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  • 99
    Thermo Fisher agarose gel
    Agarose Gel, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 13419 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore silica gel coated tlc plate
    Silica Gel Coated Tlc Plate, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher 500 ion chromatography system
    500 Ion Chromatography System, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher semi preparative scale carbopac pa1 column
    Semi Preparative Scale Carbopac Pa1 Column, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Avanti Polar extrusion
    Extrusion, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 91/100, based on 88 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare membrane filter
    Membrane Filter, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 745 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher 3730 genetic analyzer
    3730 Genetic Analyzer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1016 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher streptavidin magnetic beads
    STAT4 regulates p66shc expression A. In silico promoter analysis of the human p66shc promoter highlighting several putative STAT4 binding sites (grey shaded regions). SP1 binding sites identified in the analysis and known to be present in the p66shc promoter are shown in bold. The transcription start site (ATG) is also shown (underlined, italic). B. Top , schematic representation of the p66shc region taken into consideration for the ChIP experiments. Black arrows indicate the position of the primers used, dark squares the position of the STAT4 binding sites. The p66shc TSS is located in exon 2. Bottom , Nuclear extracts of EBV-B cells were subjected to ChIP assay with an antibody specific for STAT4. Precipitated DNA was amplified by qRT-PCR using primers described above. Unspecific IgG was used as control. Data are presented as percentage of input DNA (mean±SD; n=6). C. Scheme of the in vitro binding experiments. EBV-B nuclear extracts were used to pull down STAT4 bound to the biotinylated p66shc promoter, and bound STAT4 was detected by immunoblot. Lanes 1, 3 and 4 correspond to the beads bound to the promoter region containing one, three or all four STAT4 binding sites, respectively. <t>Streptavidin</t> beads incubated with nuclear extract were used as negative control (lane 0). Pull-down experiment using mutants of the putative STAT4 binding sites (M) showed no STAT4 immunoreactive band compared to the control (WT). (n=3). D-F. p66shc promoter activation assays in EBV-B cells. (D) Cells were co-transfected with reporter plasmids carrying p66shc promoter sequences containing none (pGL4p66Shc-460/+71), one (pGL4p66Shc-800/+71), or all (pGL4p66Shc-1300/+71) STAT4 binding sites, or empty vector (Ctr). A co-transfected Renilla plasmid was used as normalization control. (E) EBV-B cells were co-transfected with the pGL4p66Shc-1300/+71 luciferase reporter, the Renilla transfection control and a plasmid encoding STAT4. (F) EBV-B cells were co-transfected with plasmids containing the mutated STAT4-binding sequences or the corresponding WT sequences, and the Renilla transfection control. *** P ≤0.001; ** P ≤0.01, and * P ≤0.05 (n=3)
    Streptavidin Magnetic Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 3325 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher membranes
    STAT4 regulates p66shc expression A. In silico promoter analysis of the human p66shc promoter highlighting several putative STAT4 binding sites (grey shaded regions). SP1 binding sites identified in the analysis and known to be present in the p66shc promoter are shown in bold. The transcription start site (ATG) is also shown (underlined, italic). B. Top , schematic representation of the p66shc region taken into consideration for the ChIP experiments. Black arrows indicate the position of the primers used, dark squares the position of the STAT4 binding sites. The p66shc TSS is located in exon 2. Bottom , Nuclear extracts of EBV-B cells were subjected to ChIP assay with an antibody specific for STAT4. Precipitated DNA was amplified by qRT-PCR using primers described above. Unspecific IgG was used as control. Data are presented as percentage of input DNA (mean±SD; n=6). C. Scheme of the in vitro binding experiments. EBV-B nuclear extracts were used to pull down STAT4 bound to the biotinylated p66shc promoter, and bound STAT4 was detected by immunoblot. Lanes 1, 3 and 4 correspond to the beads bound to the promoter region containing one, three or all four STAT4 binding sites, respectively. <t>Streptavidin</t> beads incubated with nuclear extract were used as negative control (lane 0). Pull-down experiment using mutants of the putative STAT4 binding sites (M) showed no STAT4 immunoreactive band compared to the control (WT). (n=3). D-F. p66shc promoter activation assays in EBV-B cells. (D) Cells were co-transfected with reporter plasmids carrying p66shc promoter sequences containing none (pGL4p66Shc-460/+71), one (pGL4p66Shc-800/+71), or all (pGL4p66Shc-1300/+71) STAT4 binding sites, or empty vector (Ctr). A co-transfected Renilla plasmid was used as normalization control. (E) EBV-B cells were co-transfected with the pGL4p66Shc-1300/+71 luciferase reporter, the Renilla transfection control and a plasmid encoding STAT4. (F) EBV-B cells were co-transfected with plasmids containing the mutated STAT4-binding sequences or the corresponding WT sequences, and the Renilla transfection control. *** P ≤0.001; ** P ≤0.01, and * P ≤0.05 (n=3)
