recombinant histones h3 3  (New England Biolabs)


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    New England Biolabs recombinant histones h3 3
    Recombinant Histones H3 3, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    recombinant histones h3 3  (New England Biolabs)


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    New England Biolabs recombinant histones h3 3
    Recombinant Histones H3 3, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    recombinant histone h3 1  (New England Biolabs)


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    New England Biolabs recombinant histone h3 1
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    histone h3 3  (New England Biolabs)


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    New England Biolabs histone h3 3
    Histone H3 3, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    histone h3 3  (New England Biolabs)


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    New England Biolabs histone h3 3
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    human histone h3 3  (New England Biolabs)


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    New England Biolabs human histone h3 3
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    human h3 3  (New England Biolabs)


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    New England Biolabs human h3 3
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    human h3 3  (New England Biolabs)


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    New England Biolabs human h3 3
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    histone h3 3  (New England Biolabs)


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    New England Biolabs histone h3 3
    SUMOylation increase PIM1 kinase activity in vitro . ( a ) Bacterially purified 6His-PIM1 was SUMOylated in vitro using purified GST-SUMO2. Equal amounts of SUMOylated protein (including PIM1) were captured using GST-beads and incubated without or with SENP1 catalytic domain for 1 hour at 30 °C. Kinase assays were then performed using Histone <t>H3.3</t> as a substrate for at 30 °C for 0, 15, 30 and 45 min. Kinase activity of SUMO2-modified or unmodified PIM1 was measured by analyzing Histone H3.3 phosphorylation using a phospho-specific antibody. Equal levels of substrate and kinase were confirmed by western blotting using indicated antibodies. ( b ) Purified WT PIM1 was first incubated with or without SENP1 catalytic domain fragment for 1 hour at 30 °C, and immediately used in a kinase assay using Histone H3.3 as substrate for 30 min at 30 °C. PIM1 kinase activity was measured by analyzing Histone H3.3 phosphorylation using a phospho-specific antibody. Equal levels of substrate and kinase were confirmed by coomassie staining of the gel.
    Histone H3 3, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "A functional SUMO-motif in the active site of PIM1 promotes its degradation via RNF4, and stimulates protein kinase activity"

    Article Title: A functional SUMO-motif in the active site of PIM1 promotes its degradation via RNF4, and stimulates protein kinase activity

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-03775-w

    SUMOylation increase PIM1 kinase activity in vitro . ( a ) Bacterially purified 6His-PIM1 was SUMOylated in vitro using purified GST-SUMO2. Equal amounts of SUMOylated protein (including PIM1) were captured using GST-beads and incubated without or with SENP1 catalytic domain for 1 hour at 30 °C. Kinase assays were then performed using Histone H3.3 as a substrate for at 30 °C for 0, 15, 30 and 45 min. Kinase activity of SUMO2-modified or unmodified PIM1 was measured by analyzing Histone H3.3 phosphorylation using a phospho-specific antibody. Equal levels of substrate and kinase were confirmed by western blotting using indicated antibodies. ( b ) Purified WT PIM1 was first incubated with or without SENP1 catalytic domain fragment for 1 hour at 30 °C, and immediately used in a kinase assay using Histone H3.3 as substrate for 30 min at 30 °C. PIM1 kinase activity was measured by analyzing Histone H3.3 phosphorylation using a phospho-specific antibody. Equal levels of substrate and kinase were confirmed by coomassie staining of the gel.
    Figure Legend Snippet: SUMOylation increase PIM1 kinase activity in vitro . ( a ) Bacterially purified 6His-PIM1 was SUMOylated in vitro using purified GST-SUMO2. Equal amounts of SUMOylated protein (including PIM1) were captured using GST-beads and incubated without or with SENP1 catalytic domain for 1 hour at 30 °C. Kinase assays were then performed using Histone H3.3 as a substrate for at 30 °C for 0, 15, 30 and 45 min. Kinase activity of SUMO2-modified or unmodified PIM1 was measured by analyzing Histone H3.3 phosphorylation using a phospho-specific antibody. Equal levels of substrate and kinase were confirmed by western blotting using indicated antibodies. ( b ) Purified WT PIM1 was first incubated with or without SENP1 catalytic domain fragment for 1 hour at 30 °C, and immediately used in a kinase assay using Histone H3.3 as substrate for 30 min at 30 °C. PIM1 kinase activity was measured by analyzing Histone H3.3 phosphorylation using a phospho-specific antibody. Equal levels of substrate and kinase were confirmed by coomassie staining of the gel.

