anti-actin Search Results


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  • 99
    Millipore anti beta actin antibody
    Effect of TSN on expression of HCV replicon. (A) HCV replicon cells were treated with various concentrations of TSN for 48 h. Replication levels of HCV RNA were analyzed by luciferase assay. Bars indicate luciferase activities relative to that of the drug-negative control. (B) Cell viability was determined by MTS assay. Bars indicate the value relative to that of the drug-negative control. (C) Western blotting analyses. The expression of NS5A and <t>beta-actin</t> was detected using anti-NS5A and anti-beta-actin antibodies. Densitometry of NS5A protein was performed, and the result is indicated as a percentage of the result for the drug-negative control. The assay was repeated three times, and a representative result is shown. (D) A bicistronic reporter gene plasmid, pCIneo-Rluc-IRES-Fluc, was transfected into Huh7 cells. The cells were cultured with TSN at the concentrations indicated, and dual luciferase activities were measured after 24 h of treatment. Values are displayed as ratios of Fluc to Rluc. In panels A, B, and D, the assays were done in triplicate and repeated three times. Error bars indicate means ± SDs.
    Anti Beta Actin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1137 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bethyl anti actin ab
    Effect of TSN on expression of HCV replicon. (A) HCV replicon cells were treated with various concentrations of TSN for 48 h. Replication levels of HCV RNA were analyzed by luciferase assay. Bars indicate luciferase activities relative to that of the drug-negative control. (B) Cell viability was determined by MTS assay. Bars indicate the value relative to that of the drug-negative control. (C) Western blotting analyses. The expression of NS5A and <t>beta-actin</t> was detected using anti-NS5A and anti-beta-actin antibodies. Densitometry of NS5A protein was performed, and the result is indicated as a percentage of the result for the drug-negative control. The assay was repeated three times, and a representative result is shown. (D) A bicistronic reporter gene plasmid, pCIneo-Rluc-IRES-Fluc, was transfected into Huh7 cells. The cells were cultured with TSN at the concentrations indicated, and dual luciferase activities were measured after 24 h of treatment. Values are displayed as ratios of Fluc to Rluc. In panels A, B, and D, the assays were done in triplicate and repeated three times. Error bars indicate means ± SDs.
    Anti Actin Ab, supplied by Bethyl, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc anti beta actin antibodies
    Expression of proteins which were reported to be associated with sensitivity to anti-microtubule agents. (A) Protein expression was evaluated by western blot analysis. Expression values of class Ⅲ <t>beta-tubulin</t> (TUBB3) relative to beta-actin were determined using Just TLC software. (B) Representative images of HCC4006 and HCC4006ER cells immunohistochemically stained with antibodies to ATP-binding cassette subfamily B, member 1 (ABCB1).
    Anti Beta Actin Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 61 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Santa Cruz Biotechnology anti beta actin antibody
    Effects of MEKS on the activations of apoptosis-related proteins. MDA-MB-231 cells were treated with 0, 25, or 50 μg/ml of MEKS for 4 h or 30 nM paclitaxel for 24 h (positive control). Protein expressions of cleaved caspase 3 (C), 8 (B) and 9 (A), cleaved PARP (D) and <t>beta-actin</t> (the loading control) were detected by Western blotting
    Anti Beta Actin Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 142 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Becton Dickinson anti actin antibody
    Effects of MEKS on the activations of apoptosis-related proteins. MDA-MB-231 cells were treated with 0, 25, or 50 μg/ml of MEKS for 4 h or 30 nM paclitaxel for 24 h (positive control). Protein expressions of cleaved caspase 3 (C), 8 (B) and 9 (A), cleaved PARP (D) and <t>beta-actin</t> (the loading control) were detected by Western blotting
    Anti Actin Antibody, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 138 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ICN Biomedicals anti actin ab
    Effects of MEKS on the activations of apoptosis-related proteins. MDA-MB-231 cells were treated with 0, 25, or 50 μg/ml of MEKS for 4 h or 30 nM paclitaxel for 24 h (positive control). Protein expressions of cleaved caspase 3 (C), 8 (B) and 9 (A), cleaved PARP (D) and <t>beta-actin</t> (the loading control) were detected by Western blotting
    Anti Actin Ab, supplied by ICN Biomedicals, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    SouthernBiotech anti actin ab
    Effects of MEKS on the activations of apoptosis-related proteins. MDA-MB-231 cells were treated with 0, 25, or 50 μg/ml of MEKS for 4 h or 30 nM paclitaxel for 24 h (positive control). Protein expressions of cleaved caspase 3 (C), 8 (B) and 9 (A), cleaved PARP (D) and <t>beta-actin</t> (the loading control) were detected by Western blotting
    Anti Actin Ab, supplied by SouthernBiotech, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Abcam anti beta actin antibody
    CD47 is highly expressed in osteosarcoma Quantitative RT-PCR A. and immunoblot analysis B. showed CD47 expression in ten freshly isolated osteosarcoma tissues and their adjacent nontumorous tissues. <t>Beta-actin</t> was treated as the reference control. CD47 immunostaining C. showed higher of CD47 expression in osteosarcoma of the same samples with or without metastasis and their adjacent nontumorous tissues. The tissues were counterstained with DAPI Fluorescent Stain. Representative images are shown here. (magnification × 100). D. Flow-cytometry analysis of CD47 and CD44 expressions on osteosarcoma tumor cells and quantification of CD44 cells also expressing CD47.
    Anti Beta Actin Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 98/100, based on 1248 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc mouse anti actin ab
    CD47 is highly expressed in osteosarcoma Quantitative RT-PCR A. and immunoblot analysis B. showed CD47 expression in ten freshly isolated osteosarcoma tissues and their adjacent nontumorous tissues. <t>Beta-actin</t> was treated as the reference control. CD47 immunostaining C. showed higher of CD47 expression in osteosarcoma of the same samples with or without metastasis and their adjacent nontumorous tissues. The tissues were counterstained with DAPI Fluorescent Stain. Representative images are shown here. (magnification × 100). D. Flow-cytometry analysis of CD47 and CD44 expressions on osteosarcoma tumor cells and quantification of CD44 cells also expressing CD47.
    Mouse Anti Actin Ab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 88/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore actin ab 1
