10.1128/JVI.01157-18

    Figure Lengend Snippet: Accumulation of viral proteins and RNA in infected 293/CD26 cells. (A) 293/CD26 cells were either mock infected (Mock) or infected with MERS-CoV-WT (WT), MERS-CoV-CD (CD), or MERS-CoV-mt (mt) at an MOI of 3. At indicated times postinfection, total proteins were extracted (A) or total RNAs were extracted (B and C). (A) Western blot analysis was performed to detect the S, M, N, nsp1, and tubulin. (B) The viral mRNAs were detected by Northern blotting using a probe that binds to the 3′ end of the MERS-CoV genome, and the 28S and 18S rRNAs were detected by ethidium bromide staining. (C) The amounts of genomic RNA and subgenomic mRNA 8 were quantified by qRT-PCR, and expression levels were normalized to levels of 18s rRNA. Each bar represents the mean (± the standard deviation) for three wells.

    Article Snippet: Anti-myc antibody (Millipore), anti-tubulin antibody (Calbiochem), or antibodies against each of MERS-CoV protein described above were used as primary antibodies.

    Techniques: Infection, Western Blot, Northern Blot, Staining, Quantitative RT-PCR, Expressing, Standard Deviation

    Characterization of the loss-of-function mutant, MERS-CoV nsp1-mt, in expressed cells. (A) 293 cells were transfected with 2 μg of capped and polyadenylated RNA transcripts encoding CAT, SARS-CoV nsp1, MERS-CoV nsp1-WT, MERS-CoV nsp1-CD, or MERS-CoV nsp1-mt, all of which carried a C-terminal myc epitope tag, radiolabeled with Tran 35 S-label from 8.5 to 9.5 h posttransfection. Lysates were resolved using SDS–12% PAGE, followed by autoradiography (top panel), colloidal Coomassie blue staining (middle panel), and Western blot analysis with anti-myc and tubulin antibodies (bottom two panels). (B) 293 cells were transfected with RNA transcripts as described in panel A. Intracellular RNAs were extracted at 9 h posttransfection and subjected to Northern blot analysis using a probe for GAPDH mRNA (top). The 28S and 18S rRNAs were detected by ethidium bromide staining (bottom). (C) A schematic diagram of Ren-EMCV-FF is shown at the top of the panel. 293 cells were cotransfected with a plasmid encoding Ren-EMCV-FF and the plasmid expressing CAT, SARS-CoV nsp1, MERS-CoV nsp1-WT, MERS-CoV nsp1-CD, or MERS-CoV nsp1-mt protein; all nsp1s carried the C-terminal myc tag. At 24 h posttransfection, intracellular RNAs were extracted and subjected to Northern blot analysis using an RNA probe that binds to the rLuc gene (second panel). Arrowhead, full-length Ren-EMCV-FF; arrow, cleaved RNA fragment. The 28S and 18S rRNAs were detected by ethidium bromide staining (third panel). Cell extracts, prepared at 24 h posttransfection, were used for Western blot analysis using anti-myc and tubulin antibodies (fourth and fifth panels).

    Journal: Journal of Virology

    Article Title: The Endonucleolytic RNA Cleavage Function of nsp1 of Middle East Respiratory Syndrome Coronavirus Promotes the Production of Infectious Virus Particles in Specific Human Cell Lines

    doi: 10.1128/JVI.01157-18

    Figure Lengend Snippet: Characterization of the loss-of-function mutant, MERS-CoV nsp1-mt, in expressed cells. (A) 293 cells were transfected with 2 μg of capped and polyadenylated RNA transcripts encoding CAT, SARS-CoV nsp1, MERS-CoV nsp1-WT, MERS-CoV nsp1-CD, or MERS-CoV nsp1-mt, all of which carried a C-terminal myc epitope tag, radiolabeled with Tran 35 S-label from 8.5 to 9.5 h posttransfection. Lysates were resolved using SDS–12% PAGE, followed by autoradiography (top panel), colloidal Coomassie blue staining (middle panel), and Western blot analysis with anti-myc and tubulin antibodies (bottom two panels). (B) 293 cells were transfected with RNA transcripts as described in panel A. Intracellular RNAs were extracted at 9 h posttransfection and subjected to Northern blot analysis using a probe for GAPDH mRNA (top). The 28S and 18S rRNAs were detected by ethidium bromide staining (bottom). (C) A schematic diagram of Ren-EMCV-FF is shown at the top of the panel. 293 cells were cotransfected with a plasmid encoding Ren-EMCV-FF and the plasmid expressing CAT, SARS-CoV nsp1, MERS-CoV nsp1-WT, MERS-CoV nsp1-CD, or MERS-CoV nsp1-mt protein; all nsp1s carried the C-terminal myc tag. At 24 h posttransfection, intracellular RNAs were extracted and subjected to Northern blot analysis using an RNA probe that binds to the rLuc gene (second panel). Arrowhead, full-length Ren-EMCV-FF; arrow, cleaved RNA fragment. The 28S and 18S rRNAs were detected by ethidium bromide staining (third panel). Cell extracts, prepared at 24 h posttransfection, were used for Western blot analysis using anti-myc and tubulin antibodies (fourth and fifth panels).