    Membranes, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 7835 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher streptavidin pe
    STAT4 regulates p66shc expression A. In silico promoter analysis of the human p66shc promoter highlighting several putative STAT4 binding sites (grey shaded regions). SP1 binding sites identified in the analysis and known to be present in the p66shc promoter are shown in bold. The transcription start site (ATG) is also shown (underlined, italic). B. Top , schematic representation of the p66shc region taken into consideration for the ChIP experiments. Black arrows indicate the position of the primers used, dark squares the position of the STAT4 binding sites. The p66shc TSS is located in exon 2. Bottom , Nuclear extracts of EBV-B cells were subjected to ChIP assay with an antibody specific for STAT4. Precipitated DNA was amplified by qRT-PCR using primers described above. Unspecific IgG was used as control. Data are presented as percentage of input DNA (mean±SD; n=6). C. Scheme of the in vitro binding experiments. EBV-B nuclear extracts were used to pull down STAT4 bound to the biotinylated p66shc promoter, and bound STAT4 was detected by immunoblot. Lanes 1, 3 and 4 correspond to the beads bound to the promoter region containing one, three or all four STAT4 binding sites, respectively. <t>Streptavidin</t> beads incubated with nuclear extract were used as negative control (lane 0). Pull-down experiment using mutants of the putative STAT4 binding sites (M) showed no STAT4 immunoreactive band compared to the control (WT). (n=3). D-F. p66shc promoter activation assays in EBV-B cells. (D) Cells were co-transfected with reporter plasmids carrying p66shc promoter sequences containing none (pGL4p66Shc-460/+71), one (pGL4p66Shc-800/+71), or all (pGL4p66Shc-1300/+71) STAT4 binding sites, or empty vector (Ctr). A co-transfected Renilla plasmid was used as normalization control. (E) EBV-B cells were co-transfected with the pGL4p66Shc-1300/+71 luciferase reporter, the Renilla transfection control and a plasmid encoding STAT4. (F) EBV-B cells were co-transfected with plasmids containing the mutated STAT4-binding sequences or the corresponding WT sequences, and the Renilla transfection control. *** P ≤0.001; ** P ≤0.01, and * P ≤0.05 (n=3)
    Streptavidin Pe, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2491 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Carl Zeiss zeiss axiovert
    STAT4 regulates p66shc expression A. In silico promoter analysis of the human p66shc promoter highlighting several putative STAT4 binding sites (grey shaded regions). SP1 binding sites identified in the analysis and known to be present in the p66shc promoter are shown in bold. The transcription start site (ATG) is also shown (underlined, italic). B. Top , schematic representation of the p66shc region taken into consideration for the ChIP experiments. Black arrows indicate the position of the primers used, dark squares the position of the STAT4 binding sites. The p66shc TSS is located in exon 2. Bottom , Nuclear extracts of EBV-B cells were subjected to ChIP assay with an antibody specific for STAT4. Precipitated DNA was amplified by qRT-PCR using primers described above. Unspecific IgG was used as control. Data are presented as percentage of input DNA (mean±SD; n=6). C. Scheme of the in vitro binding experiments. EBV-B nuclear extracts were used to pull down STAT4 bound to the biotinylated p66shc promoter, and bound STAT4 was detected by immunoblot. Lanes 1, 3 and 4 correspond to the beads bound to the promoter region containing one, three or all four STAT4 binding sites, respectively. <t>Streptavidin</t> beads incubated with nuclear extract were used as negative control (lane 0). Pull-down experiment using mutants of the putative STAT4 binding sites (M) showed no STAT4 immunoreactive band compared to the control (WT). (n=3). D-F. p66shc promoter activation assays in EBV-B cells. (D) Cells were co-transfected with reporter plasmids carrying p66shc promoter sequences containing none (pGL4p66Shc-460/+71), one (pGL4p66Shc-800/+71), or all (pGL4p66Shc-1300/+71) STAT4 binding sites, or empty vector (Ctr). A co-transfected Renilla plasmid was used as normalization control. (E) EBV-B cells were co-transfected with the pGL4p66Shc-1300/+71 luciferase reporter, the Renilla transfection control and a plasmid encoding STAT4. (F) EBV-B cells were co-transfected with plasmids containing the mutated STAT4-binding sequences or the corresponding WT sequences, and the Renilla transfection control. *** P ≤0.001; ** P ≤0.01, and * P ≤0.05 (n=3)
    Zeiss Axiovert, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 92/100, based on 13776 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher xcell ii blot modules
