anti-h4 Search Results


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  • 93
    Millipore anti h4
    Induction of apoptosis by BZ in hypoxia. ( A ) Total cell lysates in Laemmli buffer were subjected to immuno-blotting with the indicated antibodies. <t>Anti-H4</t> was used to verify equalization of protein loading. One representative experiment out of 3 is shown. ( B ) Percentages cells undergone “early” (annexin-V+/PI-) or “late” (annexin-V+/PI+) apoptosis, as determined by flow-cytometry. Values are means±S.E.M. of 3 independent experiments.
    Anti H4, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 108 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti h4/product/Millipore
    Average 93 stars, based on 108 article reviews
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    anti h4 - by Bioz Stars, 2020-05
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    92
    Active Motif anti h4
    Induction of apoptosis by BZ in hypoxia. ( A ) Total cell lysates in Laemmli buffer were subjected to immuno-blotting with the indicated antibodies. <t>Anti-H4</t> was used to verify equalization of protein loading. One representative experiment out of 3 is shown. ( B ) Percentages cells undergone “early” (annexin-V+/PI-) or “late” (annexin-V+/PI+) apoptosis, as determined by flow-cytometry. Values are means±S.E.M. of 3 independent experiments.
    Anti H4, supplied by Active Motif, used in various techniques. Bioz Stars score: 92/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti h4 - by Bioz Stars, 2020-05
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    91
    Upstate Biotechnology Inc anti h4
    Induction of apoptosis by BZ in hypoxia. ( A ) Total cell lysates in Laemmli buffer were subjected to immuno-blotting with the indicated antibodies. <t>Anti-H4</t> was used to verify equalization of protein loading. One representative experiment out of 3 is shown. ( B ) Percentages cells undergone “early” (annexin-V+/PI-) or “late” (annexin-V+/PI+) apoptosis, as determined by flow-cytometry. Values are means±S.E.M. of 3 independent experiments.
    Anti H4, supplied by Upstate Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 91 stars, based on 29 article reviews
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    anti h4 - by Bioz Stars, 2020-05
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    93
    Cell Signaling Technology Inc anti h4
    Induction of apoptosis by BZ in hypoxia. ( A ) Total cell lysates in Laemmli buffer were subjected to immuno-blotting with the indicated antibodies. <t>Anti-H4</t> was used to verify equalization of protein loading. One representative experiment out of 3 is shown. ( B ) Percentages cells undergone “early” (annexin-V+/PI-) or “late” (annexin-V+/PI+) apoptosis, as determined by flow-cytometry. Values are means±S.E.M. of 3 independent experiments.
    Anti H4, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 41 article reviews
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    91
    Santa Cruz Biotechnology anti h4
    Induction of apoptosis by BZ in hypoxia. ( A ) Total cell lysates in Laemmli buffer were subjected to immuno-blotting with the indicated antibodies. <t>Anti-H4</t> was used to verify equalization of protein loading. One representative experiment out of 3 is shown. ( B ) Percentages cells undergone “early” (annexin-V+/PI-) or “late” (annexin-V+/PI+) apoptosis, as determined by flow-cytometry. Values are means±S.E.M. of 3 independent experiments.
    Anti H4, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    GeneTex anti h4
    Induction of apoptosis by BZ in hypoxia. ( A ) Total cell lysates in Laemmli buffer were subjected to immuno-blotting with the indicated antibodies. <t>Anti-H4</t> was used to verify equalization of protein loading. One representative experiment out of 3 is shown. ( B ) Percentages cells undergone “early” (annexin-V+/PI-) or “late” (annexin-V+/PI+) apoptosis, as determined by flow-cytometry. Values are means±S.E.M. of 3 independent experiments.
    Anti H4, supplied by GeneTex, used in various techniques. Bioz Stars score: 90/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Diagenode anti h4
    Induction of apoptosis by BZ in hypoxia. ( A ) Total cell lysates in Laemmli buffer were subjected to immuno-blotting with the indicated antibodies. <t>Anti-H4</t> was used to verify equalization of protein loading. One representative experiment out of 3 is shown. ( B ) Percentages cells undergone “early” (annexin-V+/PI-) or “late” (annexin-V+/PI+) apoptosis, as determined by flow-cytometry. Values are means±S.E.M. of 3 independent experiments.
    Anti H4, supplied by Diagenode, used in various techniques. Bioz Stars score: 90/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Abcam anti h4