    Article Snippet: Anti-myc antibody (Millipore), anti-tubulin antibody (Calbiochem), or antibodies against each of MERS-CoV protein described above were used as primary antibodies.

    Techniques: Mutagenesis, Transfection, Polyacrylamide Gel Electrophoresis, Autoradiography, Staining, Western Blot, Northern Blot, Plasmid Preparation, Expressing

    LPS-induced JNK phosphorylation is increased in Dap12 -knockdown BV2 cells. (A) BV2 cells were transiently transfected with NT or Dap12 -specific siRNAs for 48 h, then stimulated with 500 ng/mL LPS for the indicated times. (B–E) Bar graphs show the quantification of Western blots as ratios of phospho-JNK/total JNK (B) phospho-ERK1/2/total ERK1/2 (C) phospho-p38-MAPK/total p38-MAPK (D) and phospho-IκBα/total IκBα (E) , respectively. α-Tubulin was used as an internal control. The ratio at “0” time point of NT cells served as a control ( n = 3, unpaired Student’s t -test). Data represent mean ± SEM. * p

    Journal: Frontiers in Aging Neuroscience

    Article Title: TREM2/DAP12 Complex Regulates Inflammatory Responses in Microglia via the JNK Signaling Pathway

    doi: 10.3389/fnagi.2017.00204

    Figure Lengend Snippet: LPS-induced JNK phosphorylation is increased in Dap12 -knockdown BV2 cells. (A) BV2 cells were transiently transfected with NT or Dap12 -specific siRNAs for 48 h, then stimulated with 500 ng/mL LPS for the indicated times. (B–E) Bar graphs show the quantification of Western blots as ratios of phospho-JNK/total JNK (B) phospho-ERK1/2/total ERK1/2 (C) phospho-p38-MAPK/total p38-MAPK (D) and phospho-IκBα/total IκBα (E) , respectively. α-Tubulin was used as an internal control. The ratio at “0” time point of NT cells served as a control ( n = 3, unpaired Student’s t -test). Data represent mean ± SEM. * p

    Article Snippet: Antibodies used in this study are as followed: anti-phospho-p38-MAPK, anti-total-p38-MAPK, anti-phospho-ERK1/2, anti-total-ERK1/2, anti-phospho-JNK, anti-total-JNK, anti-phospho-IκBα, anti-total-IκBα, anti-phosho-NF-κB, anti-total-NF-κB, anti-phospho-c-Jun, anti-total-c-Jun and anti-β-actin were purchased from Cell Signaling Technology; anti-tubulin (Millipore); anti-mouse IgG and anti-rabbit IgG antibody conjugated with horseradish peroxidase (ThermoFisher Scientific).

    Techniques: Transfection, Western Blot

    Effect of Clostridium perfringens enterotoxin (CPE) on CLDN4 expression ( A ) Expression of CLDN4 protein in HT29 and Caco-2 human CRC cells. ( B ) Growth inhibitory effect of CPE in CRC cells. ( C ) Expression of CLDN4 and TNFα in CPE-treated CRC cells. ( D ) Expression of CLDN4 in TNFα-treated CRC cells. ( E ) Effect of knockdown of TNFα on CLDN4 expression in CPE-treated CRC cells. ( F ) Effect of TNFα on protein levels of epithelial claudins was examined. ( G – H ) Relationship between concentrations of CPE and TNFα (G) or between concentrations of CPE and CLDN4 (H). Concentrations of CPE and TNFα were measured by ELISA in the fresh-frozen tumor tissues of 11 human CRCs. Tubulin or ACTB served as loading controls.