    STAT4 regulates p66shc expression A. In silico promoter analysis of the human p66shc promoter highlighting several putative STAT4 binding sites (grey shaded regions). SP1 binding sites identified in the analysis and known to be present in the p66shc promoter are shown in bold. The transcription start site (ATG) is also shown (underlined, italic). B. Top , schematic representation of the p66shc region taken into consideration for the ChIP experiments. Black arrows indicate the position of the primers used, dark squares the position of the STAT4 binding sites. The p66shc TSS is located in exon 2. Bottom , Nuclear extracts of EBV-B cells were subjected to ChIP assay with an antibody specific for STAT4. Precipitated DNA was amplified by qRT-PCR using primers described above. Unspecific IgG was used as control. Data are presented as percentage of input DNA (mean±SD; n=6). C. Scheme of the in vitro binding experiments. EBV-B nuclear extracts were used to pull down STAT4 bound to the biotinylated p66shc promoter, and bound STAT4 was detected by immunoblot. Lanes 1, 3 and 4 correspond to the beads bound to the promoter region containing one, three or all four STAT4 binding sites, respectively. <t>Streptavidin</t> beads incubated with nuclear extract were used as negative control (lane 0). Pull-down experiment using mutants of the putative STAT4 binding sites (M) showed no STAT4 immunoreactive band compared to the control (WT). (n=3). D-F. p66shc promoter activation assays in EBV-B cells. (D) Cells were co-transfected with reporter plasmids carrying p66shc promoter sequences containing none (pGL4p66Shc-460/+71), one (pGL4p66Shc-800/+71), or all (pGL4p66Shc-1300/+71) STAT4 binding sites, or empty vector (Ctr). A co-transfected Renilla plasmid was used as normalization control. (E) EBV-B cells were co-transfected with the pGL4p66Shc-1300/+71 luciferase reporter, the Renilla transfection control and a plasmid encoding STAT4. (F) EBV-B cells were co-transfected with plasmids containing the mutated STAT4-binding sequences or the corresponding WT sequences, and the Renilla transfection control. *** P ≤0.001; ** P ≤0.01, and * P ≤0.05 (n=3)
    Xcell Ii Blot Modules, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 496 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher 3730xl dna analyzer
    STAT4 regulates p66shc expression A. In silico promoter analysis of the human p66shc promoter highlighting several putative STAT4 binding sites (grey shaded regions). SP1 binding sites identified in the analysis and known to be present in the p66shc promoter are shown in bold. The transcription start site (ATG) is also shown (underlined, italic). B. Top , schematic representation of the p66shc region taken into consideration for the ChIP experiments. Black arrows indicate the position of the primers used, dark squares the position of the STAT4 binding sites. The p66shc TSS is located in exon 2. Bottom , Nuclear extracts of EBV-B cells were subjected to ChIP assay with an antibody specific for STAT4. Precipitated DNA was amplified by qRT-PCR using primers described above. Unspecific IgG was used as control. Data are presented as percentage of input DNA (mean±SD; n=6). C. Scheme of the in vitro binding experiments. EBV-B nuclear extracts were used to pull down STAT4 bound to the biotinylated p66shc promoter, and bound STAT4 was detected by immunoblot. Lanes 1, 3 and 4 correspond to the beads bound to the promoter region containing one, three or all four STAT4 binding sites, respectively. <t>Streptavidin</t> beads incubated with nuclear extract were used as negative control (lane 0). Pull-down experiment using mutants of the putative STAT4 binding sites (M) showed no STAT4 immunoreactive band compared to the control (WT). (n=3). D-F. p66shc promoter activation assays in EBV-B cells. (D) Cells were co-transfected with reporter plasmids carrying p66shc promoter sequences containing none (pGL4p66Shc-460/+71), one (pGL4p66Shc-800/+71), or all (pGL4p66Shc-1300/+71) STAT4 binding sites, or empty vector (Ctr). A co-transfected Renilla plasmid was used as normalization control. (E) EBV-B cells were co-transfected with the pGL4p66Shc-1300/+71 luciferase reporter, the Renilla transfection control and a plasmid encoding STAT4. (F) EBV-B cells were co-transfected with plasmids containing the mutated STAT4-binding sequences or the corresponding WT sequences, and the Renilla transfection control. *** P ≤0.001; ** P ≤0.01, and * P ≤0.05 (n=3)
    3730xl Dna Analyzer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 46653 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher kb plus dna ladder
    STAT4 regulates p66shc expression A. In silico promoter analysis of the human p66shc promoter highlighting several putative STAT4 binding sites (grey shaded regions). SP1 binding sites identified in the analysis and known to be present in the p66shc promoter are shown in bold. The transcription start site (ATG) is also shown (underlined, italic). B. Top , schematic representation of the p66shc region taken into consideration for the ChIP experiments. Black arrows indicate the position of the primers used, dark squares the position of the STAT4 binding sites. The p66shc TSS is located in exon 2. Bottom , Nuclear extracts of EBV-B cells were subjected to ChIP assay with an antibody specific for STAT4. Precipitated DNA was amplified by qRT-PCR using primers described above. Unspecific IgG was used as control. Data are presented as percentage of input DNA (mean±SD; n=6). C. Scheme of the in vitro binding experiments. EBV-B nuclear extracts were used to pull down STAT4 bound to the biotinylated p66shc promoter, and bound STAT4 was detected by immunoblot. Lanes 1, 3 and 4 correspond to the beads bound to the promoter region containing one, three or all four STAT4 binding sites, respectively. <t>Streptavidin</t> beads incubated with nuclear extract were used as negative control (lane 0). Pull-down experiment using mutants of the putative STAT4 binding sites (M) showed no STAT4 immunoreactive band compared to the control (WT). (n=3). D-F. p66shc promoter activation assays in EBV-B cells. (D) Cells were co-transfected with reporter plasmids carrying p66shc promoter sequences containing none (pGL4p66Shc-460/+71), one (pGL4p66Shc-800/+71), or all (pGL4p66Shc-1300/+71) STAT4 binding sites, or empty vector (Ctr). A co-transfected Renilla plasmid was used as normalization control. (E) EBV-B cells were co-transfected with the pGL4p66Shc-1300/+71 luciferase reporter, the Renilla transfection control and a plasmid encoding STAT4. (F) EBV-B cells were co-transfected with plasmids containing the mutated STAT4-binding sequences or the corresponding WT sequences, and the Renilla transfection control. *** P ≤0.001; ** P ≤0.01, and * P ≤0.05 (n=3)