    Mutations in Yaf9-YEATS disrupt binding to H3K27ac in vitro and loading of H2A.Z in vivo . ( A ) TAP purification of NuA4 complex using Epl1-TAP tagged background. Yaf9 WT and point mutants (Y70A and W89A) associate with the NuA4 complex, but the C-terminal truncated form (ΔC; 1–186 aa) of Yaf9 does not. Purified NuA4 complex was ran on 10% Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose membrane and detected with indicated antibodies. ( B ) Peptide pull-down assay using indicated H3 peptides and GST-tagged Yaf9-YEATS. Recombinant WT Yaf9 binds to H3K27ac peptides, whereas the W89A mutant does not. None of the proteins show binding to unmodified H3 peptide. Empty GST is used as negative control. ( C ) Chromatin pull-down assay using human nucleosomes and GST-tagged Yaf9-YEATS. WT Yaf9 binds to nucleosomes harboring the H3K27ac mark, while the W89A mutant does not. Empty GST is used as negative control. ( D ) Phenotypic analysis of yeast strains with integrated alleles YAF9 (WT), yaf9-Y70A, yaf9-W89A, yaf9(1–186) and Δyaf9 . The strains expressing the YEATS domain point mutants showed similar growth defects as truncated yaf9(1–186) and Δyaf9 at 16°C, and in the presence of formamide or DNA-damaging agent MMS. ( E ) The point mutation W89A introduced in endogenous Yaf9 creates a strong defect in incorporation of histone variant H2A.Z (Htz1) at the PHO5 gene promoter in vivo . ChIP-qPCR was performed using anti-Htz1 and <t>anti-H4</t> antibodies and the indicated yeast strains. The precipitated DNA was quantified with primers spanning the PHO5 UAS2 region. Data are presented as ratio of IP for Htz1 normalized on total H4. The error bar represents range between two biological replicates. ( F and G ) Levels of H4 hyperacetylation and H3K27ac were measured by ChIP-qPCR in the same conditions as in (E).
    Anti H4, supplied by Abcam, used in various techniques. Bioz Stars score: 94/100, based on 281 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 281 article reviews
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    anti h4 - by Bioz Stars, 2020-05
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    86
    Active Motif anti h4 acetyl
    Mutations in Yaf9-YEATS disrupt binding to H3K27ac in vitro and loading of H2A.Z in vivo . ( A ) TAP purification of NuA4 complex using Epl1-TAP tagged background. Yaf9 WT and point mutants (Y70A and W89A) associate with the NuA4 complex, but the C-terminal truncated form (ΔC; 1–186 aa) of Yaf9 does not. Purified NuA4 complex was ran on 10% Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose membrane and detected with indicated antibodies. ( B ) Peptide pull-down assay using indicated H3 peptides and GST-tagged Yaf9-YEATS. Recombinant WT Yaf9 binds to H3K27ac peptides, whereas the W89A mutant does not. None of the proteins show binding to unmodified H3 peptide. Empty GST is used as negative control. ( C ) Chromatin pull-down assay using human nucleosomes and GST-tagged Yaf9-YEATS. WT Yaf9 binds to nucleosomes harboring the H3K27ac mark, while the W89A mutant does not. Empty GST is used as negative control. ( D ) Phenotypic analysis of yeast strains with integrated alleles YAF9 (WT), yaf9-Y70A, yaf9-W89A, yaf9(1–186) and Δyaf9 . The strains expressing the YEATS domain point mutants showed similar growth defects as truncated yaf9(1–186) and Δyaf9 at 16°C, and in the presence of formamide or DNA-damaging agent MMS. ( E ) The point mutation W89A introduced in endogenous Yaf9 creates a strong defect in incorporation of histone variant H2A.Z (Htz1) at the PHO5 gene promoter in vivo . ChIP-qPCR was performed using anti-Htz1 and <t>anti-H4</t> antibodies and the indicated yeast strains. The precipitated DNA was quantified with primers spanning the PHO5 UAS2 region. Data are presented as ratio of IP for Htz1 normalized on total H4. The error bar represents range between two biological replicates. ( F and G ) Levels of H4 hyperacetylation and H3K27ac were measured by ChIP-qPCR in the same conditions as in (E).
    Anti H4 Acetyl, supplied by Active Motif, used in various techniques. Bioz Stars score: 86/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Upstate Biotechnology Inc anti h4 r3me2
    Mutations in Yaf9-YEATS disrupt binding to H3K27ac in vitro and loading of H2A.Z in vivo . ( A ) TAP purification of NuA4 complex using Epl1-TAP tagged background. Yaf9 WT and point mutants (Y70A and W89A) associate with the NuA4 complex, but the C-terminal truncated form (ΔC; 1–186 aa) of Yaf9 does not. Purified NuA4 complex was ran on 10% Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose membrane and detected with indicated antibodies. ( B ) Peptide pull-down assay using indicated H3 peptides and GST-tagged Yaf9-YEATS. Recombinant WT Yaf9 binds to H3K27ac peptides, whereas the W89A mutant does not. None of the proteins show binding to unmodified H3 peptide. Empty GST is used as negative control. ( C ) Chromatin pull-down assay using human nucleosomes and GST-tagged Yaf9-YEATS. WT Yaf9 binds to nucleosomes harboring the H3K27ac mark, while the W89A mutant does not. Empty GST is used as negative control. ( D ) Phenotypic analysis of yeast strains with integrated alleles YAF9 (WT), yaf9-Y70A, yaf9-W89A, yaf9(1–186) and Δyaf9 . The strains expressing the YEATS domain point mutants showed similar growth defects as truncated yaf9(1–186) and Δyaf9 at 16°C, and in the presence of formamide or DNA-damaging agent MMS. ( E ) The point mutation W89A introduced in endogenous Yaf9 creates a strong defect in incorporation of histone variant H2A.Z (Htz1) at the PHO5 gene promoter in vivo . ChIP-qPCR was performed using anti-Htz1 and <t>anti-H4</t> antibodies and the indicated yeast strains. The precipitated DNA was quantified with primers spanning the PHO5 UAS2 region. Data are presented as ratio of IP for Htz1 normalized on total H4. The error bar represents range between two biological replicates. ( F and G ) Levels of H4 hyperacetylation and H3K27ac were measured by ChIP-qPCR in the same conditions as in (E).