    CD47 is highly expressed in osteosarcoma Quantitative RT-PCR A. and immunoblot analysis B. showed CD47 expression in ten freshly isolated osteosarcoma tissues and their adjacent nontumorous tissues. <t>Beta-actin</t> was treated as the reference control. CD47 immunostaining C. showed higher of CD47 expression in osteosarcoma of the same samples with or without metastasis and their adjacent nontumorous tissues. The tissues were counterstained with DAPI Fluorescent Stain. Representative images are shown here. (magnification × 100). D. Flow-cytometry analysis of CD47 and CD44 expressions on osteosarcoma tumor cells and quantification of CD44 cells also expressing CD47.
    Actin Ab 1, supplied by Millipore, used in various techniques. Bioz Stars score: 98/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore polyclonal anti actin antibody
    RUNX2 associates with p53 in response to ADR. ( a ) Indirect immunostaining experiments. U2OS cells were treated with 1.0 μ M of ADR or left untreated. Twenty-four hours after ADR treatment, cells were simultaneously incubated with monoclonal anti-p53 and <t>polyclonal</t> anti-RUNX2 antibodies followed by the incubation with rhodamine-conjugated anti-mouse IgG (red) and fluorescein isothiocyanate (FITC)-conjugated anti-rabbit IgG (green). Cell nuclei were stained with DAPI (blue). Merged images (yellow) indicate the colocalization of RUNX2 with p53 in cell nucleus. ( b and c ) Co-immunoprecipitation experiments. U2OS cells were exposed to 0.5 μ M of ADR ( b ) or left untreated ( c ). Twenty-four hours after ADR treatment, cell lysates were prepared and immunoprecipitated with NMS or with monoclonal anti-p53 antibody. The immunoprecipitates were analyzed by immnublotting with monoclonal anti-RUNX2 antibody. The reciprocal experiments and 1/20 of inputs were also shown
    Polyclonal Anti Actin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 131 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Cell Signaling Technology Inc rabbit anti actin antibodies
    RUNX2 associates with p53 in response to ADR. ( a ) Indirect immunostaining experiments. U2OS cells were treated with 1.0 μ M of ADR or left untreated. Twenty-four hours after ADR treatment, cells were simultaneously incubated with monoclonal anti-p53 and <t>polyclonal</t> anti-RUNX2 antibodies followed by the incubation with rhodamine-conjugated anti-mouse IgG (red) and fluorescein isothiocyanate (FITC)-conjugated anti-rabbit IgG (green). Cell nuclei were stained with DAPI (blue). Merged images (yellow) indicate the colocalization of RUNX2 with p53 in cell nucleus. ( b and c ) Co-immunoprecipitation experiments. U2OS cells were exposed to 0.5 μ M of ADR ( b ) or left untreated ( c ). Twenty-four hours after ADR treatment, cell lysates were prepared and immunoprecipitated with NMS or with monoclonal anti-p53 antibody. The immunoprecipitates were analyzed by immnublotting with monoclonal anti-RUNX2 antibody. The reciprocal experiments and 1/20 of inputs were also shown
    Rabbit Anti Actin Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Becton Dickinson anti actin ab 5
    RUNX2 associates with p53 in response to ADR. ( a ) Indirect immunostaining experiments. U2OS cells were treated with 1.0 μ M of ADR or left untreated. Twenty-four hours after ADR treatment, cells were simultaneously incubated with monoclonal anti-p53 and <t>polyclonal</t> anti-RUNX2 antibodies followed by the incubation with rhodamine-conjugated anti-mouse IgG (red) and fluorescein isothiocyanate (FITC)-conjugated anti-rabbit IgG (green). Cell nuclei were stained with DAPI (blue). Merged images (yellow) indicate the colocalization of RUNX2 with p53 in cell nucleus. ( b and c ) Co-immunoprecipitation experiments. U2OS cells were exposed to 0.5 μ M of ADR ( b ) or left untreated ( c ). Twenty-four hours after ADR treatment, cell lysates were prepared and immunoprecipitated with NMS or with monoclonal anti-p53 antibody. The immunoprecipitates were analyzed by immnublotting with monoclonal anti-RUNX2 antibody. The reciprocal experiments and 1/20 of inputs were also shown
    Anti Actin Ab 5, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 88/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam mouse anti beta actin antibody
    Tnmd expression in human musculoskeletal elements and mechano-regulation. (a) Representative western blot with anti-C-terminal Tnmd antibody on human (tendon, MTJ myotendinous junction, muscle and bone) and mouse (tendon) tissues. Detection of <t>beta</t> actin served as loading control. (b) Representative immunofluorescent detection of Tnmd in human and mouse Achilles tendons. Tnmd expression in green and nuclear DAPI in blue colour. Upper panel: low magnification epi-fluorescence images; lower panel: confocal microscopy. (c) Semi-quantitative PCR for Tnmd expression in cultured human TSPC (passage 0 and 3). The house-keeping gene GAPDH was used for normalization. Western blotting, staining and PCR were reproduced three times (n = 3). (d) Luciferase activity assays (expressed in RLU, relative light units) with human TSPC transfected with a promoter-less (mock-luc) or Tnmd promoter (− 769/+84F Tnmd genomic fragment)-driven luciferase (pTnmd-luc) plasmids without or undergoing mechanical stimulation of 5% axial strain. Two independent stimulations with two different donors were carried out (n = 4). (e) Semi-quantitative PCR bands and densitometric evaluation of Tnmd expression against GAPDH in human TSPC (passage 3) prior and after mechanical stimulation (presented in fold change). Statistical significance: ***p
    Mouse Anti Beta Actin Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 97 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology mouse anti actin antibodies
    Tnmd expression in human musculoskeletal elements and mechano-regulation. (a) Representative western blot with anti-C-terminal Tnmd antibody on human (tendon, MTJ myotendinous junction, muscle and bone) and mouse (tendon) tissues. Detection of <t>beta</t> actin served as loading control. (b) Representative immunofluorescent detection of Tnmd in human and mouse Achilles tendons. Tnmd expression in green and nuclear DAPI in blue colour. Upper panel: low magnification epi-fluorescence images; lower panel: confocal microscopy. (c) Semi-quantitative PCR for Tnmd expression in cultured human TSPC (passage 0 and 3). The house-keeping gene GAPDH was used for normalization. Western blotting, staining and PCR were reproduced three times (n = 3). (d) Luciferase activity assays (expressed in RLU, relative light units) with human TSPC transfected with a promoter-less (mock-luc) or Tnmd promoter (− 769/+84F Tnmd genomic fragment)-driven luciferase (pTnmd-luc) plasmids without or undergoing mechanical stimulation of 5% axial strain. Two independent stimulations with two different donors were carried out (n = 4). (e) Semi-quantitative PCR bands and densitometric evaluation of Tnmd expression against GAPDH in human TSPC (passage 3) prior and after mechanical stimulation (presented in fold change). Statistical significance: ***p
    Mouse Anti Actin Antibodies, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 89/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore anti actin ab 1501