    Kb Plus Dna Ladder, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2068 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher membrane stain cellmask deep red
    lsq plants have normal tetrahedral arrangement of microspores in a tetrad. Some of the developing apertures in lsq6 tetrads are not aligned with any apertures in sister microspores. (A-D) Tetrads from the wild-type (A, C) and lsq6 (B, D) plants exhibit similar tetrahedral morphology. (A, B) Single optical sections. Membrane structures are stained with <t>CellMask</t> Deep Red (magenta) and callose walls are stained with calcofluor white (blue). Scale bars = 5 μm. (C, D) 3-D reconstructions from confocal z-stacks of the tetrads shown in (A) and (B). Each of the four microspores in a tetrad is labeled with a number. (E-F’) 3-D reconstruction and surface rendering from confocal z-stacks of a wild-type ( INP1pr : INP1-YFP ) (E) and a lsq6 (F, F’) tetrad of microspores allows visualizing apertures developing on microspore surfaces (magenta). Microspore surfaces were transiently labeled with DAPI (green) and rendered with IMARIS (E) or Nikon Elements (F, F’). Developing apertures (indicated by arrowheads) are visible due to underlying INP1-YFP fluorescence (E, magenta) or with the help of the membrane stain CellMask Deep Red (F, F’, magenta). (F) A view of a lsq6 tetrad that shows alignment between apertures on sister microspores (arrowheads). (F’) A different view of the same tetrad that shows an aperture (arrow) not aligned with any apertures in a sister microspore. See also S1 and S2 Movies.
    Membrane Stain Cellmask Deep Red, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher streptavidin coated magnetic beads
    Ca Bdf1 BDs are resistant to BETi. ( a ) HTRF assay. A biotinylated tetra-acetylated histone H4 peptide is bound to <t>streptavidin</t> beads coupled to the donor fluorophore. A GST-tagged BD is bound by an anti-GST antibody coupled to the acceptor fluorophor. Peptide binding by the BD results in FRET. The addition of a BETi reduces FRET. ( b ) HTRF assays performed on BDs from Ca Bdf1 and human Brd4 in the presence of the indicated BETi. Inhibition curves are shown as closed (BD1) and open (BD2) circles in green (Brd4) and magenta (Bdf1). IC 50 values are listed below each graph. Data represent the mean and s.d. values from three independent experiments. ( c ) Representative ITC experiments measuring the binding of JQ1 to Ca BDF1 BDs (magenta) and to human Brd4 BD1 (green). The values indicated for K d and N represent the mean and s.d. from three independent experiments. See also Supplementary Table 1 . ( d ) BET inhibitors do not affect C. albicans growth, even when Bdf1 BD1 or BD2 is deleted. Inhibitors were tested at 10 μM concentration. Experiments were performed in the presence of doxycyline to repress expression from the pTetO -BDF1 allele. Data represent the mean and s.d. values from three independent experiments.
    Streptavidin Coated Magnetic Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 5203 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher xcell surelock mini cell and xcell ii blot module
    Ca Bdf1 BDs are resistant to BETi. ( a ) HTRF assay. A biotinylated tetra-acetylated histone H4 peptide is bound to <t>streptavidin</t> beads coupled to the donor fluorophore. A GST-tagged BD is bound by an anti-GST antibody coupled to the acceptor fluorophor. Peptide binding by the BD results in FRET. The addition of a BETi reduces FRET. ( b ) HTRF assays performed on BDs from Ca Bdf1 and human Brd4 in the presence of the indicated BETi. Inhibition curves are shown as closed (BD1) and open (BD2) circles in green (Brd4) and magenta (Bdf1). IC 50 values are listed below each graph. Data represent the mean and s.d. values from three independent experiments. ( c ) Representative ITC experiments measuring the binding of JQ1 to Ca BDF1 BDs (magenta) and to human Brd4 BD1 (green). The values indicated for K d and N represent the mean and s.d. from three independent experiments. See also Supplementary Table 1 . ( d ) BET inhibitors do not affect C. albicans growth, even when Bdf1 BD1 or BD2 is deleted. Inhibitors were tested at 10 μM concentration. Experiments were performed in the presence of doxycyline to repress expression from the pTetO -BDF1 allele. Data represent the mean and s.d. values from three independent experiments.
    Xcell Surelock Mini Cell And Xcell Ii Blot Module, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 60 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher dynabeads mrna purification kit
    Ca Bdf1 BDs are resistant to BETi. ( a ) HTRF assay. A biotinylated tetra-acetylated histone H4 peptide is bound to <t>streptavidin</t> beads coupled to the donor fluorophore. A GST-tagged BD is bound by an anti-GST antibody coupled to the acceptor fluorophor. Peptide binding by the BD results in FRET. The addition of a BETi reduces FRET. ( b ) HTRF assays performed on BDs from Ca Bdf1 and human Brd4 in the presence of the indicated BETi. Inhibition curves are shown as closed (BD1) and open (BD2) circles in green (Brd4) and magenta (Bdf1). IC 50 values are listed below each graph. Data represent the mean and s.d. values from three independent experiments. ( c ) Representative ITC experiments measuring the binding of JQ1 to Ca BDF1 BDs (magenta) and to human Brd4 BD1 (green). The values indicated for K d and N represent the mean and s.d. from three independent experiments. See also Supplementary Table 1 . ( d ) BET inhibitors do not affect C. albicans growth, even when Bdf1 BD1 or BD2 is deleted. Inhibitors were tested at 10 μM concentration. Experiments were performed in the presence of doxycyline to repress expression from the pTetO -BDF1 allele. Data represent the mean and s.d. values from three independent experiments.