    Anti H4 R3me2, supplied by Upstate Biotechnology Inc, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti h4 r3me2/product/Upstate Biotechnology Inc
    Average 85 stars, based on 2 article reviews
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    anti h4 r3me2 - by Bioz Stars, 2020-05
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    85
    Abcam polyclonal anti h4
    Mutations in Yaf9-YEATS disrupt binding to H3K27ac in vitro and loading of H2A.Z in vivo . ( A ) TAP purification of NuA4 complex using Epl1-TAP tagged background. Yaf9 WT and point mutants (Y70A and W89A) associate with the NuA4 complex, but the C-terminal truncated form (ΔC; 1–186 aa) of Yaf9 does not. Purified NuA4 complex was ran on 10% Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose membrane and detected with indicated antibodies. ( B ) Peptide pull-down assay using indicated H3 peptides and GST-tagged Yaf9-YEATS. Recombinant WT Yaf9 binds to H3K27ac peptides, whereas the W89A mutant does not. None of the proteins show binding to unmodified H3 peptide. Empty GST is used as negative control. ( C ) Chromatin pull-down assay using human nucleosomes and GST-tagged Yaf9-YEATS. WT Yaf9 binds to nucleosomes harboring the H3K27ac mark, while the W89A mutant does not. Empty GST is used as negative control. ( D ) Phenotypic analysis of yeast strains with integrated alleles YAF9 (WT), yaf9-Y70A, yaf9-W89A, yaf9(1–186) and Δyaf9 . The strains expressing the YEATS domain point mutants showed similar growth defects as truncated yaf9(1–186) and Δyaf9 at 16°C, and in the presence of formamide or DNA-damaging agent MMS. ( E ) The point mutation W89A introduced in endogenous Yaf9 creates a strong defect in incorporation of histone variant H2A.Z (Htz1) at the PHO5 gene promoter in vivo . ChIP-qPCR was performed using anti-Htz1 and <t>anti-H4</t> antibodies and the indicated yeast strains. The precipitated DNA was quantified with primers spanning the PHO5 UAS2 region. Data are presented as ratio of IP for Htz1 normalized on total H4. The error bar represents range between two biological replicates. ( F and G ) Levels of H4 hyperacetylation and H3K27ac were measured by ChIP-qPCR in the same conditions as in (E).
    Polyclonal Anti H4, supplied by Abcam, used in various techniques. Bioz Stars score: 85/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Millipore h4 k12ac
    Mutations in Yaf9-YEATS disrupt binding to H3K27ac in vitro and loading of H2A.Z in vivo . ( A ) TAP purification of NuA4 complex using Epl1-TAP tagged background. Yaf9 WT and point mutants (Y70A and W89A) associate with the NuA4 complex, but the C-terminal truncated form (ΔC; 1–186 aa) of Yaf9 does not. Purified NuA4 complex was ran on 10% Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose membrane and detected with indicated antibodies. ( B ) Peptide pull-down assay using indicated H3 peptides and GST-tagged Yaf9-YEATS. Recombinant WT Yaf9 binds to H3K27ac peptides, whereas the W89A mutant does not. None of the proteins show binding to unmodified H3 peptide. Empty GST is used as negative control. ( C ) Chromatin pull-down assay using human nucleosomes and GST-tagged Yaf9-YEATS. WT Yaf9 binds to nucleosomes harboring the H3K27ac mark, while the W89A mutant does not. Empty GST is used as negative control. ( D ) Phenotypic analysis of yeast strains with integrated alleles YAF9 (WT), yaf9-Y70A, yaf9-W89A, yaf9(1–186) and Δyaf9 . The strains expressing the YEATS domain point mutants showed similar growth defects as truncated yaf9(1–186) and Δyaf9 at 16°C, and in the presence of formamide or DNA-damaging agent MMS. ( E ) The point mutation W89A introduced in endogenous Yaf9 creates a strong defect in incorporation of histone variant H2A.Z (Htz1) at the PHO5 gene promoter in vivo . ChIP-qPCR was performed using anti-Htz1 and <t>anti-H4</t> antibodies and the indicated yeast strains. The precipitated DNA was quantified with primers spanning the PHO5 UAS2 region. Data are presented as ratio of IP for Htz1 normalized on total H4. The error bar represents range between two biological replicates. ( F and G ) Levels of H4 hyperacetylation and H3K27ac were measured by ChIP-qPCR in the same conditions as in (E).
    H4 K12ac, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Active Motif h4 k16ac
    Mutations in Yaf9-YEATS disrupt binding to H3K27ac in vitro and loading of H2A.Z in vivo . ( A ) TAP purification of NuA4 complex using Epl1-TAP tagged background. Yaf9 WT and point mutants (Y70A and W89A) associate with the NuA4 complex, but the C-terminal truncated form (ΔC; 1–186 aa) of Yaf9 does not. Purified NuA4 complex was ran on 10% Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose membrane and detected with indicated antibodies. ( B ) Peptide pull-down assay using indicated H3 peptides and GST-tagged Yaf9-YEATS. Recombinant WT Yaf9 binds to H3K27ac peptides, whereas the W89A mutant does not. None of the proteins show binding to unmodified H3 peptide. Empty GST is used as negative control. ( C ) Chromatin pull-down assay using human nucleosomes and GST-tagged Yaf9-YEATS. WT Yaf9 binds to nucleosomes harboring the H3K27ac mark, while the W89A mutant does not. Empty GST is used as negative control. ( D ) Phenotypic