β actin antibodies  (Millipore)

 
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    Millipore β actin antibodies
    Knockout of EZH2 gene by CRISPR/Cas9 and stable infection of EBV. (A) Loss of EZH2 expression in the EZH2-KO Akata(−) cells. Two independent clones were used (named cl1 and cl2) for both WT and KO. Levels of EZH2, H3K27me3, histone H3, and <t>β-actin</t> in the samples from WT and EZH2-KO cells were examined by Western blotting. (B) Growth kinetics of EZH2-KO Akata(−) cells. A quantity of 1.0 × 10 5 cells/ml was seeded and cultured. Cell numbers were counted after the indicated number of days. (C) Reduced growth speed in the EZH2-KO cells. The WT and EZH2-KO Akata cells were infected with EBV and cultured in the presence of G418. At 0, 4, 8, and 12 weeks postinfection, cells were seeded at 1.0 × 10 5 cells/ml, and cell numbers were counted after 3 days. The average and SD from 2 independent replicates are shown as a ratio relative to the value of the starting point (0 week). Student’s t test was performed, and asterisks indicate statistical significance (*, P
    β Actin Antibodies, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/β actin antibodies/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    β actin antibodies - by Bioz Stars, 2021-03
    99/100 stars

    Images

    1) Product Images from "Regulation of Epstein-Barr Virus Life Cycle and Cell Proliferation by Histone H3K27 Methyltransferase EZH2 in Akata Cells"

    Article Title: Regulation of Epstein-Barr Virus Life Cycle and Cell Proliferation by Histone H3K27 Methyltransferase EZH2 in Akata Cells

    Journal: mSphere

    doi: 10.1128/mSphere.00478-18

    Knockout of EZH2 gene by CRISPR/Cas9 and stable infection of EBV. (A) Loss of EZH2 expression in the EZH2-KO Akata(−) cells. Two independent clones were used (named cl1 and cl2) for both WT and KO. Levels of EZH2, H3K27me3, histone H3, and β-actin in the samples from WT and EZH2-KO cells were examined by Western blotting. (B) Growth kinetics of EZH2-KO Akata(−) cells. A quantity of 1.0 × 10 5 cells/ml was seeded and cultured. Cell numbers were counted after the indicated number of days. (C) Reduced growth speed in the EZH2-KO cells. The WT and EZH2-KO Akata cells were infected with EBV and cultured in the presence of G418. At 0, 4, 8, and 12 weeks postinfection, cells were seeded at 1.0 × 10 5 cells/ml, and cell numbers were counted after 3 days. The average and SD from 2 independent replicates are shown as a ratio relative to the value of the starting point (0 week). Student’s t test was performed, and asterisks indicate statistical significance (*, P
    Figure Legend Snippet: Knockout of EZH2 gene by CRISPR/Cas9 and stable infection of EBV. (A) Loss of EZH2 expression in the EZH2-KO Akata(−) cells. Two independent clones were used (named cl1 and cl2) for both WT and KO. Levels of EZH2, H3K27me3, histone H3, and β-actin in the samples from WT and EZH2-KO cells were examined by Western blotting. (B) Growth kinetics of EZH2-KO Akata(−) cells. A quantity of 1.0 × 10 5 cells/ml was seeded and cultured. Cell numbers were counted after the indicated number of days. (C) Reduced growth speed in the EZH2-KO cells. The WT and EZH2-KO Akata cells were infected with EBV and cultured in the presence of G418. At 0, 4, 8, and 12 weeks postinfection, cells were seeded at 1.0 × 10 5 cells/ml, and cell numbers were counted after 3 days. The average and SD from 2 independent replicates are shown as a ratio relative to the value of the starting point (0 week). Student’s t test was performed, and asterisks indicate statistical significance (*, P

    Techniques Used: Knock-Out, CRISPR, Infection, Expressing, Clone Assay, Western Blot, Cell Culture