    Tnmd expression in human musculoskeletal elements and mechano-regulation. (a) Representative western blot with anti-C-terminal Tnmd antibody on human (tendon, MTJ myotendinous junction, muscle and bone) and mouse (tendon) tissues. Detection of <t>beta</t> actin served as loading control. (b) Representative immunofluorescent detection of Tnmd in human and mouse Achilles tendons. Tnmd expression in green and nuclear DAPI in blue colour. Upper panel: low magnification epi-fluorescence images; lower panel: confocal microscopy. (c) Semi-quantitative PCR for Tnmd expression in cultured human TSPC (passage 0 and 3). The house-keeping gene GAPDH was used for normalization. Western blotting, staining and PCR were reproduced three times (n = 3). (d) Luciferase activity assays (expressed in RLU, relative light units) with human TSPC transfected with a promoter-less (mock-luc) or Tnmd promoter (− 769/+84F Tnmd genomic fragment)-driven luciferase (pTnmd-luc) plasmids without or undergoing mechanical stimulation of 5% axial strain. Two independent stimulations with two different donors were carried out (n = 4). (e) Semi-quantitative PCR bands and densitometric evaluation of Tnmd expression against GAPDH in human TSPC (passage 3) prior and after mechanical stimulation (presented in fold change). Statistical significance: ***p
    Anti Actin Ab 1501, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam anti actin ab 3280 antibodies
    Tnmd expression in human musculoskeletal elements and mechano-regulation. (a) Representative western blot with anti-C-terminal Tnmd antibody on human (tendon, MTJ myotendinous junction, muscle and bone) and mouse (tendon) tissues. Detection of <t>beta</t> actin served as loading control. (b) Representative immunofluorescent detection of Tnmd in human and mouse Achilles tendons. Tnmd expression in green and nuclear DAPI in blue colour. Upper panel: low magnification epi-fluorescence images; lower panel: confocal microscopy. (c) Semi-quantitative PCR for Tnmd expression in cultured human TSPC (passage 0 and 3). The house-keeping gene GAPDH was used for normalization. Western blotting, staining and PCR were reproduced three times (n = 3). (d) Luciferase activity assays (expressed in RLU, relative light units) with human TSPC transfected with a promoter-less (mock-luc) or Tnmd promoter (− 769/+84F Tnmd genomic fragment)-driven luciferase (pTnmd-luc) plasmids without or undergoing mechanical stimulation of 5% axial strain. Two independent stimulations with two different donors were carried out (n = 4). (e) Semi-quantitative PCR bands and densitometric evaluation of Tnmd expression against GAPDH in human TSPC (passage 3) prior and after mechanical stimulation (presented in fold change). Statistical significance: ***p
    Anti Actin Ab 3280 Antibodies, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology rabbit anti actin primary ab
    Tnmd expression in human musculoskeletal elements and mechano-regulation. (a) Representative western blot with anti-C-terminal Tnmd antibody on human (tendon, MTJ myotendinous junction, muscle and bone) and mouse (tendon) tissues. Detection of <t>beta</t> actin served as loading control. (b) Representative immunofluorescent detection of Tnmd in human and mouse Achilles tendons. Tnmd expression in green and nuclear DAPI in blue colour. Upper panel: low magnification epi-fluorescence images; lower panel: confocal microscopy. (c) Semi-quantitative PCR for Tnmd expression in cultured human TSPC (passage 0 and 3). The house-keeping gene GAPDH was used for normalization. Western blotting, staining and PCR were reproduced three times (n = 3). (d) Luciferase activity assays (expressed in RLU, relative light units) with human TSPC transfected with a promoter-less (mock-luc) or Tnmd promoter (− 769/+84F Tnmd genomic fragment)-driven luciferase (pTnmd-luc) plasmids without or undergoing mechanical stimulation of 5% axial strain. Two independent stimulations with two different donors were carried out (n = 4). (e) Semi-quantitative PCR bands and densitometric evaluation of Tnmd expression against GAPDH in human TSPC (passage 3) prior and after mechanical stimulation (presented in fold change). Statistical significance: ***p
    Rabbit Anti Actin Primary Ab, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore mouse anti actin antibody
    (A–C) HeLa cells stimulating by nutrient‐deprivation were analyzed in every 2 h. Bars = 20 μm. (A) Relative expression level of LC 3‐I and LC 3‐ II were detected using with anti‐ LC 3 antibody and <t>anti‐actin</t> antibody for loading control of western blotting analysis. (B) Immunocytochemical analysis with anti‐ LC 3 antibodies (Green) and DAPI (Blue). (C) Live‐cell imaging with 1 μ m DALG reen staining. (D) Live‐cell imaging of 4 h rapamycin treated HeLa cells colabeling with 1 μ m DALG reen and tag RFP ‐ LC 3. Bars = 10 μm.
    Mouse Anti Actin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 934 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore anti actin antibody ab 1
    (A–C) HeLa cells stimulating by nutrient‐deprivation were analyzed in every 2 h. Bars = 20 μm. (A) Relative expression level of LC 3‐I and LC 3‐ II were detected using with anti‐ LC 3 antibody and <t>anti‐actin</t> antibody for loading control of western blotting analysis. (B) Immunocytochemical analysis with anti‐ LC 3 antibodies (Green) and DAPI (Blue). (C) Live‐cell imaging with 1 μ m DALG reen staining. (D) Live‐cell imaging of 4 h rapamycin treated HeLa cells colabeling with 1 μ m DALG reen and tag RFP ‐ LC 3. Bars = 10 μm.
    Anti Actin Antibody Ab 1, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology anti actin polyclonal ab i 19
    (A–C) HeLa cells stimulating by nutrient‐deprivation were analyzed in every 2 h. Bars = 20 μm. (A) Relative expression level of LC 3‐I and LC 3‐ II were detected using with anti‐ LC 3 antibody and <t>anti‐actin</t> antibody for loading control of western blotting analysis. (B) Immunocytochemical analysis with anti‐ LC 3 antibodies (Green) and DAPI (Blue). (C) Live‐cell imaging with 1 μ m DALG reen staining. (D) Live‐cell imaging of 4 h rapamycin treated HeLa cells colabeling with 1 μ m DALG reen and tag RFP ‐ LC 3. Bars = 10 μm.
    Anti Actin Polyclonal Ab I 19, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Effect of TSN on expression of HCV replicon. (A) HCV replicon cells were treated with various concentrations of TSN for 48 h. Replication levels of HCV RNA were analyzed by luciferase assay. Bars indicate luciferase activities relative to that of the drug-negative control. (B) Cell viability was determined by MTS assay. Bars indicate the value relative to that of the drug-negative control. (C) Western blotting analyses. The expression of NS5A and beta-actin was detected using anti-NS5A and anti-beta-actin antibodies. Densitometry of NS5A protein was performed, and the result is indicated as a percentage of the result for the drug-negative control. The assay was repeated three times, and a representative result is shown. (D) A bicistronic reporter gene plasmid, pCIneo-Rluc-IRES-Fluc, was transfected into Huh7 cells. The cells were cultured with TSN at the concentrations indicated, and dual luciferase activities were measured after 24 h of treatment. Values are displayed as ratios of Fluc to Rluc. In panels A, B, and D, the assays were done in triplicate and repeated three times. Error bars indicate means ± SDs.