analysis of yeast strains with integrated alleles YAF9 (WT), yaf9-Y70A, yaf9-W89A, yaf9(1–186) and Δyaf9 . The strains expressing the YEATS domain point mutants showed similar growth defects as truncated yaf9(1–186) and Δyaf9 at 16°C, and in the presence of formamide or DNA-damaging agent MMS. ( E ) The point mutation W89A introduced in endogenous Yaf9 creates a strong defect in incorporation of histone variant H2A.Z (Htz1) at the PHO5 gene promoter in vivo . ChIP-qPCR was performed using anti-Htz1 and <t>anti-H4</t> antibodies and the indicated yeast strains. The precipitated DNA was quantified with primers spanning the PHO5 UAS2 region. Data are presented as ratio of IP for Htz1 normalized on total H4. The error bar represents range between two biological replicates. ( F and G ) Levels of H4 hyperacetylation and H3K27ac were measured by ChIP-qPCR in the same conditions as in (E).
    H4 K16ac, supplied by Active Motif, used in various techniques. Bioz Stars score: 88/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    h4 k16ac - by Bioz Stars, 2020-05
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    85
    Abcam h4 k5ac
    Mutations in Yaf9-YEATS disrupt binding to H3K27ac in vitro and loading of H2A.Z in vivo . ( A ) TAP purification of NuA4 complex using Epl1-TAP tagged background. Yaf9 WT and point mutants (Y70A and W89A) associate with the NuA4 complex, but the C-terminal truncated form (ΔC; 1–186 aa) of Yaf9 does not. Purified NuA4 complex was ran on 10% Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose membrane and detected with indicated antibodies. ( B ) Peptide pull-down assay using indicated H3 peptides and GST-tagged Yaf9-YEATS. Recombinant WT Yaf9 binds to H3K27ac peptides, whereas the W89A mutant does not. None of the proteins show binding to unmodified H3 peptide. Empty GST is used as negative control. ( C ) Chromatin pull-down assay using human nucleosomes and GST-tagged Yaf9-YEATS. WT Yaf9 binds to nucleosomes harboring the H3K27ac mark, while the W89A mutant does not. Empty GST is used as negative control. ( D ) Phenotypic analysis of yeast strains with integrated alleles YAF9 (WT), yaf9-Y70A, yaf9-W89A, yaf9(1–186) and Δyaf9 . The strains expressing the YEATS domain point mutants showed similar growth defects as truncated yaf9(1–186) and Δyaf9 at 16°C, and in the presence of formamide or DNA-damaging agent MMS. ( E ) The point mutation W89A introduced in endogenous Yaf9 creates a strong defect in incorporation of histone variant H2A.Z (Htz1) at the PHO5 gene promoter in vivo . ChIP-qPCR was performed using anti-Htz1 and <t>anti-H4</t> antibodies and the indicated yeast strains. The precipitated DNA was quantified with primers spanning the PHO5 UAS2 region. Data are presented as ratio of IP for Htz1 normalized on total H4. The error bar represents range between two biological replicates. ( F and G ) Levels of H4 hyperacetylation and H3K27ac were measured by ChIP-qPCR in the same conditions as in (E).
    H4 K5ac, supplied by Abcam, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    h4 k5ac - by Bioz Stars, 2020-05
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    88
    Bethyl h4 k16ac
    Mutations in Yaf9-YEATS disrupt binding to H3K27ac in vitro and loading of H2A.Z in vivo . ( A ) TAP purification of NuA4 complex using Epl1-TAP tagged background. Yaf9 WT and point mutants (Y70A and W89A) associate with the NuA4 complex, but the C-terminal truncated form (ΔC; 1–186 aa) of Yaf9 does not. Purified NuA4 complex was ran on 10% Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose membrane and detected with indicated antibodies. ( B ) Peptide pull-down assay using indicated H3 peptides and GST-tagged Yaf9-YEATS. Recombinant WT Yaf9 binds to H3K27ac peptides, whereas the W89A mutant does not. None of the proteins show binding to unmodified H3 peptide. Empty GST is used as negative control. ( C ) Chromatin pull-down assay using human nucleosomes and GST-tagged Yaf9-YEATS. WT Yaf9 binds to nucleosomes harboring the H3K27ac mark, while the W89A mutant does not. Empty GST is used as negative control. ( D ) Phenotypic analysis of yeast strains with integrated alleles YAF9 (WT), yaf9-Y70A, yaf9-W89A, yaf9(1–186) and Δyaf9 . The strains expressing the YEATS domain point mutants showed similar growth defects as truncated yaf9(1–186) and Δyaf9 at 16°C, and in the presence of formamide or DNA-damaging agent MMS. ( E ) The point mutation W89A introduced in endogenous Yaf9 creates a strong defect in incorporation of histone variant H2A.Z (Htz1) at the PHO5 gene promoter in vivo . ChIP-qPCR was performed using anti-Htz1 and <t>anti-H4</t> antibodies and the indicated yeast strains. The precipitated DNA was quantified with primers spanning the PHO5 UAS2 region. Data are presented as ratio of IP for Htz1 normalized on total H4. The error bar represents range between two biological replicates. ( F and G ) Levels of H4 hyperacetylation and H3K27ac were measured by ChIP-qPCR in the same conditions as in (E).
    H4 K16ac, supplied by Bethyl, used in various techniques. Bioz Stars score: 88/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Upstate Biotechnology Inc anti h4 acetyl