    Increased viral gene expression in WT and EZH2-KO Akata cells during lytic phase. (A to H) WT and EZH2-KO cells latently infected with EBV were treated with anti-IgG. RNA was harvested from the cells at 0 (latency), 1, and 2 days postinduction (dpi) and subjected to qRT-PCR analysis. The data are normalized and shown as fold change for the average and SD from three samples. (I) WT and EZH2-KO cells latently infected with EBV were treated with anti-IgG as in panels A to H. Protein samples were collected on days 0 and 2, and LMP1, BZLF1, BRLF1, BALF2, BMRF1, gB, and β-actin levels were assessed by Western blotting. Student’s t test was performed, and asterisks indicate statistical significance (*, P
    Figure Legend Snippet: Increased viral gene expression in WT and EZH2-KO Akata cells during lytic phase. (A to H) WT and EZH2-KO cells latently infected with EBV were treated with anti-IgG. RNA was harvested from the cells at 0 (latency), 1, and 2 days postinduction (dpi) and subjected to qRT-PCR analysis. The data are normalized and shown as fold change for the average and SD from three samples. (I) WT and EZH2-KO cells latently infected with EBV were treated with anti-IgG as in panels A to H. Protein samples were collected on days 0 and 2, and LMP1, BZLF1, BRLF1, BALF2, BMRF1, gB, and β-actin levels were assessed by Western blotting. Student’s t test was performed, and asterisks indicate statistical significance (*, P

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

    2) Product Images from "Regulation of Epstein-Barr Virus Life Cycle and Cell Proliferation by Histone H3K27 Methyltransferase EZH2 in Akata Cells"

    Article Title: Regulation of Epstein-Barr Virus Life Cycle and Cell Proliferation by Histone H3K27 Methyltransferase EZH2 in Akata Cells

    Journal: mSphere

    doi: 10.1128/mSphere.00478-18

    Knockout of EZH2 gene by CRISPR/Cas9 and stable infection of EBV. (A) Loss of EZH2 expression in the EZH2-KO Akata(−) cells. Two independent clones were used (named cl1 and cl2) for both WT and KO. Levels of EZH2, H3K27me3, histone H3, and β-actin in the samples from WT and EZH2-KO cells were examined by Western blotting. (B) Growth kinetics of EZH2-KO Akata(−) cells. A quantity of 1.0 × 10 5 cells/ml was seeded and cultured. Cell numbers were counted after the indicated number of days. (C) Reduced growth speed in the EZH2-KO cells. The WT and EZH2-KO Akata cells were infected with EBV and cultured in the presence of G418. At 0, 4, 8, and 12 weeks postinfection, cells were seeded at 1.0 × 10 5 cells/ml, and cell numbers were counted after 3 days. The average and SD from 2 independent replicates are shown as a ratio relative to the value of the starting point (0 week). Student’s t test was performed, and asterisks indicate statistical significance (*, P
    Figure Legend Snippet: Knockout of EZH2 gene by CRISPR/Cas9 and stable infection of EBV. (A) Loss of EZH2 expression in the EZH2-KO Akata(−) cells. Two independent clones were used (named cl1 and cl2) for both WT and KO. Levels of EZH2, H3K27me3, histone H3, and β-actin in the samples from WT and EZH2-KO cells were examined by Western blotting. (B) Growth kinetics of EZH2-KO Akata(−) cells. A quantity of 1.0 × 10 5 cells/ml was seeded and cultured. Cell numbers were counted after the indicated number of days. (C) Reduced growth speed in the EZH2-KO cells. The WT and EZH2-KO Akata cells were infected with EBV and cultured in the presence of G418. At 0, 4, 8, and 12 weeks postinfection, cells were seeded at 1.0 × 10 5 cells/ml, and cell numbers were counted after 3 days. The average and SD from 2 independent replicates are shown as a ratio relative to the value of the starting point (0 week). Student’s t test was performed, and asterisks indicate statistical significance (*, P

    Techniques Used: Knock-Out, CRISPR, Infection, Expressing, Clone Assay, Western Blot, Cell Culture