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: Inhibitory Effect of a Triterpenoid Compound, with or without Alpha Interferon, on Hepatitis C Virus Infection ▿Inhibitory Effect of a Triterpenoid Compound, with or without Alpha Interferon, on Hepatitis C Virus Infection ▿ †

    doi: 10.1128/AAC.01780-10

    Figure Lengend Snippet: Effect of TSN on expression of HCV replicon. (A) HCV replicon cells were treated with various concentrations of TSN for 48 h. Replication levels of HCV RNA were analyzed by luciferase assay. Bars indicate luciferase activities relative to that of the drug-negative control. (B) Cell viability was determined by MTS assay. Bars indicate the value relative to that of the drug-negative control. (C) Western blotting analyses. The expression of NS5A and beta-actin was detected using anti-NS5A and anti-beta-actin antibodies. Densitometry of NS5A protein was performed, and the result is indicated as a percentage of the result for the drug-negative control. The assay was repeated three times, and a representative result is shown. (D) A bicistronic reporter gene plasmid, pCIneo-Rluc-IRES-Fluc, was transfected into Huh7 cells. The cells were cultured with TSN at the concentrations indicated, and dual luciferase activities were measured after 24 h of treatment. Values are displayed as ratios of Fluc to Rluc. In panels A, B, and D, the assays were done in triplicate and repeated three times. Error bars indicate means ± SDs.

    Article Snippet: The antibodies used were mouse anti-NS5A (BioDesign, ME), rabbit anti-signal transducer and activator of transcription 1 (anti-STAT1) p84/p91, rabbit anti-phospho-STAT1 (Tyr 701), rabbit anti-STAT2, rabbit anti-phospho-STAT2 (Tyr 690) (Santa Cruz, CA), and anti-beta-actin antibody (Sigma).

    Techniques: Expressing, Luciferase, Negative Control, MTS Assay, Western Blot, Plasmid Preparation, Transfection, Cell Culture

    ISRE reporter screening and aberrant pathway of α-IFN. (A) Pretreatment with TSN. Huh7 cells transfected with a reporter gene (pISRE-Luc and pRL-CMV) were pretreated with TSN (0 or 100 nM) for 0, 24, or 48 h, followed by treatment with α-IFN (0 or 100 IU/ml). Six hours later, the relative ISRE-luciferase activity ( n = 4) was determined as described in Materials and Methods. The data are expressed as means ± SDs and are a representative example of the data from three similar experiments. (B) Pretreatment with TSN at the concentrations indicated for 24 h, followed by treatment with α-IFN (0 to 100 IU/ml). The ISRE reporter assay was performed as described for panel A. (C) Type I IFN-induced antiviral ISG expression in Huh7 cells. Huh7 cells were treated with TSN for 24 h, followed by treatment with α-IFN at 100 IU/ml for 24 h. The total cellular RNA was then isolated for real-time RT-PCR analysis of the mRNAs of 25AS, MxA, p56, viperin, and ISG20. Beta-actin was used as a control. The data are expressed as means ± SDs and are a representative example of data from three similar experiments. *, P

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: Inhibitory Effect of a Triterpenoid Compound, with or without Alpha Interferon, on Hepatitis C Virus Infection ▿Inhibitory Effect of a Triterpenoid Compound, with or without Alpha Interferon, on Hepatitis C Virus Infection ▿ †

    doi: 10.1128/AAC.01780-10

    Figure Lengend Snippet: ISRE reporter screening and aberrant pathway of α-IFN. (A) Pretreatment with TSN. Huh7 cells transfected with a reporter gene (pISRE-Luc and pRL-CMV) were pretreated with TSN (0 or 100 nM) for 0, 24, or 48 h, followed by treatment with α-IFN (0 or 100 IU/ml). Six hours later, the relative ISRE-luciferase activity ( n = 4) was determined as described in Materials and Methods. The data are expressed as means ± SDs and are a representative example of the data from three similar experiments. (B) Pretreatment with TSN at the concentrations indicated for 24 h, followed by treatment with α-IFN (0 to 100 IU/ml). The ISRE reporter assay was performed as described for panel A. (C) Type I IFN-induced antiviral ISG expression in Huh7 cells. Huh7 cells were treated with TSN for 24 h, followed by treatment with α-IFN at 100 IU/ml for 24 h. The total cellular RNA was then isolated for real-time RT-PCR analysis of the mRNAs of 25AS, MxA, p56, viperin, and ISG20. Beta-actin was used as a control. The data are expressed as means ± SDs and are a representative example of data from three similar experiments. *, P

    Article Snippet: The antibodies used were mouse anti-NS5A (BioDesign, ME), rabbit anti-signal transducer and activator of transcription 1 (anti-STAT1) p84/p91, rabbit anti-phospho-STAT1 (Tyr 701), rabbit anti-STAT2, rabbit anti-phospho-STAT2 (Tyr 690) (Santa Cruz, CA), and anti-beta-actin antibody (Sigma).