    Mutations in Yaf9-YEATS disrupt binding to H3K27ac in vitro and loading of H2A.Z in vivo . ( A ) TAP purification of NuA4 complex using Epl1-TAP tagged background. Yaf9 WT and point mutants (Y70A and W89A) associate with the NuA4 complex, but the C-terminal truncated form (ΔC; 1–186 aa) of Yaf9 does not. Purified NuA4 complex was ran on 10% Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose membrane and detected with indicated antibodies. ( B ) Peptide pull-down assay using indicated H3 peptides and GST-tagged Yaf9-YEATS. Recombinant WT Yaf9 binds to H3K27ac peptides, whereas the W89A mutant does not. None of the proteins show binding to unmodified H3 peptide. Empty GST is used as negative control. ( C ) Chromatin pull-down assay using human nucleosomes and GST-tagged Yaf9-YEATS. WT Yaf9 binds to nucleosomes harboring the H3K27ac mark, while the W89A mutant does not. Empty GST is used as negative control. ( D ) Phenotypic analysis of yeast strains with integrated alleles YAF9 (WT), yaf9-Y70A, yaf9-W89A, yaf9(1–186) and Δyaf9 . The strains expressing the YEATS domain point mutants showed similar growth defects as truncated yaf9(1–186) and Δyaf9 at 16°C, and in the presence of formamide or DNA-damaging agent MMS. ( E ) The point mutation W89A introduced in endogenous Yaf9 creates a strong defect in incorporation of histone variant H2A.Z (Htz1) at the PHO5 gene promoter in vivo . ChIP-qPCR was performed using anti-Htz1 and <t>anti-H4</t> antibodies and the indicated yeast strains. The precipitated DNA was quantified with primers spanning the PHO5 UAS2 region. Data are presented as ratio of IP for Htz1 normalized on total H4. The error bar represents range between two biological replicates. ( F and G ) Levels of H4 hyperacetylation and H3K27ac were measured by ChIP-qPCR in the same conditions as in (E).
    Anti H4 Acetyl, supplied by Upstate Biotechnology Inc, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti h4 acetyl/product/Upstate Biotechnology Inc
    Average 85 stars, based on 5 article reviews
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    anti h4 acetyl - by Bioz Stars, 2020-05
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    Santa Cruz Biotechnology h4 lys12
    Mutations in Yaf9-YEATS disrupt binding to H3K27ac in vitro and loading of H2A.Z in vivo . ( A ) TAP purification of NuA4 complex using Epl1-TAP tagged background. Yaf9 WT and point mutants (Y70A and W89A) associate with the NuA4 complex, but the C-terminal truncated form (ΔC; 1–186 aa) of Yaf9 does not. Purified NuA4 complex was ran on 10% Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose membrane and detected with indicated antibodies. ( B ) Peptide pull-down assay using indicated H3 peptides and GST-tagged Yaf9-YEATS. Recombinant WT Yaf9 binds to H3K27ac peptides, whereas the W89A mutant does not. None of the proteins show binding to unmodified H3 peptide. Empty GST is used as negative control. ( C ) Chromatin pull-down assay using human nucleosomes and GST-tagged Yaf9-YEATS. WT Yaf9 binds to nucleosomes harboring the H3K27ac mark, while the W89A mutant does not. Empty GST is used as negative control. ( D ) Phenotypic analysis of yeast strains with integrated alleles YAF9 (WT), yaf9-Y70A, yaf9-W89A, yaf9(1–186) and Δyaf9 . The strains expressing the YEATS domain point mutants showed similar growth defects as truncated yaf9(1–186) and Δyaf9 at 16°C, and in the presence of formamide or DNA-damaging agent MMS. ( E ) The point mutation W89A introduced in endogenous Yaf9 creates a strong defect in incorporation of histone variant H2A.Z (Htz1) at the PHO5 gene promoter in vivo . ChIP-qPCR was performed using anti-Htz1 and <t>anti-H4</t> antibodies and the indicated yeast strains. The precipitated DNA was quantified with primers spanning the PHO5 UAS2 region. Data are presented as ratio of IP for Htz1 normalized on total H4. The error bar represents range between two biological replicates. ( F and G ) Levels of H4 hyperacetylation and H3K27ac were measured by ChIP-qPCR in the same conditions as in (E).
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    Millipore h4 k16ac
    Mutations in Yaf9-YEATS disrupt binding to H3K27ac in vitro and loading of H2A.Z in vivo . ( A ) TAP purification of NuA4 complex using Epl1-TAP tagged background. Yaf9 WT and point mutants (Y70A and W89A) associate with the NuA4 complex, but the C-terminal truncated form (ΔC; 1–186 aa) of Yaf9 does not. Purified NuA4 complex was ran on 10% Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose membrane and detected with indicated antibodies. ( B ) Peptide pull-down assay using indicated H3 peptides and GST-tagged Yaf9-YEATS. Recombinant WT Yaf9 binds to H3K27ac peptides, whereas the W89A mutant does not. None of the proteins show binding to unmodified H3 peptide. Empty GST is used as negative control. ( C ) Chromatin pull-down assay using human nucleosomes and GST-tagged Yaf9-YEATS. WT Yaf9 binds to nucleosomes harboring the H3K27ac mark, while the W89A mutant does not. Empty GST is used as negative control. ( D ) Phenotypic analysis of yeast strains with integrated alleles YAF9 (WT), yaf9-Y70A, yaf9-W89A, yaf9(1–186) and Δyaf9 . The strains expressing the YEATS domain point mutants showed similar growth defects as truncated yaf9(1–186) and Δyaf9 at 16°C, and in the presence of formamide or DNA-damaging agent MMS. ( E ) The point mutation W89A introduced in endogenous Yaf9 creates a strong defect in incorporation of histone variant H2A.Z (Htz1) at the PHO5 gene promoter in vivo . ChIP-qPCR was performed using anti-Htz1 and <t>anti-H4</t> antibodies and the indicated yeast strains. The precipitated DNA was quantified with primers spanning the PHO5 UAS2 region. Data are presented as ratio of IP for Htz1 normalized on total H4. The error bar represents range between two biological replicates. ( F and G ) Levels of H4 hyperacetylation and H3K27ac were measured by ChIP-qPCR in the same conditions as in (E).