    Increased viral gene expression in WT and EZH2-KO Akata cells during lytic phase. (A to H) WT and EZH2-KO cells latently infected with EBV were treated with anti-IgG. RNA was harvested from the cells at 0 (latency), 1, and 2 days postinduction (dpi) and subjected to qRT-PCR analysis. The data are normalized and shown as fold change for the average and SD from three samples. (I) WT and EZH2-KO cells latently infected with EBV were treated with anti-IgG as in panels A to H. Protein samples were collected on days 0 and 2, and LMP1, BZLF1, BRLF1, BALF2, BMRF1, gB, and β-actin levels were assessed by Western blotting. Student’s t test was performed, and asterisks indicate statistical significance (*, P
    Figure Legend Snippet: Increased viral gene expression in WT and EZH2-KO Akata cells during lytic phase. (A to H) WT and EZH2-KO cells latently infected with EBV were treated with anti-IgG. RNA was harvested from the cells at 0 (latency), 1, and 2 days postinduction (dpi) and subjected to qRT-PCR analysis. The data are normalized and shown as fold change for the average and SD from three samples. (I) WT and EZH2-KO cells latently infected with EBV were treated with anti-IgG as in panels A to H. Protein samples were collected on days 0 and 2, and LMP1, BZLF1, BRLF1, BALF2, BMRF1, gB, and β-actin levels were assessed by Western blotting. Student’s t test was performed, and asterisks indicate statistical significance (*, P

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

    3) Product Images from "Crosstalk between ATF4 and MTA1/HDAC1 promotes osteosarcoma progression"

    Article Title: Crosstalk between ATF4 and MTA1/HDAC1 promotes osteosarcoma progression

    Journal: Oncotarget

    doi: 10.18632/oncotarget.6940

    MTA1 physically binds with ATF4 Changes in ATF4 under ER stress induced by Thapsigargin (Tg) A. HEK293T cells were treated with Tg (10 nM) over increasing time periods (0, 3, 6, 12, 24 hours). Cell lysates were immunoblotted using antibodies directed against ATF4 and β-actin. Endogenous MTA1 in HEK293 cells without treatment was also probed. B. HEK293 cells were transfected with expression vectors encoding Myc-MTA1 and Flag-ATF4 and immunoprecipitated with IgG control or specific antibodies against Myc or Flag, followed by immunoblotting with the indicated antibodies c. Protein extracts from 143B and ZOS cells were subjected to IP with anti-ATF4 or anti-MTA1 antibody or IgG control, followed by western blot analyses with the indicated antibodies D. Diagrammatic summary of in vitro -translated MTA1 binding with a series of GST-ATF4 proteins.
    Figure Legend Snippet: MTA1 physically binds with ATF4 Changes in ATF4 under ER stress induced by Thapsigargin (Tg) A. HEK293T cells were treated with Tg (10 nM) over increasing time periods (0, 3, 6, 12, 24 hours). Cell lysates were immunoblotted using antibodies directed against ATF4 and β-actin. Endogenous MTA1 in HEK293 cells without treatment was also probed. B. HEK293 cells were transfected with expression vectors encoding Myc-MTA1 and Flag-ATF4 and immunoprecipitated with IgG control or specific antibodies against Myc or Flag, followed by immunoblotting with the indicated antibodies c. Protein extracts from 143B and ZOS cells were subjected to IP with anti-ATF4 or anti-MTA1 antibody or IgG control, followed by western blot analyses with the indicated antibodies D. Diagrammatic summary of in vitro -translated MTA1 binding with a series of GST-ATF4 proteins.

    Techniques Used: Transfection, Expressing, Immunoprecipitation, Western Blot, In Vitro, Binding Assay

    Related Articles

    Incubation:

    Article Title: Apolipoprotein E is an HIV-1-inducible inhibitor of viral production and infectivity in macrophages
    Article Snippet: Supernatants from these lysates were subjected to SDS-polyacrylamide gel electrophoresis and transferred to Immobilon-P PVDF transfer membranes. .. The membranes were then incubated with the following primary antibodies: anti-ApoE (EP1347Y; Abcam), anti-apolipoprotein B (AB742; EMD Millipore), anti-HIV-1 p24 rabbit polyclonal antibody (65–004; Bioacademia, Japan), anti-HIV-1 p24 mouse monoclonal antibody (A2-851-100; Icosagen, Estonia), anti-HIV-1 Env (KD-247) [ ], anti-VSV Glycoprotein (P5D4; Sigma), anti-HA (HA-7; Sigma), and anti- β -actin (AC-15; Sigma). .. After the incubation with HRP-labeled secondary antibodies, proteins were visualized using Western Lightning Plus-ECL (PerkinElmer) and an Amersham Imager 600 imaging system (GE Healthcare).