    Techniques: Transfection, Luciferase, Activity Assay, Reporter Assay, Expressing, Isolation, Quantitative RT-PCR

    Suppression of HCV RNA replication by TSN combined with α-IFN. (A and B) Luciferase activity (A, absolute value; B, relative value). Huh7/Rep-Feo cells, which constitutively express an HCV replicon, enable the quantification of replication levels through the measurement of luciferase activity. Absolute and relative dose-response curves in the presence of 24 h of pretreatment of various concentrations of TSN (0, 0.01, 0.03 μg/ml) and α-IFN (0, 100 IU/ml). (A) Bars indicate luciferase activities. (B) Bars indicate luciferase activities relative to the activity of each α-IFN-negative control. Luciferase assays were performed in triplicate. Error bars indicate means ± SDs. (C) MTS assay of Huh7/Rep-Feo cells cultured with the indicated concentrations of TSN and α-IFN. The assays were done in triplicate and repeated three times. Error bars indicate means ± SDs. (D) Western blotting. Ten micrograms of total cellular protein was separated by polyacrylamide gel electrophoresis and transferred onto the membrane. Monoclonal anti-NS5A antibody or an anti-beta-actin antibody was used as the primary antibody. Densitometry of NS5A or beta-actin protein was performed and the result is indicated as a percentage of that for the drug-negative control. The assay was repeated three times, and representative results are shown. (E) Dose-inhibition curves of α-IFN and TSN when they were combined at the indicated ratios, adjusted by the EC 50 of the individual drug. Assays were done in triplicate, and mean values were plotted and indicated as means ± SDs. (F) Graphical representation of the isobologram analysis. For each drug combination in panel E, the EC 50 s of α-IFN and TSN for inhibition of HCV replication were plotted against the fractional concentrations of α-IFN and TSN, which are indicated on the x and y axes, respectively. A theoretical line of additivity is drawn between the EC 50 for each drug alone. All of the fractional EC 50 plots for the TSN and α-IFN combinations fell below the line of additivity, indicating synergy.

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: Inhibitory Effect of a Triterpenoid Compound, with or without Alpha Interferon, on Hepatitis C Virus Infection ▿Inhibitory Effect of a Triterpenoid Compound, with or without Alpha Interferon, on Hepatitis C Virus Infection ▿ †

    doi: 10.1128/AAC.01780-10

    Figure Lengend Snippet: Suppression of HCV RNA replication by TSN combined with α-IFN. (A and B) Luciferase activity (A, absolute value; B, relative value). Huh7/Rep-Feo cells, which constitutively express an HCV replicon, enable the quantification of replication levels through the measurement of luciferase activity. Absolute and relative dose-response curves in the presence of 24 h of pretreatment of various concentrations of TSN (0, 0.01, 0.03 μg/ml) and α-IFN (0, 100 IU/ml). (A) Bars indicate luciferase activities. (B) Bars indicate luciferase activities relative to the activity of each α-IFN-negative control. Luciferase assays were performed in triplicate. Error bars indicate means ± SDs. (C) MTS assay of Huh7/Rep-Feo cells cultured with the indicated concentrations of TSN and α-IFN. The assays were done in triplicate and repeated three times. Error bars indicate means ± SDs. (D) Western blotting. Ten micrograms of total cellular protein was separated by polyacrylamide gel electrophoresis and transferred onto the membrane. Monoclonal anti-NS5A antibody or an anti-beta-actin antibody was used as the primary antibody. Densitometry of NS5A or beta-actin protein was performed and the result is indicated as a percentage of that for the drug-negative control. The assay was repeated three times, and representative results are shown. (E) Dose-inhibition curves of α-IFN and TSN when they were combined at the indicated ratios, adjusted by the EC 50 of the individual drug. Assays were done in triplicate, and mean values were plotted and indicated as means ± SDs. (F) Graphical representation of the isobologram analysis. For each drug combination in panel E, the EC 50 s of α-IFN and TSN for inhibition of HCV replication were plotted against the fractional concentrations of α-IFN and TSN, which are indicated on the x and y axes, respectively. A theoretical line of additivity is drawn between the EC 50 for each drug alone. All of the fractional EC 50 plots for the TSN and α-IFN combinations fell below the line of additivity, indicating synergy.

    Article Snippet: The antibodies used were mouse anti-NS5A (BioDesign, ME), rabbit anti-signal transducer and activator of transcription 1 (anti-STAT1) p84/p91, rabbit anti-phospho-STAT1 (Tyr 701), rabbit anti-STAT2, rabbit anti-phospho-STAT2 (Tyr 690) (Santa Cruz, CA), and anti-beta-actin antibody (Sigma).

    Techniques: Luciferase, Activity Assay, Negative Control, MTS Assay, Cell Culture, Western Blot, Polyacrylamide Gel Electrophoresis, Inhibition

    Expression of proteins which were reported to be associated with sensitivity to anti-microtubule agents. (A) Protein expression was evaluated by western blot analysis. Expression values of class Ⅲ beta-tubulin (TUBB3) relative to beta-actin were determined using Just TLC software. (B) Representative images of HCC4006 and HCC4006ER cells immunohistochemically stained with antibodies to ATP-binding cassette subfamily B, member 1 (ABCB1).

    Journal: PLoS ONE

    Article Title: Collateral Chemoresistance to Anti-Microtubule Agents in a Lung Cancer Cell Line with Acquired Resistance to Erlotinib

    doi: 10.1371/journal.pone.0123901

    Figure Lengend Snippet: Expression of proteins which were reported to be associated with sensitivity to anti-microtubule agents. (A) Protein expression was evaluated by western blot analysis. Expression values of class Ⅲ beta-tubulin (TUBB3) relative to beta-actin were determined using Just TLC software. (B) Representative images of HCC4006 and HCC4006ER cells immunohistochemically stained with antibodies to ATP-binding cassette subfamily B, member 1 (ABCB1).

    Article Snippet: Antibodies and western blot analysis Anti-E-cadherin, anti-ATP-binding cassette subfamily B, member 1 (ABCB1), anti-class III beta-tubulin (TUBB3) and anti-beta-actin antibodies were purchased from Cell Signaling Technology (Beverly, MA).