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    Millipore anti h4 antibodies
    Different types of nucleosome occupancy change in the Plasmodium genome . Shown here are representatives of each type. The left panel was generated from the microarray data. Lines indicate average log 2 ratio of H4 ChIP divided by genomic DNA hybridization intensity over 150 bp windows: blue = ring, green = trophozoite, red = schizont. Blue (Red) genes are encoded on the top (bottom) strand. The x-axis indicates the base pair position on the chromosome. The right panel shows Q-PCR results to validate the microarray results. The relative enrichment level represents the 2 -ΔΔCt value obtained by comparing <t>anti-H4</t> ChIP DNA with input DNA and normalizing the data with the control gene MAL8P1.36 which had relative stable nucleosome occupancy through IDC.
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    Opposite effects of IRF1 and IRF4 on histone acetylation at Il9 locus. ( a – d ) Purified WT and ( a , b ) Irf4 −/− or ( c , d ) Irf1 −/− CD4 + T cells were cultured under Th9 conditions with or without IFN-γ. ( a , c ) ChIP analysis of histone H4 acetylation (Ac) at CNS of the Il9 gene. ( c ) Bars show fold induction of <t>H4-Ac</t> relative to WT Th9 cells treated with IFN-γ. ( b , d ) ChIP analysis for RNA polymerase II (pol II) occupancy at Il9 and Rpl32 genes. ( a – d ) The same chromatin was used for control ChIP experiments with control IgG. Precipitated DNA is presented relative to input (% input). Values for nonspecific binding (as determined by using control IgG) were subtracted. ( a – d ) Data are shown as mean±s.d. of combined results from two independent experiments (triplicates to quintuplets in qRT-PCR). The experiments were repeated ( b ) three or ( d ) five times with consistent results. * P
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    Cell Signaling Technology Inc rabbit anti h4
    Opposite effects of IRF1 and IRF4 on histone acetylation at Il9 locus. ( a – d ) Purified WT and ( a , b ) Irf4 −/− or ( c , d ) Irf1 −/− CD4 + T cells were cultured under Th9 conditions with or without IFN-γ. ( a , c ) ChIP analysis of histone H4 acetylation (Ac) at CNS of the Il9 gene. ( c ) Bars show fold induction of <t>H4-Ac</t> relative to WT Th9 cells treated with IFN-γ. ( b , d ) ChIP analysis for RNA polymerase II (pol II) occupancy at Il9 and Rpl32 genes. ( a – d ) The same chromatin was used for control ChIP experiments with control IgG. Precipitated DNA is presented relative to input (% input). Values for nonspecific binding (as determined by using control IgG) were subtracted. ( a – d ) Data are shown as mean±s.d. of combined results from two independent experiments (triplicates to quintuplets in qRT-PCR). The experiments were repeated ( b ) three or ( d ) five times with consistent results. * P
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    Opposite effects of IRF1 and IRF4 on histone acetylation at Il9 locus. ( a – d ) Purified WT and ( a , b ) Irf4 −/− or ( c , d ) Irf1 −/− CD4 + T cells were cultured under Th9 conditions with or without IFN-γ. ( a , c ) ChIP analysis of histone H4 acetylation (Ac) at CNS of the Il9 gene. ( c ) Bars show fold induction of <t>H4-Ac</t> relative to WT Th9 cells treated with IFN-γ. ( b , d ) ChIP analysis for RNA polymerase II (pol II) occupancy at Il9 and Rpl32 genes. ( a – d ) The same chromatin was used for control ChIP experiments with control IgG. Precipitated DNA is presented relative to input (% input). Values for nonspecific binding (as determined by using control IgG) were subtracted. ( a – d ) Data are shown as mean±s.d. of combined results from two independent experiments (triplicates to quintuplets in qRT-PCR). The experiments were repeated ( b ) three or ( d ) five times with consistent results. * P
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    Millipore h4 upstate millipore
    Opposite effects of IRF1 and IRF4 on histone acetylation at Il9 locus. ( a – d ) Purified WT and ( a , b ) Irf4 −/− or ( c , d ) Irf1 −/− CD4 + T cells were cultured under Th9 conditions with or without IFN-γ. ( a , c ) ChIP analysis of histone H4 acetylation (Ac) at CNS of the Il9 gene. ( c ) Bars show fold induction of <t>H4-Ac</t> relative to WT Th9 cells treated with IFN-γ. ( b , d ) ChIP analysis for RNA polymerase II (pol II) occupancy at Il9 and Rpl32 genes. ( a – d ) The same chromatin was used for control ChIP experiments with control IgG. Precipitated DNA is presented relative to input (% input). Values for nonspecific binding (as determined by using control IgG) were subtracted. ( a – d ) Data are shown as mean±s.d. of combined results from two independent experiments (triplicates to quintuplets in qRT-PCR). The experiments were repeated ( b ) three or ( d ) five times with consistent results. * P
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    Image Search Results


