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sf9 insect cells  (Expression Systems Inc)


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    Expression Systems Inc sf9 insect cells
    Sf9 Insect Cells, supplied by Expression Systems Inc, used in various techniques. Bioz Stars score: 99/100, based on 4776 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/sf9+insect+cells/Sf9+Cells/pm42115595-157-7-10
    Average 99 stars, based on 4776 article reviews
    sf9 insect cells - by Bioz Stars, 2026-09
    99/100 stars

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    Recombinant:

    Article Title: Complete inhibition of β-tryptase by tetramer dissociation and active site allostery due to a single antibody residue
    Article Snippet: .. Recombinant baculovirus were generated using the Baculogold system (BD Biosciences, San Jose CA) in Sf9 insect cells (Expression Systems, Davis CA) following standard protocols. .. Tni insect cells (Expression Systems, Davis CA) were infected for large-scale protein production and harvested 48 h post-infection.

    Article Title: Complete inhibition of β-tryptase by tetramer dissociation and active site allostery due to a single antibody residue.
    Article Snippet: .. Recombinant baculovirus were generated using the Baculogold system (BD Biosciences, San Jose CA) in Sf9 insect cells (Expression Systems, Davis CA) following standard protocols. .. Tni insect cells (Expression Systems, Davis CA) were infected for large-scale protein production and harvested 48h post-infection.

    Article Title: Structural basis of CD28 and CTLA-4 interactions with CD80, CD86, and the CD80-PD-L1 heterodimer on artificial and cellular membranes
    Article Snippet: Genes encoding the extracellular domains of CTLA-4, CD28, CD80, CD86, and PD-L1, together with the indicated affinity tags, were synthesized (Twist Bioscience) and cloned into the pAcGP67A or pVL1393 baculovirus transfer vectors (BD Biosciences) (Table S1). .. Recombinant baculoviruses were generated by co-transfection of Sf9 insect cells with the linearized baculovirus genome BestBac2.0 (Expression Systems). .. For protein expression, High Five insect cells cultured in ESF 921 medium (Expression Systems) were infected with the recombinant baculovirus at 3% (v/v) and incubated at 21°C for 72 hours.

    Generated:

    Article Title: Complete inhibition of β-tryptase by tetramer dissociation and active site allostery due to a single antibody residue
    Article Snippet: .. Recombinant baculovirus were generated using the Baculogold system (BD Biosciences, San Jose CA) in Sf9 insect cells (Expression Systems, Davis CA) following standard protocols. .. Tni insect cells (Expression Systems, Davis CA) were infected for large-scale protein production and harvested 48 h post-infection.

    Article Title: Complete inhibition of β-tryptase by tetramer dissociation and active site allostery due to a single antibody residue.
    Article Snippet: .. Recombinant baculovirus were generated using the Baculogold system (BD Biosciences, San Jose CA) in Sf9 insect cells (Expression Systems, Davis CA) following standard protocols. .. Tni insect cells (Expression Systems, Davis CA) were infected for large-scale protein production and harvested 48h post-infection.

    Article Title: Structural basis of CD28 and CTLA-4 interactions with CD80, CD86, and the CD80-PD-L1 heterodimer on artificial and cellular membranes
    Article Snippet: Genes encoding the extracellular domains of CTLA-4, CD28, CD80, CD86, and PD-L1, together with the indicated affinity tags, were synthesized (Twist Bioscience) and cloned into the pAcGP67A or pVL1393 baculovirus transfer vectors (BD Biosciences) (Table S1). .. Recombinant baculoviruses were generated by co-transfection of Sf9 insect cells with the linearized baculovirus genome BestBac2.0 (Expression Systems). .. For protein expression, High Five insect cells cultured in ESF 921 medium (Expression Systems) were infected with the recombinant baculovirus at 3% (v/v) and incubated at 21°C for 72 hours.

    Construct:

    Article Title: Dynamic monomer-dimer transition in ligand-induced apelin receptor activation.
    Article Snippet: .. APLNR, Gαi1 and Gβγ constructs were co-expressed at the ratio of 1:1:1 in sf9 insect cells using the bac-to-bac Baculovirus Expression System (Invitrogen). .. The cells were then incubated for 48 h at 27 °C and subsequently collected by centrifugation at 1,000 × g for 30 min. For the purification of APLNR–Gi1 complexes, the cell pellets were suspended in buffer containing 20 mM HEPES pH 7.5, 2 mM MgCl2, 100 mM NaCl and protease inhibitor cocktail (Bimake), followed by addition of 1.2 mg scFv16 antibody, 12 mU/ml apyrase (Sigma), and agonist (100 nM AMG986 or 1 μM JN241-9).

    Article Title: Dynamic monomer-dimer transition in ligand-induced apelin receptor activation.
    Article Snippet: .. APLNR constructs were expressed in sf9 insect cells using the bac-to-bac Baculovirus Expression System (Invitrogen). ..



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    sf9 insect cells  (ATCC)
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    A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. <t>Sf9-purified</t> PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.
    Sf9 Insect Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    sf9 insect cells  (Expression Systems Inc)
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    A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. <t>Sf9-purified</t> PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.
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    A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. <t>Sf9-purified</t> PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.
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    sf 9 insect cells  (ATCC)
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    A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. <t>Sf9-purified</t> PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.
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    A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. <t>Sf9-purified</t> PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.
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    insect cells  (Expression Systems Inc)
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    A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. <t>Sf9-purified</t> PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.
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    sf9 insect cell cultures  (Expression Systems Inc)
    99
    Expression Systems Inc sf9 insect cell cultures
    A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. <t>Sf9-purified</t> PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.
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    Image Search Results


    A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. Sf9-purified PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.

    Journal: bioRxiv

    Article Title: EZH2 Serine 21 Phosphorylation Restrains Compact-State PRC2 Activation and H3K27me3 Propagation

    doi: 10.64898/2026.06.02.729660

    Figure Lengend Snippet: A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. Sf9-purified PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.

    Article Snippet: Sf9 insect cells were obtained from ATCC (CRL-1711; RRID:CVCL 0549) and were used for baculovirus-mediated expression of recombinant PRC2 complexes.

    Techniques: Purification, Recombinant, Phospho-proteomics, High Throughput Screening Assay, In Vitro, Incubation, Serial Dilution, Western Blot, Activity Assay, Sequencing, Residue, Knock-Out, Plasmid Preparation, Control, ChIP-sequencing, Expressing