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    • mouse anti β actin  (Millipore)
    97
    Millipore mouse anti β actin
    K562 cells with ectopic HD5 expression. (A) Screening of cell lines for endogenous HD5 expression. HD5 mRNA levels were measured in total cellular RNA by qRT-PCR and expressed as percentages of <t>β-actin</t> (Act B) mRNA levels. (B) HD5 mRNA expression
    Mouse Anti β Actin, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse anti β actin/product/Millipore
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse anti β actin - by Bioz Stars, 2021-03
    97/100 stars
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    K562 cells with ectopic HD5 expression. (A) Screening of cell lines for endogenous HD5 expression. HD5 mRNA levels were measured in total cellular RNA by qRT-PCR and expressed as percentages of β-actin (Act B) mRNA levels. (B) HD5 mRNA expression

    Journal: Journal of Virology

    Article Title: Studies on the Interaction of Tumor-Derived HD5 Alpha Defensins with Adenoviruses and Implications for Oncolytic Adenovirus Therapy

    doi: 10.1128/JVI.02030-16

    Figure Lengend Snippet: K562 cells with ectopic HD5 expression. (A) Screening of cell lines for endogenous HD5 expression. HD5 mRNA levels were measured in total cellular RNA by qRT-PCR and expressed as percentages of β-actin (Act B) mRNA levels. (B) HD5 mRNA expression

    Article Snippet: After blots were stripped with Restore Western blot striping buffer (Thermo Scientific, Waltham, MA), they were incubated with mouse anti-β-actin (Sigma, St. Louis, MO) (1:5,000).

    Techniques: Expressing, Quantitative RT-PCR, Activated Clotting Time Assay

    ShRNA plasmid design and in vitro LGI1-shRNA downregulation. A) shRNA construct: LGI1-shRNA is under the promoter mU6 (murine U6 small-non-coding-RNA), meanwhile the EGFP (enhanced green fluorescent protein) is under the independent promoter PGK (phosphoglycerate kinase). NeoR/KanR (Neomycin/Kanamycin Resistance). B) LGI1 expression in neuronal cultures. The first lane is the endogenous level of LGI1 in untreated primary cultures, the second lane shows the levels of LGI1 in cultures transduced with scramble virus and the fourth and last lane shows the levels of LGI1 in cultures transduced with shRNA-LGI1. The β-actin and EGFP signals are also shown. EGFP intensity was detected to evaluate that the reporter gene was also expressed at the same time as the shRNA and hence could be a reliable source of transduction rate. C) Quantification of LGI1 concentrations detected by the western blot method. p=0.005 two-tailed Student’s t-test (blots n=5 from 5 distinct preparations).

    Journal: bioRxiv

    Article Title: LGI1 downregulation increases neuronal circuit excitability

    doi: 10.1101/2019.12.17.879833

    Figure Lengend Snippet: ShRNA plasmid design and in vitro LGI1-shRNA downregulation. A) shRNA construct: LGI1-shRNA is under the promoter mU6 (murine U6 small-non-coding-RNA), meanwhile the EGFP (enhanced green fluorescent protein) is under the independent promoter PGK (phosphoglycerate kinase). NeoR/KanR (Neomycin/Kanamycin Resistance). B) LGI1 expression in neuronal cultures. The first lane is the endogenous level of LGI1 in untreated primary cultures, the second lane shows the levels of LGI1 in cultures transduced with scramble virus and the fourth and last lane shows the levels of LGI1 in cultures transduced with shRNA-LGI1. The β-actin and EGFP signals are also shown. EGFP intensity was detected to evaluate that the reporter gene was also expressed at the same time as the shRNA and hence could be a reliable source of transduction rate. C) Quantification of LGI1 concentrations detected by the western blot method. p=0.005 two-tailed Student’s t-test (blots n=5 from 5 distinct preparations).

    Article Snippet: The following antibodies and dilutions were used: 1:250 polyclonal goat-anti-LGI1 (Santa Cruz, c-19), 1:4000 monoclonal mouse-anti β-actin (Sigma), 1:1000 rabbit-anti-GFP (Abcam ab6556).