    Induction of apoptosis by BZ in hypoxia. ( A ) Total cell lysates in Laemmli buffer were subjected to immuno-blotting with the indicated antibodies. Anti-H4 was used to verify equalization of protein loading. One representative experiment out of 3 is shown. ( B ) Percentages cells undergone “early” (annexin-V+/PI-) or “late” (annexin-V+/PI+) apoptosis, as determined by flow-cytometry. Values are means±S.E.M. of 3 independent experiments.

    Journal: PLoS ONE

    Article Title: Hypoxia Selects Bortezomib-Resistant Stem Cells of Chronic Myeloid Leukemia

    doi: 10.1371/journal.pone.0017008

    Figure Lengend Snippet: Induction of apoptosis by BZ in hypoxia. ( A ) Total cell lysates in Laemmli buffer were subjected to immuno-blotting with the indicated antibodies. Anti-H4 was used to verify equalization of protein loading. One representative experiment out of 3 is shown. ( B ) Percentages cells undergone “early” (annexin-V+/PI-) or “late” (annexin-V+/PI+) apoptosis, as determined by flow-cytometry. Values are means±S.E.M. of 3 independent experiments.

    Article Snippet: Primary (all rabbit) antibodies were: anti-c-Abl and anti-cleaved-caspase 3 (from Cell Signaling Technology, Danvers, MA, U.S.A.), anti-caspase 3 and anti-ERK-1/2 (from Santa Cruz Biotechnology, S. Cruz, CA, U.S.A.), anti-H4 (from Millipore, Billerica, MA, U.S.A.) and anti-vinculin (from Sigma-Aldrich®, St. Louis, MO, U.S.A.).

    Techniques: Flow Cytometry, Cytometry

    Mutations in Yaf9-YEATS disrupt binding to H3K27ac in vitro and loading of H2A.Z in vivo . ( A ) TAP purification of NuA4 complex using Epl1-TAP tagged background. Yaf9 WT and point mutants (Y70A and W89A) associate with the NuA4 complex, but the C-terminal truncated form (ΔC; 1–186 aa) of Yaf9 does not. Purified NuA4 complex was ran on 10% Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose membrane and detected with indicated antibodies. ( B ) Peptide pull-down assay using indicated H3 peptides and GST-tagged Yaf9-YEATS. Recombinant WT Yaf9 binds to H3K27ac peptides, whereas the W89A mutant does not. None of the proteins show binding to unmodified H3 peptide. Empty GST is used as negative control. ( C ) Chromatin pull-down assay using human nucleosomes and GST-tagged Yaf9-YEATS. WT Yaf9 binds to nucleosomes harboring the H3K27ac mark, while the W89A mutant does not. Empty GST is used as negative control. ( D ) Phenotypic analysis of yeast strains with integrated alleles YAF9 (WT), yaf9-Y70A, yaf9-W89A, yaf9(1–186) and Δyaf9 . The strains expressing the YEATS domain point mutants showed similar growth defects as truncated yaf9(1–186) and Δyaf9 at 16°C, and in the presence of formamide or DNA-damaging agent MMS. ( E ) The point mutation W89A introduced in endogenous Yaf9 creates a strong defect in incorporation of histone variant H2A.Z (Htz1) at the PHO5 gene promoter in vivo . ChIP-qPCR was performed using anti-Htz1 and anti-H4 antibodies and the indicated yeast strains. The precipitated DNA was quantified with primers spanning the PHO5 UAS2 region. Data are presented as ratio of IP for Htz1 normalized on total H4. The error bar represents range between two biological replicates. ( F and G ) Levels of H4 hyperacetylation and H3K27ac were measured by ChIP-qPCR in the same conditions as in (E).

    Journal: Nucleic Acids Research

    Article Title: Yaf9 subunit of the NuA4 and SWR1 complexes targets histone H3K27ac through its YEATS domain

    doi: 10.1093/nar/gkx1151

    Figure Lengend Snippet: Mutations in Yaf9-YEATS disrupt binding to H3K27ac in vitro and loading of H2A.Z in vivo . ( A ) TAP purification of NuA4 complex using Epl1-TAP tagged background. Yaf9 WT and point mutants (Y70A and W89A) associate with the NuA4 complex, but the C-terminal truncated form (ΔC; 1–186 aa) of Yaf9 does not. Purified NuA4 complex was ran on 10% Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose membrane and detected with indicated antibodies. ( B ) Peptide pull-down assay using indicated H3 peptides and GST-tagged Yaf9-YEATS. Recombinant WT Yaf9 binds to H3K27ac peptides, whereas the W89A mutant does not. None of the proteins show binding to unmodified H3 peptide. Empty GST is used as negative control. ( C ) Chromatin pull-down assay using human nucleosomes and GST-tagged Yaf9-YEATS. WT Yaf9 binds to nucleosomes harboring the H3K27ac mark, while the W89A mutant does not. Empty GST is used as negative control. ( D ) Phenotypic analysis of yeast strains with integrated alleles YAF9 (WT), yaf9-Y70A, yaf9-W89A, yaf9(1–186) and Δyaf9 . The strains expressing the YEATS domain point mutants showed similar growth defects as truncated yaf9(1–186) and Δyaf9 at 16°C, and in the presence of formamide or DNA-damaging agent MMS. ( E ) The point mutation W89A introduced in endogenous Yaf9 creates a strong defect in incorporation of histone variant H2A.Z (Htz1) at the PHO5 gene promoter in vivo . ChIP-qPCR was performed using anti-Htz1 and anti-H4 antibodies and the indicated yeast strains. The precipitated DNA was quantified with primers spanning the PHO5 UAS2 region. Data are presented as ratio of IP for Htz1 normalized on total H4. The error bar represents range between two biological replicates. ( F and G ) Levels of H4 hyperacetylation and H3K27ac were measured by ChIP-qPCR in the same conditions as in (E).