    Dynabeads Mrna Purification Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 4204 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher cover glasses
    Ca Bdf1 BDs are resistant to BETi. ( a ) HTRF assay. A biotinylated tetra-acetylated histone H4 peptide is bound to <t>streptavidin</t> beads coupled to the donor fluorophore. A GST-tagged BD is bound by an anti-GST antibody coupled to the acceptor fluorophor. Peptide binding by the BD results in FRET. The addition of a BETi reduces FRET. ( b ) HTRF assays performed on BDs from Ca Bdf1 and human Brd4 in the presence of the indicated BETi. Inhibition curves are shown as closed (BD1) and open (BD2) circles in green (Brd4) and magenta (Bdf1). IC 50 values are listed below each graph. Data represent the mean and s.d. values from three independent experiments. ( c ) Representative ITC experiments measuring the binding of JQ1 to Ca BDF1 BDs (magenta) and to human Brd4 BD1 (green). The values indicated for K d and N represent the mean and s.d. from three independent experiments. See also Supplementary Table 1 . ( d ) BET inhibitors do not affect C. albicans growth, even when Bdf1 BD1 or BD2 is deleted. Inhibitors were tested at 10 μM concentration. Experiments were performed in the presence of doxycyline to repress expression from the pTetO -BDF1 allele. Data represent the mean and s.d. values from three independent experiments.
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    Ca Bdf1 BDs are resistant to BETi. ( a ) HTRF assay. A biotinylated tetra-acetylated histone H4 peptide is bound to <t>streptavidin</t> beads coupled to the donor fluorophore. A GST-tagged BD is bound by an anti-GST antibody coupled to the acceptor fluorophor. Peptide binding by the BD results in FRET. The addition of a BETi reduces FRET. ( b ) HTRF assays performed on BDs from Ca Bdf1 and human Brd4 in the presence of the indicated BETi. Inhibition curves are shown as closed (BD1) and open (BD2) circles in green (Brd4) and magenta (Bdf1). IC 50 values are listed below each graph. Data represent the mean and s.d. values from three independent experiments. ( c ) Representative ITC experiments measuring the binding of JQ1 to Ca BDF1 BDs (magenta) and to human Brd4 BD1 (green). The values indicated for K d and N represent the mean and s.d. from three independent experiments. See also Supplementary Table 1 . ( d ) BET inhibitors do not affect C. albicans growth, even when Bdf1 BD1 or BD2 is deleted. Inhibitors were tested at 10 μM concentration. Experiments were performed in the presence of doxycyline to repress expression from the pTetO -BDF1 allele. Data represent the mean and s.d. values from three independent experiments.
    Abi 3730 Dna Analyzer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 5973 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    STAT4 regulates p66shc expression A. In silico promoter analysis of the human p66shc promoter highlighting several putative STAT4 binding sites (grey shaded regions). SP1 binding sites identified in the analysis and known to be present in the p66shc promoter are shown in bold. The transcription start site (ATG) is also shown (underlined, italic). B. Top , schematic representation of the p66shc region taken into consideration for the ChIP experiments. Black arrows indicate the position of the primers used, dark squares the position of the STAT4 binding sites. The p66shc TSS is located in exon 2. Bottom , Nuclear extracts of EBV-B cells were subjected to ChIP assay with an antibody specific for STAT4. Precipitated DNA was amplified by qRT-PCR using primers described above. Unspecific IgG was used as control. Data are presented as percentage of input DNA (mean±SD; n=6). C. Scheme of the in vitro binding experiments. EBV-B nuclear extracts were used to pull down STAT4 bound to the biotinylated p66shc promoter, and bound STAT4 was detected by immunoblot. Lanes 1, 3 and 4 correspond to the beads bound to the promoter region containing one, three or all four STAT4 binding sites, respectively. Streptavidin beads incubated with nuclear extract were used as negative control (lane 0). Pull-down experiment using mutants of the putative STAT4 binding sites (M) showed no STAT4 immunoreactive band compared to the control (WT). (n=3). D-F. p66shc promoter activation assays in EBV-B cells. (D) Cells were co-transfected with reporter plasmids carrying p66shc promoter sequences containing none (pGL4p66Shc-460/+71), one (pGL4p66Shc-800/+71), or all (pGL4p66Shc-1300/+71) STAT4 binding sites, or empty vector (Ctr). A co-transfected Renilla plasmid was used as normalization control. (E) EBV-B cells were co-transfected with the pGL4p66Shc-1300/+71 luciferase reporter, the Renilla transfection control and a plasmid encoding STAT4. (F) EBV-B cells were co-transfected with plasmids containing the mutated STAT4-binding sequences or the corresponding WT sequences, and the Renilla transfection control. *** P ≤0.001; ** P ≤0.01, and * P ≤0.05 (n=3)