    Journal: Oncotarget

    Article Title: Anti-claudin-4 extracellular domain antibody enhances the antitumoral effects of chemotherapeutic and antibody drugs in colorectal cancer

    doi: 10.18632/oncotarget.26427

    Figure Lengend Snippet: Effect of Clostridium perfringens enterotoxin (CPE) on CLDN4 expression ( A ) Expression of CLDN4 protein in HT29 and Caco-2 human CRC cells. ( B ) Growth inhibitory effect of CPE in CRC cells. ( C ) Expression of CLDN4 and TNFα in CPE-treated CRC cells. ( D ) Expression of CLDN4 in TNFα-treated CRC cells. ( E ) Effect of knockdown of TNFα on CLDN4 expression in CPE-treated CRC cells. ( F ) Effect of TNFα on protein levels of epithelial claudins was examined. ( G – H ) Relationship between concentrations of CPE and TNFα (G) or between concentrations of CPE and CLDN4 (H). Concentrations of CPE and TNFα were measured by ELISA in the fresh-frozen tumor tissues of 11 human CRCs. Tubulin or ACTB served as loading controls.

    Article Snippet: Anti-tubulin antibody was used to assess the levels of protein loaded per lane (Oncogene Research Products, Cambridge, MA, USA).

    Techniques: Expressing, Enzyme-linked Immunosorbent Assay

    Alcohol Induces HDAC2 Protein and this Effect is Inhibited by TSA After reaching confluency, SK-N-MC were pre-incubated with TSA for 2 hours, then treated with EtOH (0.1%) for 48 hours. In figure 3a, 10 µg of protein were analyzed using western blot with primary anti-HDAC2 and secondary anti-IgG-HRP antibodies. GAPDH was used as a loading control. Data presented show a representative blot indicating modulation of HDAC2 protein expression and a bar graph representing the mean ± SE of % densitometry values of HDAC2 protein levels (% control) of three independent experiments. # represents significance compared to control. * represents significance compared to EtOH treatment. For the flow cytometry experiments, 1 × 10 6 cells were fixed and permeabilized prior to intracellular staining with primary anti-HDAC2 and secondary anti-IgG-FITC antibody. Data presented in figure 3b show a representative histogram overlay of the gated cells. The bar graph represents the mean ± SE of % of gated cells expressing HDAC2. 10000 events were analyzed per sample. The gray and black histograms represent the unlabeled and secondary antibody controls respectively; the green histogram is the untreated control (~52%), blue represents EtOH (~69 %), purple represents TSA (~45%), and orange represents TSA + EtOH (~49%) treated cells. Data are representative of three independent experiments.

    Journal: Alcoholism, clinical and experimental research

    Article Title: Effects of Alcohol on Histone Deacetylase 2 (HDAC2) and the Neuroprotective Role of Trichostatin A (TSA)

    doi: 10.1111/j.1530-0277.2011.01492.x

    Figure Lengend Snippet: Alcohol Induces HDAC2 Protein and this Effect is Inhibited by TSA After reaching confluency, SK-N-MC were pre-incubated with TSA for 2 hours, then treated with EtOH (0.1%) for 48 hours. In figure 3a, 10 µg of protein were analyzed using western blot with primary anti-HDAC2 and secondary anti-IgG-HRP antibodies. GAPDH was used as a loading control. Data presented show a representative blot indicating modulation of HDAC2 protein expression and a bar graph representing the mean ± SE of % densitometry values of HDAC2 protein levels (% control) of three independent experiments. # represents significance compared to control. * represents significance compared to EtOH treatment. For the flow cytometry experiments, 1 × 10 6 cells were fixed and permeabilized prior to intracellular staining with primary anti-HDAC2 and secondary anti-IgG-FITC antibody. Data presented in figure 3b show a representative histogram overlay of the gated cells. The bar graph represents the mean ± SE of % of gated cells expressing HDAC2. 10000 events were analyzed per sample. The gray and black histograms represent the unlabeled and secondary antibody controls respectively; the green histogram is the untreated control (~52%), blue represents EtOH (~69 %), purple represents TSA (~45%), and orange represents TSA + EtOH (~49%) treated cells. Data are representative of three independent experiments.

    Article Snippet: The HDAC2 protein was detected with the primary monoclonal antibody, rabbit anti-histone deacetylase 2 (Millipore) and secondary antibody, goat anti-rabbit IgG FITC-conjugated (Millipore).

    Techniques: Incubation, Western Blot, Expressing, Flow Cytometry, Cytometry, Staining