    Techniques: Expressing, Western Blot, Thin Layer Chromatography, Software, Staining, Binding Assay

    Effects of MEKS on the activations of apoptosis-related proteins. MDA-MB-231 cells were treated with 0, 25, or 50 μg/ml of MEKS for 4 h or 30 nM paclitaxel for 24 h (positive control). Protein expressions of cleaved caspase 3 (C), 8 (B) and 9 (A), cleaved PARP (D) and beta-actin (the loading control) were detected by Western blotting

    Journal: Pharmacognosy Magazine

    Article Title: Anti-cancer effects of Kochia scoparia fruit in human breast cancer cells

    doi: 10.4103/0973-1296.139812

    Figure Lengend Snippet: Effects of MEKS on the activations of apoptosis-related proteins. MDA-MB-231 cells were treated with 0, 25, or 50 μg/ml of MEKS for 4 h or 30 nM paclitaxel for 24 h (positive control). Protein expressions of cleaved caspase 3 (C), 8 (B) and 9 (A), cleaved PARP (D) and beta-actin (the loading control) were detected by Western blotting

    Article Snippet: The antibodies targeting cleaved caspase 3, cleaved caspase 8, cleaved caspase 9 and cleaved Poly (ADP-ribose) polymerase (PARP) were purchased from Cell Signaling Technology (Beverly, MA, USA), while anti-beta actin antibody was purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Multiple Displacement Amplification, Positive Control, Western Blot

    Leptin required functional leptin receptor (Ob-R) for activation of PI3-kinase/AKT signaling in EOC cell lines . MDAH2774 cells were transfected with scrambled siRNA and Ob-R siRNA (50 and 100 nM) with Lipofectamine. After 48 hours, cells were starved and treated with 100 ng/ml for 3 hours and proteins were immuno-blotted with antibodies against Ob-R, p-AKT-Ser473, and FOXO1, Bcl-XL, XIAP and beta actin.

    Journal: Molecular Cancer

    Article Title: Overexpression of leptin receptor predicts an unfavorable outcome in Middle Eastern ovarian cancer

    doi: 10.1186/1476-4598-8-74

    Figure Lengend Snippet: Leptin required functional leptin receptor (Ob-R) for activation of PI3-kinase/AKT signaling in EOC cell lines . MDAH2774 cells were transfected with scrambled siRNA and Ob-R siRNA (50 and 100 nM) with Lipofectamine. After 48 hours, cells were starved and treated with 100 ng/ml for 3 hours and proteins were immuno-blotted with antibodies against Ob-R, p-AKT-Ser473, and FOXO1, Bcl-XL, XIAP and beta actin.

    Article Snippet: Beta-actin antibody was purchased from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA, USA).

    Techniques: Functional Assay, Activation Assay, Transfection

    Leptin activate PI3-kinase/AKT signaling pathway . ( A ) MDAH2774 cells were serum starved for 24 hours in serum free medium, followed by stimulation with recombinant leptin (100 ng/ml) for various time periods as indicated. After cell lysis, 20 μg proteins were separated by SDS-PAGE, transferred to immobilon membrane, and immunoblotted with antibodies against p-AKT-Ser 473, FOXO1, and beta actin. ( B ) Inhibition of PI3-kinase/AKT pathway prevented leptin-induced activation of AKT pathway in EOC cells. SKOV3 cells were serum starved in the presence and absence of LY294002 as indicated for 48 hours and subsequently stimulated with 100 ng/ml of recombinant leptin for 3 hours, Cells were lysed and proteins were separated by SDS-PAGE, transferred to immobilon membrane, and immunoblotted with antibodies against p-AKT-Ser 473, FOXO1, and beta actin. ( C ) LY294002-inhibitor abrogate leptin-mediated cell proliferation and prevented leptin-induced anti-apoptotic effects in EOC cells. MADH2774 and SKOV3 cells were serum starved in the presence and absence of LY294002 as indicated and subsequently stimulated with 100 ng/ml of recombinant leptin for 48 hours. Cell proliferation was measured by MTT assays and ( D ) apoptosis was measured by Anenexin/PI staining. The graph displays the mean +/- SD of six independent experiments (* p

    Journal: Molecular Cancer

    Article Title: Overexpression of leptin receptor predicts an unfavorable outcome in Middle Eastern ovarian cancer

    doi: 10.1186/1476-4598-8-74

    Figure Lengend Snippet: Leptin activate PI3-kinase/AKT signaling pathway . ( A ) MDAH2774 cells were serum starved for 24 hours in serum free medium, followed by stimulation with recombinant leptin (100 ng/ml) for various time periods as indicated. After cell lysis, 20 μg proteins were separated by SDS-PAGE, transferred to immobilon membrane, and immunoblotted with antibodies against p-AKT-Ser 473, FOXO1, and beta actin. ( B ) Inhibition of PI3-kinase/AKT pathway prevented leptin-induced activation of AKT pathway in EOC cells. SKOV3 cells were serum starved in the presence and absence of LY294002 as indicated for 48 hours and subsequently stimulated with 100 ng/ml of recombinant leptin for 3 hours, Cells were lysed and proteins were separated by SDS-PAGE, transferred to immobilon membrane, and immunoblotted with antibodies against p-AKT-Ser 473, FOXO1, and beta actin. ( C ) LY294002-inhibitor abrogate leptin-mediated cell proliferation and prevented leptin-induced anti-apoptotic effects in EOC cells. MADH2774 and SKOV3 cells were serum starved in the presence and absence of LY294002 as indicated and subsequently stimulated with 100 ng/ml of recombinant leptin for 48 hours. Cell proliferation was measured by MTT assays and ( D ) apoptosis was measured by Anenexin/PI staining. The graph displays the mean +/- SD of six independent experiments (* p

    Article Snippet: Beta-actin antibody was purchased from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA, USA).

    Techniques: Recombinant, Lysis, SDS Page, Inhibition, Activation Assay, MTT Assay, Staining

    CD47 is highly expressed in osteosarcoma Quantitative RT-PCR A. and immunoblot analysis B. showed CD47 expression in ten freshly isolated osteosarcoma tissues and their adjacent nontumorous tissues. Beta-actin was treated as the reference control. CD47 immunostaining C. showed higher of CD47 expression in osteosarcoma of the same samples with or without metastasis and their adjacent nontumorous tissues. The tissues were counterstained with DAPI Fluorescent Stain. Representative images are shown here. (magnification × 100). D. Flow-cytometry analysis of CD47 and CD44 expressions on osteosarcoma tumor cells and quantification of CD44 cells also expressing CD47.