    Journal: Oncotarget

    Article Title: Expression of the p66Shc protein adaptor is regulated by the activator of transcription STAT4 in normal and chronic lymphocytic leukemia B cells

    doi: 10.18632/oncotarget.10977

    Figure Lengend Snippet: STAT4 regulates p66shc expression A. In silico promoter analysis of the human p66shc promoter highlighting several putative STAT4 binding sites (grey shaded regions). SP1 binding sites identified in the analysis and known to be present in the p66shc promoter are shown in bold. The transcription start site (ATG) is also shown (underlined, italic). B. Top , schematic representation of the p66shc region taken into consideration for the ChIP experiments. Black arrows indicate the position of the primers used, dark squares the position of the STAT4 binding sites. The p66shc TSS is located in exon 2. Bottom , Nuclear extracts of EBV-B cells were subjected to ChIP assay with an antibody specific for STAT4. Precipitated DNA was amplified by qRT-PCR using primers described above. Unspecific IgG was used as control. Data are presented as percentage of input DNA (mean±SD; n=6). C. Scheme of the in vitro binding experiments. EBV-B nuclear extracts were used to pull down STAT4 bound to the biotinylated p66shc promoter, and bound STAT4 was detected by immunoblot. Lanes 1, 3 and 4 correspond to the beads bound to the promoter region containing one, three or all four STAT4 binding sites, respectively. Streptavidin beads incubated with nuclear extract were used as negative control (lane 0). Pull-down experiment using mutants of the putative STAT4 binding sites (M) showed no STAT4 immunoreactive band compared to the control (WT). (n=3). D-F. p66shc promoter activation assays in EBV-B cells. (D) Cells were co-transfected with reporter plasmids carrying p66shc promoter sequences containing none (pGL4p66Shc-460/+71), one (pGL4p66Shc-800/+71), or all (pGL4p66Shc-1300/+71) STAT4 binding sites, or empty vector (Ctr). A co-transfected Renilla plasmid was used as normalization control. (E) EBV-B cells were co-transfected with the pGL4p66Shc-1300/+71 luciferase reporter, the Renilla transfection control and a plasmid encoding STAT4. (F) EBV-B cells were co-transfected with plasmids containing the mutated STAT4-binding sequences or the corresponding WT sequences, and the Renilla transfection control. *** P ≤0.001; ** P ≤0.01, and * P ≤0.05 (n=3)

    Article Snippet: The PCR reactions were performed using the following amplification conditions: 95°C for 3 minutes followed by 40 cycles at 95°C for 30 sec, 60°C for 30 sec, 72°C for 45 sec, and a final elongation at 72°C for 4 min. PCR products were purified with the High Pure PCR Product Purification Kit (Roche Applied Science, Indianapolis, IN) and incubated for 2 h at room temperature with Pierce™ Streptavidin Magnetic Beads.