    Techniques: shRNA, Plasmid Preparation, In Vitro, Construct, Expressing, Transduction, Western Blot, Two Tailed Test

    Effects of various concentrations of the resveratrol on KGN cells. Cells were incubated with resveratrol at 0, 10, 25, 50, and 100 μmol/L for 24 h. A, SIRT1 mRNA levels were assessed by real‐time PCR and calculated after normalization to EF1α mRNA levels. B, The protein levels of SIRT1 were quantified by Western blotting, and β‐actin was used as the control. C, The protein levels were quantified using ImageJ. D, VEGF protein levels were analyzed by ELISA. E, The mtDNA copy number was determined using real‐time PCR. Fold differences are shown compared with the control, for which the value was defined as 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

    Journal: Reproductive Medicine and Biology

    Article Title: Resveratrol protects mitochondrial quantity by activating SIRT1/PGC‐1α expression during ovarian hypoxia, et al. Resveratrol protects mitochondrial quantity by activating SIRT1/PGC‐1α expression during ovarian hypoxia

    doi: 10.1002/rmb2.12323

    Figure Lengend Snippet: Effects of various concentrations of the resveratrol on KGN cells. Cells were incubated with resveratrol at 0, 10, 25, 50, and 100 μmol/L for 24 h. A, SIRT1 mRNA levels were assessed by real‐time PCR and calculated after normalization to EF1α mRNA levels. B, The protein levels of SIRT1 were quantified by Western blotting, and β‐actin was used as the control. C, The protein levels were quantified using ImageJ. D, VEGF protein levels were analyzed by ELISA. E, The mtDNA copy number was determined using real‐time PCR. Fold differences are shown compared with the control, for which the value was defined as 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

    Article Snippet: Blots were then incubated for 1 hour at room temperature (25°C) with rabbit monoclonal SIRT1 antibody (1:400; Santa Cruz Biotechnology, Inc), rabbit monoclonal HIF‐1a antibody (1:1000; Epitomics), or mouse monoclonal β‐actin antibody (1:5000; Sigma‐Aldrich) as the primary antibody, and anti‐rabbit immunoglobulin IgG peroxidase‐labeled secondary antibody (1:10 000; GE Healthcare Life Science) or anti‐mouse IgG peroxidase‐labeled secondary antibody (1:10 000; GE Healthcare Life Science) as the secondary antibody.

    Techniques: Incubation, Real-time Polymerase Chain Reaction, Western Blot, Enzyme-linked Immunosorbent Assay

    Protective effects of resveratrol against CoCl 2 ‐induced hypoxic stress. KGN cells were cultured in medium containing 100 μmol/L CoCl 2 with or without the 50 μmol/L resveratrol. A, SIRT1 mRNA levels were assessed by real‐time PCR and calculated after normalization to EF1α mRNA levels. B, The protein levels of SIRT1 were quantified by Western blotting, and β‐actin was used as the control protein. C, The protein levels were quantified using ImageJ. D, VEGF protein levels were analyzed by ELISA. E, The mtDNA copy number was determined using real‐time PCR. Fold differences are shown compared with the control, for which the value was defined as 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

    Journal: Reproductive Medicine and Biology

    Article Title: Resveratrol protects mitochondrial quantity by activating SIRT1/PGC‐1α expression during ovarian hypoxia, et al. Resveratrol protects mitochondrial quantity by activating SIRT1/PGC‐1α expression during ovarian hypoxia

    doi: 10.1002/rmb2.12323

    Figure Lengend Snippet: Protective effects of resveratrol against CoCl 2 ‐induced hypoxic stress. KGN cells were cultured in medium containing 100 μmol/L CoCl 2 with or without the 50 μmol/L resveratrol. A, SIRT1 mRNA levels were assessed by real‐time PCR and calculated after normalization to EF1α mRNA levels. B, The protein levels of SIRT1 were quantified by Western blotting, and β‐actin was used as the control protein. C, The protein levels were quantified using ImageJ. D, VEGF protein levels were analyzed by ELISA. E, The mtDNA copy number was determined using real‐time PCR. Fold differences are shown compared with the control, for which the value was defined as 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

    Article Snippet: Blots were then incubated for 1 hour at room temperature (25°C) with rabbit monoclonal SIRT1 antibody (1:400; Santa Cruz Biotechnology, Inc), rabbit monoclonal HIF‐1a antibody (1:1000; Epitomics), or mouse monoclonal β‐actin antibody (1:5000; Sigma‐Aldrich) as the primary antibody, and anti‐rabbit immunoglobulin IgG peroxidase‐labeled secondary antibody (1:10 000; GE Healthcare Life Science) or anti‐mouse IgG peroxidase‐labeled secondary antibody (1:10 000; GE Healthcare Life Science) as the secondary antibody.