    Journal: Oncotarget

    Article Title: CD47 blockade inhibits tumor progression human osteosarcoma in xenograft models

    doi:

    Figure Lengend Snippet: CD47 is highly expressed in osteosarcoma Quantitative RT-PCR A. and immunoblot analysis B. showed CD47 expression in ten freshly isolated osteosarcoma tissues and their adjacent nontumorous tissues. Beta-actin was treated as the reference control. CD47 immunostaining C. showed higher of CD47 expression in osteosarcoma of the same samples with or without metastasis and their adjacent nontumorous tissues. The tissues were counterstained with DAPI Fluorescent Stain. Representative images are shown here. (magnification × 100). D. Flow-cytometry analysis of CD47 and CD44 expressions on osteosarcoma tumor cells and quantification of CD44 cells also expressing CD47.

    Article Snippet: After stripping with Restore Western Blot Stripping Buffer (Pierce) for 20 min at room temperature, membranes were processed similarly with anti-beta-actin antibody (1:2, 000 dilution, Abcam) as a loading control.

    Techniques: Quantitative RT-PCR, Expressing, Isolation, Immunostaining, Staining, Flow Cytometry, Cytometry

    RUNX2 associates with p53 in response to ADR. ( a ) Indirect immunostaining experiments. U2OS cells were treated with 1.0 μ M of ADR or left untreated. Twenty-four hours after ADR treatment, cells were simultaneously incubated with monoclonal anti-p53 and polyclonal anti-RUNX2 antibodies followed by the incubation with rhodamine-conjugated anti-mouse IgG (red) and fluorescein isothiocyanate (FITC)-conjugated anti-rabbit IgG (green). Cell nuclei were stained with DAPI (blue). Merged images (yellow) indicate the colocalization of RUNX2 with p53 in cell nucleus. ( b and c ) Co-immunoprecipitation experiments. U2OS cells were exposed to 0.5 μ M of ADR ( b ) or left untreated ( c ). Twenty-four hours after ADR treatment, cell lysates were prepared and immunoprecipitated with NMS or with monoclonal anti-p53 antibody. The immunoprecipitates were analyzed by immnublotting with monoclonal anti-RUNX2 antibody. The reciprocal experiments and 1/20 of inputs were also shown

    Journal: Cell Death & Disease

    Article Title: Runt-related transcription factor 2 (RUNX2) inhibits p53-dependent apoptosis through the collaboration with HDAC6 in response to DNA damage

    doi: 10.1038/cddis.2013.127

    Figure Lengend Snippet: RUNX2 associates with p53 in response to ADR. ( a ) Indirect immunostaining experiments. U2OS cells were treated with 1.0 μ M of ADR or left untreated. Twenty-four hours after ADR treatment, cells were simultaneously incubated with monoclonal anti-p53 and polyclonal anti-RUNX2 antibodies followed by the incubation with rhodamine-conjugated anti-mouse IgG (red) and fluorescein isothiocyanate (FITC)-conjugated anti-rabbit IgG (green). Cell nuclei were stained with DAPI (blue). Merged images (yellow) indicate the colocalization of RUNX2 with p53 in cell nucleus. ( b and c ) Co-immunoprecipitation experiments. U2OS cells were exposed to 0.5 μ M of ADR ( b ) or left untreated ( c ). Twenty-four hours after ADR treatment, cell lysates were prepared and immunoprecipitated with NMS or with monoclonal anti-p53 antibody. The immunoprecipitates were analyzed by immnublotting with monoclonal anti-RUNX2 antibody. The reciprocal experiments and 1/20 of inputs were also shown

    Article Snippet: After blocking, the membrane was incubated with monoclonal anti-p53 (DO-1, Santa Cruz Biotechnologies, Santa Cruz, CA, USA), monoclonal anti-RUNX2 (8G5, Medical and Biological Laboratories, Nagoya, Japan), polyclonal anti-phospho-p53 at Ser-15 (Cell Signaling Technologies, Beverly, MA, USA), polyclonal anti-acetyl-p53 at Lys-373/382 (Millipore), polyclonal anti-p21WAF1 (H-164, Santa Cruz Biotechnologies), polyclonal anti-BAX (Cell Signaling Technologies), polyclonal anti-PARP (Cell Signaling Technologies), polyclonal anti-HDAC6 (Cell Signaling Technologies) or with polyclonal anti-actin antibody (20-33, Sigma) at room temperature for 1 h. After washing with TBS-T, the membrane was then incubated with HRP-conjugated anti-mouse IgG or with HRP-conjugated anti-rabbit IgG (Invitrogen) at room temperature for 1 h. The membrane was extensively washed with TBS-T and the immunoblotted proteins were then visualized by enhanced chemiluminescence (ECL, Amersham Biosciences, Piscataway, NJ, USA).

    Techniques: Immunostaining, Incubation, Staining, Immunoprecipitation

    Interaction among p53, RUNX2 and HDAC6. Co-immunoprecipitation. U2OS cells were left untreated ( a ) or treated with 0.5 μ M of ADR ( b ). Twenty-four hours after ADR treatment, cell lysates were prepared and immunoprecipitated with NRS or with polyclonal anti-HDAC6 antibody followed by immunoblotting with the indicated antibodies. Reciprocal immunoprecipitation experiments using NMS or monoclonal anti-RUNX2 and 1/20 of input were also shown

    Journal: Cell Death & Disease

    Article Title: Runt-related transcription factor 2 (RUNX2) inhibits p53-dependent apoptosis through the collaboration with HDAC6 in response to DNA damage

    doi: 10.1038/cddis.2013.127

    Figure Lengend Snippet: Interaction among p53, RUNX2 and HDAC6. Co-immunoprecipitation. U2OS cells were left untreated ( a ) or treated with 0.5 μ M of ADR ( b ). Twenty-four hours after ADR treatment, cell lysates were prepared and immunoprecipitated with NRS or with polyclonal anti-HDAC6 antibody followed by immunoblotting with the indicated antibodies. Reciprocal immunoprecipitation experiments using NMS or monoclonal anti-RUNX2 and 1/20 of input were also shown