    Article Snippet: After washes in the same buffer, western blotting was performed with anti-H3K27ac (Abcam) and anti-H4 (Abcam).

    Techniques: Binding Assay, In Vitro, In Vivo, Purification, Polyacrylamide Gel Electrophoresis, Pull Down Assay, Recombinant, Mutagenesis, Negative Control, Expressing, Variant Assay, Chromatin Immunoprecipitation, Real-time Polymerase Chain Reaction

    Different types of nucleosome occupancy change in the Plasmodium genome . Shown here are representatives of each type. The left panel was generated from the microarray data. Lines indicate average log 2 ratio of H4 ChIP divided by genomic DNA hybridization intensity over 150 bp windows: blue = ring, green = trophozoite, red = schizont. Blue (Red) genes are encoded on the top (bottom) strand. The x-axis indicates the base pair position on the chromosome. The right panel shows Q-PCR results to validate the microarray results. The relative enrichment level represents the 2 -ΔΔCt value obtained by comparing anti-H4 ChIP DNA with input DNA and normalizing the data with the control gene MAL8P1.36 which had relative stable nucleosome occupancy through IDC.

    Journal: BMC Genomics

    Article Title: Genome-wide nucleosome mapping of Plasmodium falciparum reveals histone-rich coding and histone-poor intergenic regions and chromatin remodeling of core and subtelomeric genes

    doi: 10.1186/1471-2164-10-610

    Figure Lengend Snippet: Different types of nucleosome occupancy change in the Plasmodium genome . Shown here are representatives of each type. The left panel was generated from the microarray data. Lines indicate average log 2 ratio of H4 ChIP divided by genomic DNA hybridization intensity over 150 bp windows: blue = ring, green = trophozoite, red = schizont. Blue (Red) genes are encoded on the top (bottom) strand. The x-axis indicates the base pair position on the chromosome. The right panel shows Q-PCR results to validate the microarray results. The relative enrichment level represents the 2 -ΔΔCt value obtained by comparing anti-H4 ChIP DNA with input DNA and normalizing the data with the control gene MAL8P1.36 which had relative stable nucleosome occupancy through IDC.

    Article Snippet: After removing cell debris by centrifugation, the digested chromatin was used for IP with the anti-H4 antibodies (Millipore) as previously described [ ].

    Techniques: Generated, Microarray, Chromatin Immunoprecipitation, DNA Hybridization, Polymerase Chain Reaction

    Opposite effects of IRF1 and IRF4 on histone acetylation at Il9 locus. ( a – d ) Purified WT and ( a , b ) Irf4 −/− or ( c , d ) Irf1 −/− CD4 + T cells were cultured under Th9 conditions with or without IFN-γ. ( a , c ) ChIP analysis of histone H4 acetylation (Ac) at CNS of the Il9 gene. ( c ) Bars show fold induction of H4-Ac relative to WT Th9 cells treated with IFN-γ. ( b , d ) ChIP analysis for RNA polymerase II (pol II) occupancy at Il9 and Rpl32 genes. ( a – d ) The same chromatin was used for control ChIP experiments with control IgG. Precipitated DNA is presented relative to input (% input). Values for nonspecific binding (as determined by using control IgG) were subtracted. ( a – d ) Data are shown as mean±s.d. of combined results from two independent experiments (triplicates to quintuplets in qRT-PCR). The experiments were repeated ( b ) three or ( d ) five times with consistent results. * P

    Journal: Nature Communications

    Article Title: Reciprocal regulation of the Il9 locus by counteracting activities of transcription factors IRF1 and IRF4

    doi: 10.1038/ncomms15366

    Figure Lengend Snippet: Opposite effects of IRF1 and IRF4 on histone acetylation at Il9 locus. ( a – d ) Purified WT and ( a , b ) Irf4 −/− or ( c , d ) Irf1 −/− CD4 + T cells were cultured under Th9 conditions with or without IFN-γ. ( a , c ) ChIP analysis of histone H4 acetylation (Ac) at CNS of the Il9 gene. ( c ) Bars show fold induction of H4-Ac relative to WT Th9 cells treated with IFN-γ. ( b , d ) ChIP analysis for RNA polymerase II (pol II) occupancy at Il9 and Rpl32 genes. ( a – d ) The same chromatin was used for control ChIP experiments with control IgG. Precipitated DNA is presented relative to input (% input). Values for nonspecific binding (as determined by using control IgG) were subtracted. ( a – d ) Data are shown as mean±s.d. of combined results from two independent experiments (triplicates to quintuplets in qRT-PCR). The experiments were repeated ( b ) three or ( d ) five times with consistent results. * P

    Article Snippet: For immunoprecipitation, 2.5–4 μg of the following Abs were used: anti-IRF1 (M-20, sc-640x, Santa Cruz), anti-STAT1 (#9172, Cell Signaling), anti-RNA pol II (N-20, sc-899x, Santa Cruz), anti-H4-Ac (06-866, Millipore) and control IgG (#2729, Cell Signaling). qRT-PCR with the precipitated chromatin was performed to calculate the percentage of input.

    Techniques: Purification, Cell Culture, Chromatin Immunoprecipitation, Binding Assay, Quantitative RT-PCR