    Techniques: Cell Culture, Real-time Polymerase Chain Reaction, Western Blot, Enzyme-linked Immunosorbent Assay

    Effects of CoCl 2 ‐induced hypoxic stress on mRNA expression and protein secretion. KGN cells were incubated for 24 h in medium containing with 10 μmol/L or 100 μmol/L CoCl 2 . A, SIRT1 mRNA levels were assessed by real‐time PCR and calculated after normalization to EF1α mRNA levels. B, The protein levels of SIRT1 were quantified by Western blotting, and β‐actin was used as the control. C, The protein levels were quantified using ImageJ. D, VEGF protein levels were analyzed by ELISA. E, The mtDNA copy number was determined using real‐time PCR. Fold differences are shown compared with the control, for which the value was defined as 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

    Journal: Reproductive Medicine and Biology

    Article Title: Resveratrol protects mitochondrial quantity by activating SIRT1/PGC‐1α expression during ovarian hypoxia, et al. Resveratrol protects mitochondrial quantity by activating SIRT1/PGC‐1α expression during ovarian hypoxia

    doi: 10.1002/rmb2.12323

    Figure Lengend Snippet: Effects of CoCl 2 ‐induced hypoxic stress on mRNA expression and protein secretion. KGN cells were incubated for 24 h in medium containing with 10 μmol/L or 100 μmol/L CoCl 2 . A, SIRT1 mRNA levels were assessed by real‐time PCR and calculated after normalization to EF1α mRNA levels. B, The protein levels of SIRT1 were quantified by Western blotting, and β‐actin was used as the control. C, The protein levels were quantified using ImageJ. D, VEGF protein levels were analyzed by ELISA. E, The mtDNA copy number was determined using real‐time PCR. Fold differences are shown compared with the control, for which the value was defined as 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

    Article Snippet: Blots were then incubated for 1 hour at room temperature (25°C) with rabbit monoclonal SIRT1 antibody (1:400; Santa Cruz Biotechnology, Inc), rabbit monoclonal HIF‐1a antibody (1:1000; Epitomics), or mouse monoclonal β‐actin antibody (1:5000; Sigma‐Aldrich) as the primary antibody, and anti‐rabbit immunoglobulin IgG peroxidase‐labeled secondary antibody (1:10 000; GE Healthcare Life Science) or anti‐mouse IgG peroxidase‐labeled secondary antibody (1:10 000; GE Healthcare Life Science) as the secondary antibody.

    Techniques: Expressing, Incubation, Real-time Polymerase Chain Reaction, Western Blot, Enzyme-linked Immunosorbent Assay

    Effect of resveratrol on HIF‐1α. KGN cells were incubated for 24 h in medium containing 100 μmol/L CoCl 2 with or without 50 μmol/L resveratrol (n = 3). A, The expression of HIF‐1α was quantified by Western blotting. The levels of HIF‐1α were normalized to levels of β‐actin (n = 3). B, The protein levels were quantified using ImageJ. C, VEGF protein levels were analyzed by ELISA. Fold differences are shown compared with the control, for which the value was defined 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

    Journal: Reproductive Medicine and Biology

    Article Title: Resveratrol protects mitochondrial quantity by activating SIRT1/PGC‐1α expression during ovarian hypoxia, et al. Resveratrol protects mitochondrial quantity by activating SIRT1/PGC‐1α expression during ovarian hypoxia

    doi: 10.1002/rmb2.12323

    Figure Lengend Snippet: Effect of resveratrol on HIF‐1α. KGN cells were incubated for 24 h in medium containing 100 μmol/L CoCl 2 with or without 50 μmol/L resveratrol (n = 3). A, The expression of HIF‐1α was quantified by Western blotting. The levels of HIF‐1α were normalized to levels of β‐actin (n = 3). B, The protein levels were quantified using ImageJ. C, VEGF protein levels were analyzed by ELISA. Fold differences are shown compared with the control, for which the value was defined 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

    Article Snippet: Blots were then incubated for 1 hour at room temperature (25°C) with rabbit monoclonal SIRT1 antibody (1:400; Santa Cruz Biotechnology, Inc), rabbit monoclonal HIF‐1a antibody (1:1000; Epitomics), or mouse monoclonal β‐actin antibody (1:5000; Sigma‐Aldrich) as the primary antibody, and anti‐rabbit immunoglobulin IgG peroxidase‐labeled secondary antibody (1:10 000; GE Healthcare Life Science) or anti‐mouse IgG peroxidase‐labeled secondary antibody (1:10 000; GE Healthcare Life Science) as the secondary antibody.