    Article Snippet: After blocking, the membrane was incubated with monoclonal anti-p53 (DO-1, Santa Cruz Biotechnologies, Santa Cruz, CA, USA), monoclonal anti-RUNX2 (8G5, Medical and Biological Laboratories, Nagoya, Japan), polyclonal anti-phospho-p53 at Ser-15 (Cell Signaling Technologies, Beverly, MA, USA), polyclonal anti-acetyl-p53 at Lys-373/382 (Millipore), polyclonal anti-p21WAF1 (H-164, Santa Cruz Biotechnologies), polyclonal anti-BAX (Cell Signaling Technologies), polyclonal anti-PARP (Cell Signaling Technologies), polyclonal anti-HDAC6 (Cell Signaling Technologies) or with polyclonal anti-actin antibody (20-33, Sigma) at room temperature for 1 h. After washing with TBS-T, the membrane was then incubated with HRP-conjugated anti-mouse IgG or with HRP-conjugated anti-rabbit IgG (Invitrogen) at room temperature for 1 h. The membrane was extensively washed with TBS-T and the immunoblotted proteins were then visualized by enhanced chemiluminescence (ECL, Amersham Biosciences, Piscataway, NJ, USA).

    Techniques: Immunoprecipitation

    Tnmd expression in human musculoskeletal elements and mechano-regulation. (a) Representative western blot with anti-C-terminal Tnmd antibody on human (tendon, MTJ myotendinous junction, muscle and bone) and mouse (tendon) tissues. Detection of beta actin served as loading control. (b) Representative immunofluorescent detection of Tnmd in human and mouse Achilles tendons. Tnmd expression in green and nuclear DAPI in blue colour. Upper panel: low magnification epi-fluorescence images; lower panel: confocal microscopy. (c) Semi-quantitative PCR for Tnmd expression in cultured human TSPC (passage 0 and 3). The house-keeping gene GAPDH was used for normalization. Western blotting, staining and PCR were reproduced three times (n = 3). (d) Luciferase activity assays (expressed in RLU, relative light units) with human TSPC transfected with a promoter-less (mock-luc) or Tnmd promoter (− 769/+84F Tnmd genomic fragment)-driven luciferase (pTnmd-luc) plasmids without or undergoing mechanical stimulation of 5% axial strain. Two independent stimulations with two different donors were carried out (n = 4). (e) Semi-quantitative PCR bands and densitometric evaluation of Tnmd expression against GAPDH in human TSPC (passage 3) prior and after mechanical stimulation (presented in fold change). Statistical significance: ***p

    Journal: EBioMedicine

    Article Title: Tenomodulin is Required for Tendon Endurance Running and Collagen I Fibril Adaptation to Mechanical Load

    doi: 10.1016/j.ebiom.2017.05.003

    Figure Lengend Snippet: Tnmd expression in human musculoskeletal elements and mechano-regulation. (a) Representative western blot with anti-C-terminal Tnmd antibody on human (tendon, MTJ myotendinous junction, muscle and bone) and mouse (tendon) tissues. Detection of beta actin served as loading control. (b) Representative immunofluorescent detection of Tnmd in human and mouse Achilles tendons. Tnmd expression in green and nuclear DAPI in blue colour. Upper panel: low magnification epi-fluorescence images; lower panel: confocal microscopy. (c) Semi-quantitative PCR for Tnmd expression in cultured human TSPC (passage 0 and 3). The house-keeping gene GAPDH was used for normalization. Western blotting, staining and PCR were reproduced three times (n = 3). (d) Luciferase activity assays (expressed in RLU, relative light units) with human TSPC transfected with a promoter-less (mock-luc) or Tnmd promoter (− 769/+84F Tnmd genomic fragment)-driven luciferase (pTnmd-luc) plasmids without or undergoing mechanical stimulation of 5% axial strain. Two independent stimulations with two different donors were carried out (n = 4). (e) Semi-quantitative PCR bands and densitometric evaluation of Tnmd expression against GAPDH in human TSPC (passage 3) prior and after mechanical stimulation (presented in fold change). Statistical significance: ***p

    Article Snippet: A mouse anti-beta-actin antibody cross-reacting with mouse and human beta-actin (Abcam, Cambridge, United Kingdom) was used as a loading control.

    Techniques: Expressing, Western Blot, Fluorescence, Confocal Microscopy, Real-time Polymerase Chain Reaction, Cell Culture, Staining, Polymerase Chain Reaction, Luciferase, Activity Assay, Transfection

    (A–C) HeLa cells stimulating by nutrient‐deprivation were analyzed in every 2 h. Bars = 20 μm. (A) Relative expression level of LC 3‐I and LC 3‐ II were detected using with anti‐ LC 3 antibody and anti‐actin antibody for loading control of western blotting analysis. (B) Immunocytochemical analysis with anti‐ LC 3 antibodies (Green) and DAPI (Blue). (C) Live‐cell imaging with 1 μ m DALG reen staining. (D) Live‐cell imaging of 4 h rapamycin treated HeLa cells colabeling with 1 μ m DALG reen and tag RFP ‐ LC 3. Bars = 10 μm.

    Journal: Febs Letters

    Article Title: Small fluorescent molecules for monitoring autophagic flux

    doi: 10.1002/1873-3468.12979

    Figure Lengend Snippet: (A–C) HeLa cells stimulating by nutrient‐deprivation were analyzed in every 2 h. Bars = 20 μm. (A) Relative expression level of LC 3‐I and LC 3‐ II were detected using with anti‐ LC 3 antibody and anti‐actin antibody for loading control of western blotting analysis. (B) Immunocytochemical analysis with anti‐ LC 3 antibodies (Green) and DAPI (Blue). (C) Live‐cell imaging with 1 μ m DALG reen staining. (D) Live‐cell imaging of 4 h rapamycin treated HeLa cells colabeling with 1 μ m DALG reen and tag RFP ‐ LC 3. Bars = 10 μm.

    Article Snippet: The samples were separated on SDS/PAGE, transferred onto a poly(vinylidene difluoride) membrane (Trans‐Blot Turbo, BIO‐RAD), and detected with a rabbit anti‐LC3 antibody (PD014, MBL) and a mouse anti‐actin antibody (MAB1501, Millipore).

    Techniques: Expressing, Western Blot, Live Cell Imaging, Staining