    Techniques Used: Activity Assay, In Vitro, Purification, Incubation, Modification, Western Blot, Kinase Assay, Staining

    PIM1 SUMOylation regulates substrate specificity in vitro and in cultured cells. ( a ) 6His-PIM1 (WT or mutant) was expressed and purified from bacterial cells, and resolved by SDS-PAGE. A western blot for the same samples was also performed using a pan-phospho tyrosine antibody to detect PIM1 autophosphorylation. ( b ) The purified 6His-PIM1 proteins were treated with lambda phosphatase (+) to remove overall phosphorylation or untreated (−). Samples were resolved by SDS-PAGE, and stained with coomassie to visualize a shift in mobility, which is indicative of dephosphorylation. ( c ) In vitro kinase assays were carried out using recombinant c-MYC or Histone H3.3 as substrates, in the absence or presence of the indicated purified 6His-PIM1 proteins. The samples were resolved by SDS-PAGE, and either stained with coomassie to detect total protein levels or transferred to a nitrocellulose membrane for western blotting using phospho-specific antibodies as a measure of PIM1 kinase activity. ( d ) U2OS-FRT cells expressing YFP alone, YFP-WT PIM1 and YFP-E171A were treated with 10 ng/ml doxycycline; U2OS-FRT expressing YFP-K169R was treated with 20 ng/ml doxycycline and U2OS-FRT expressing YFP-K67M was treated with 50 ng/ml doxycycline for 48 hours, followed by western blotting using indicated antibodies.
    Figure Legend Snippet: PIM1 SUMOylation regulates substrate specificity in vitro and in cultured cells. ( a ) 6His-PIM1 (WT or mutant) was expressed and purified from bacterial cells, and resolved by SDS-PAGE. A western blot for the same samples was also performed using a pan-phospho tyrosine antibody to detect PIM1 autophosphorylation. ( b ) The purified 6His-PIM1 proteins were treated with lambda phosphatase (+) to remove overall phosphorylation or untreated (−). Samples were resolved by SDS-PAGE, and stained with coomassie to visualize a shift in mobility, which is indicative of dephosphorylation. ( c ) In vitro kinase assays were carried out using recombinant c-MYC or Histone H3.3 as substrates, in the absence or presence of the indicated purified 6His-PIM1 proteins. The samples were resolved by SDS-PAGE, and either stained with coomassie to detect total protein levels or transferred to a nitrocellulose membrane for western blotting using phospho-specific antibodies as a measure of PIM1 kinase activity. ( d ) U2OS-FRT cells expressing YFP alone, YFP-WT PIM1 and YFP-E171A were treated with 10 ng/ml doxycycline; U2OS-FRT expressing YFP-K169R was treated with 20 ng/ml doxycycline and U2OS-FRT expressing YFP-K67M was treated with 50 ng/ml doxycycline for 48 hours, followed by western blotting using indicated antibodies.

    Techniques Used: In Vitro, Cell Culture, Mutagenesis, Purification, SDS Page, Western Blot, Staining, De-Phosphorylation Assay, Recombinant, Activity Assay, Expressing

    recombinant human histones h3  (New England Biolabs)


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    New England Biolabs recombinant human histones h3
    Fluorescence and immunofluorescence microscopy of stimulated human neutrophils for NETs formation. Stimulated normal human neutrophils were seeded on poly-l-lysine–coated slides and incubated at 37°C + 5% CO2 for 3 hours. After incubation, the preparations were fixed using 4% paraformaldehyde and stained using 2.5 μM Sytox Green, a DNA staining dye. Unstimulated neutrophils did not form NETs (A) and were intact after treatment with DNAase (20 μM) (B). Robust NET release after stimulation with 600 nM PMA (C) or 5 μM A23187 (E) as shown by the bright and scattered Sytox Green signal pattern. Digestion of PMA-stimulated (D) and A23187-stimulated (F) NETs after treatment with DNAase (20 μg/mL), indicating the extracellular location of NETs. (G) Dual immunofluorescence staining of NETs by Sytox Green (2.5 μM) for DNA and citrillunated histone <t>H3</t> (red). A23187, calcium ionophore.
    Recombinant Human Histones H3, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "In vitro activation of coagulation by human neutrophil DNA and histone proteins but not neutrophil extracellular traps"