    Techniques: Incubation, Expressing, Western Blot, Enzyme-linked Immunosorbent Assay

    Temporal changes in synaptic plasticity-related signals in the mouse hippocampus following methotrexate (MTX) administration. (A) N-methyl-D-aspartic acid receptor 1 (NMDAR1). (B) Calcium/calmodulin-dependent protein kinase II (CaMKII). (C) Extracellular signal-regulated kinase 1/2 (ERK1/2). (D) cAMP responsive element-binding protein (CREB). (E) Glutamate receptor 1 (GluR1). The relative expression levels of phosphorylated (P) and total (T) forms were determined by densitometry and normalized to β-actin signals. Furthermore, to examine the activation levels of each signal, the relative levels of the P forms were normalized to their T-forms. Data are reported as mean ± SEM of three mice per time point. Values for protein expression levels from the hippocampus of vehicle-treated controls were arbitrarily defined as 1 (bar graphs). a P

    Journal: Neural Regeneration Research

    Article Title: Temporal profiles of synaptic plasticity-related signals in adult mouse hippocampus with methotrexate treatment ☆

    doi: 10.3969/j.issn.1673-5374.2012.21.008

    Figure Lengend Snippet: Temporal changes in synaptic plasticity-related signals in the mouse hippocampus following methotrexate (MTX) administration. (A) N-methyl-D-aspartic acid receptor 1 (NMDAR1). (B) Calcium/calmodulin-dependent protein kinase II (CaMKII). (C) Extracellular signal-regulated kinase 1/2 (ERK1/2). (D) cAMP responsive element-binding protein (CREB). (E) Glutamate receptor 1 (GluR1). The relative expression levels of phosphorylated (P) and total (T) forms were determined by densitometry and normalized to β-actin signals. Furthermore, to examine the activation levels of each signal, the relative levels of the P forms were normalized to their T-forms. Data are reported as mean ± SEM of three mice per time point. Values for protein expression levels from the hippocampus of vehicle-treated controls were arbitrarily defined as 1 (bar graphs). a P

    Article Snippet: Membranes were stripped and re-probed with a mouse monoclonal anti-β-actin (1:20 000; Sigma-Aldrich) for normalization.

    Techniques: Binding Assay, Expressing, Activation Assay, Mouse Assay

    Time-response changes of neurotrophic factors in the mouse hippocampus following administration of methotrexate (MTX). (A) Brain-derived neurotrophic factor (BDNF). (B) Glial cell line-derived neurotrophic factor (GDNF). The relative expression levels of proteins were determined by densitometry and normalized to β-actin signals. Data are reported as mean ± SEM. n = 3 mice per time point. Values for protein expression levels from the hippocampus of vehicle-treated controls (Cont) were arbitrarily defined as 1 (bar graphs). a P

    Journal: Neural Regeneration Research

    Article Title: Temporal profiles of synaptic plasticity-related signals in adult mouse hippocampus with methotrexate treatment ☆

    doi: 10.3969/j.issn.1673-5374.2012.21.008

    Figure Lengend Snippet: Time-response changes of neurotrophic factors in the mouse hippocampus following administration of methotrexate (MTX). (A) Brain-derived neurotrophic factor (BDNF). (B) Glial cell line-derived neurotrophic factor (GDNF). The relative expression levels of proteins were determined by densitometry and normalized to β-actin signals. Data are reported as mean ± SEM. n = 3 mice per time point. Values for protein expression levels from the hippocampus of vehicle-treated controls (Cont) were arbitrarily defined as 1 (bar graphs). a P

    Article Snippet: Membranes were stripped and re-probed with a mouse monoclonal anti-β-actin (1:20 000; Sigma-Aldrich) for normalization.

    Techniques: Derivative Assay, Expressing, Mouse Assay