    Techniques: Expressing, In Silico, Binding Assay, Chromatin Immunoprecipitation, Amplification, Quantitative RT-PCR, In Vitro, Incubation, Negative Control, Activation Assay, Transfection, Plasmid Preparation, Luciferase

    lsq plants have normal tetrahedral arrangement of microspores in a tetrad. Some of the developing apertures in lsq6 tetrads are not aligned with any apertures in sister microspores. (A-D) Tetrads from the wild-type (A, C) and lsq6 (B, D) plants exhibit similar tetrahedral morphology. (A, B) Single optical sections. Membrane structures are stained with CellMask Deep Red (magenta) and callose walls are stained with calcofluor white (blue). Scale bars = 5 μm. (C, D) 3-D reconstructions from confocal z-stacks of the tetrads shown in (A) and (B). Each of the four microspores in a tetrad is labeled with a number. (E-F’) 3-D reconstruction and surface rendering from confocal z-stacks of a wild-type ( INP1pr : INP1-YFP ) (E) and a lsq6 (F, F’) tetrad of microspores allows visualizing apertures developing on microspore surfaces (magenta). Microspore surfaces were transiently labeled with DAPI (green) and rendered with IMARIS (E) or Nikon Elements (F, F’). Developing apertures (indicated by arrowheads) are visible due to underlying INP1-YFP fluorescence (E, magenta) or with the help of the membrane stain CellMask Deep Red (F, F’, magenta). (F) A view of a lsq6 tetrad that shows alignment between apertures on sister microspores (arrowheads). (F’) A different view of the same tetrad that shows an aperture (arrow) not aligned with any apertures in a sister microspore. See also S1 and S2 Movies.

    Journal: PLoS Genetics

    Article Title: A Ploidy-Sensitive Mechanism Regulates Aperture Formation on the Arabidopsis Pollen Surface and Guides Localization of the Aperture Factor INP1

    doi: 10.1371/journal.pgen.1006060

    Figure Lengend Snippet: lsq plants have normal tetrahedral arrangement of microspores in a tetrad. Some of the developing apertures in lsq6 tetrads are not aligned with any apertures in sister microspores. (A-D) Tetrads from the wild-type (A, C) and lsq6 (B, D) plants exhibit similar tetrahedral morphology. (A, B) Single optical sections. Membrane structures are stained with CellMask Deep Red (magenta) and callose walls are stained with calcofluor white (blue). Scale bars = 5 μm. (C, D) 3-D reconstructions from confocal z-stacks of the tetrads shown in (A) and (B). Each of the four microspores in a tetrad is labeled with a number. (E-F’) 3-D reconstruction and surface rendering from confocal z-stacks of a wild-type ( INP1pr : INP1-YFP ) (E) and a lsq6 (F, F’) tetrad of microspores allows visualizing apertures developing on microspore surfaces (magenta). Microspore surfaces were transiently labeled with DAPI (green) and rendered with IMARIS (E) or Nikon Elements (F, F’). Developing apertures (indicated by arrowheads) are visible due to underlying INP1-YFP fluorescence (E, magenta) or with the help of the membrane stain CellMask Deep Red (F, F’, magenta). (F) A view of a lsq6 tetrad that shows alignment between apertures on sister microspores (arrowheads). (F’) A different view of the same tetrad that shows an aperture (arrow) not aligned with any apertures in a sister microspore. See also S1 and S2 Movies.

    Article Snippet: For imaging tetrads and dyads, anthers were dissected out of stage-9 flower buds [ ] and placed into the Vectashield anti-fade solution (Vector Labs, Burlingame, CA) supplemented with membrane stain CellMask Deep Red (Molecular Probes, Eugene, OR) (5 μg/ml) and calcofluor white (0.02%).

    Techniques: Staining, Labeling, Fluorescence

    Positions of the last points of contact in tetrads of wild type and lsq6 and in dyads of 2n and 4n osd1 plants. (A, C, E, G) Single optical sections through tetrads and dyads. Gaps in callose walls and last points of contact are labeled with arrows. Membrane structures are stained with CellMask Deep Red (magenta) and callose walls are stained with calcofluor white (blue). Scale bars = 5 μm. (B, D, F, H) 3-D reconstructions from confocal z-stacks of the tetrads and dyads shown in (A, C, E, G). Positions of cytoplasmic bridges at the last points of contact are indicated by arrowheads.

    Journal: PLoS Genetics

    Article Title: A Ploidy-Sensitive Mechanism Regulates Aperture Formation on the Arabidopsis Pollen Surface and Guides Localization of the Aperture Factor INP1

    doi: 10.1371/journal.pgen.1006060

    Figure Lengend Snippet: Positions of the last points of contact in tetrads of wild type and lsq6 and in dyads of 2n and 4n osd1 plants. (A, C, E, G) Single optical sections through tetrads and dyads. Gaps in callose walls and last points of contact are labeled with arrows. Membrane structures are stained with CellMask Deep Red (magenta) and callose walls are stained with calcofluor white (blue). Scale bars = 5 μm. (B, D, F, H) 3-D reconstructions from confocal z-stacks of the tetrads and dyads shown in (A, C, E, G). Positions of cytoplasmic bridges at the last points of contact are indicated by arrowheads.

    Article Snippet: For imaging tetrads and dyads, anthers were dissected out of stage-9 flower buds [ ] and placed into the Vectashield anti-fade solution (Vector Labs, Burlingame, CA) supplemented with membrane stain CellMask Deep Red (Molecular Probes, Eugene, OR) (5 μg/ml) and calcofluor white (0.02%).

    Techniques: Labeling, Staining

    Ca Bdf1 BDs are resistant to BETi. ( a ) HTRF assay. A biotinylated tetra-acetylated histone H4 peptide is bound to streptavidin beads coupled to the donor fluorophore. A GST-tagged BD is bound by an anti-GST antibody coupled to the acceptor fluorophor. Peptide binding by the BD results in FRET. The addition of a BETi reduces FRET. ( b ) HTRF assays performed on BDs from Ca Bdf1 and human Brd4 in the presence of the indicated BETi. Inhibition curves are shown as closed (BD1) and open (BD2) circles in green (Brd4) and magenta (Bdf1). IC 50 values are listed below each graph. Data represent the mean and s.d. values from three independent experiments. ( c ) Representative ITC experiments measuring the binding of JQ1 to Ca BDF1 BDs (magenta) and to human Brd4 BD1 (green). The values indicated for K d and N represent the mean and s.d. from three independent experiments. See also Supplementary Table 1 . ( d ) BET inhibitors do not affect C. albicans growth, even when Bdf1 BD1 or BD2 is deleted. Inhibitors were tested at 10 μM concentration. Experiments were performed in the presence of doxycyline to repress expression from the pTetO -BDF1 allele. Data represent the mean and s.d. values from three independent experiments.

    Journal: Nature Communications

    Article Title: Selective BET bromodomain inhibition as an antifungal therapeutic strategy

    doi: 10.1038/ncomms15482

    Figure Lengend Snippet: Ca Bdf1 BDs are resistant to BETi. ( a ) HTRF assay. A biotinylated tetra-acetylated histone H4 peptide is bound to streptavidin beads coupled to the donor fluorophore. A GST-tagged BD is bound by an anti-GST antibody coupled to the acceptor fluorophor. Peptide binding by the BD results in FRET. The addition of a BETi reduces FRET. ( b ) HTRF assays performed on BDs from Ca Bdf1 and human Brd4 in the presence of the indicated BETi. Inhibition curves are shown as closed (BD1) and open (BD2) circles in green (Brd4) and magenta (Bdf1). IC 50 values are listed below each graph. Data represent the mean and s.d. values from three independent experiments. ( c ) Representative ITC experiments measuring the binding of JQ1 to Ca BDF1 BDs (magenta) and to human Brd4 BD1 (green). The values indicated for K d and N represent the mean and s.d. from three independent experiments. See also Supplementary Table 1 . ( d ) BET inhibitors do not affect C. albicans growth, even when Bdf1 BD1 or BD2 is deleted. Inhibitors were tested at 10 μM concentration. Experiments were performed in the presence of doxycyline to repress expression from the pTetO -BDF1 allele. Data represent the mean and s.d. values from three independent experiments.

    Article Snippet: Pull-down and peptide array assays Biotinylated peptides corresponding to non-acetylated (H4ac0) and tetra-acetylated (H4K5acK8acK12acK16ac) histone H4 tails were synthesized by Covalab (Villeurbanne, France) and immobilized on Streptavidin-coated magnetic beads (Dynabeads MyOne Streptavidin C1; Thermo Fisher) according to the manufacturer's instructions.

    Techniques: HTRF Assay, Binding Assay, Inhibition, Concentration Assay, Expressing