    Article Title: In vitro activation of coagulation by human neutrophil DNA and histone proteins but not neutrophil extracellular traps

    Journal: Blood

    doi: 10.1182/blood-2016-06-722298

    Fluorescence and immunofluorescence microscopy of stimulated human neutrophils for NETs formation. Stimulated normal human neutrophils were seeded on poly-l-lysine–coated slides and incubated at 37°C + 5% CO2 for 3 hours. After incubation, the preparations were fixed using 4% paraformaldehyde and stained using 2.5 μM Sytox Green, a DNA staining dye. Unstimulated neutrophils did not form NETs (A) and were intact after treatment with DNAase (20 μM) (B). Robust NET release after stimulation with 600 nM PMA (C) or 5 μM A23187 (E) as shown by the bright and scattered Sytox Green signal pattern. Digestion of PMA-stimulated (D) and A23187-stimulated (F) NETs after treatment with DNAase (20 μg/mL), indicating the extracellular location of NETs. (G) Dual immunofluorescence staining of NETs by Sytox Green (2.5 μM) for DNA and citrillunated histone H3 (red). A23187, calcium ionophore.
    Figure Legend Snippet: Fluorescence and immunofluorescence microscopy of stimulated human neutrophils for NETs formation. Stimulated normal human neutrophils were seeded on poly-l-lysine–coated slides and incubated at 37°C + 5% CO2 for 3 hours. After incubation, the preparations were fixed using 4% paraformaldehyde and stained using 2.5 μM Sytox Green, a DNA staining dye. Unstimulated neutrophils did not form NETs (A) and were intact after treatment with DNAase (20 μM) (B). Robust NET release after stimulation with 600 nM PMA (C) or 5 μM A23187 (E) as shown by the bright and scattered Sytox Green signal pattern. Digestion of PMA-stimulated (D) and A23187-stimulated (F) NETs after treatment with DNAase (20 μg/mL), indicating the extracellular location of NETs. (G) Dual immunofluorescence staining of NETs by Sytox Green (2.5 μM) for DNA and citrillunated histone H3 (red). A23187, calcium ionophore.

    Techniques Used: Fluorescence, Immunofluorescence, Microscopy, Incubation, Staining

    hnDNA and individual human histone H3 and H4 trigger coagulation in plasma. TG in recalcified normal PFP (A) and normal PRP (B) containing hnDNA. TG in recalcified FXII-deficient (FXII-Def), FXI-deficient (FXI-Def), or FVII-deficient (FVII-Def) PFP in the presence or absence of 30 µg/mL of hnDNA (C). No TG was observed in any individual deficient plasma after recalcification in the absence of DNA, represented by a single flat curve (PFP no DNA, panel C). Quantification of FXIa-AT after activation of the contact system by hnDNA in the synthetic contact system activation assay as described in “Methods” (D). TG in recalcified PRP containing recombinant human histone H3 (rH3) (E) or recombinant human histone H4 (rH4) (F). Effect of citrullination of histones H3 (G) and H4 (H) on TG in recalcified PRP. All the figures are representative of at least 3 independent experiments.
    Figure Legend Snippet: hnDNA and individual human histone H3 and H4 trigger coagulation in plasma. TG in recalcified normal PFP (A) and normal PRP (B) containing hnDNA. TG in recalcified FXII-deficient (FXII-Def), FXI-deficient (FXI-Def), or FVII-deficient (FVII-Def) PFP in the presence or absence of 30 µg/mL of hnDNA (C). No TG was observed in any individual deficient plasma after recalcification in the absence of DNA, represented by a single flat curve (PFP no DNA, panel C). Quantification of FXIa-AT after activation of the contact system by hnDNA in the synthetic contact system activation assay as described in “Methods” (D). TG in recalcified PRP containing recombinant human histone H3 (rH3) (E) or recombinant human histone H4 (rH4) (F). Effect of citrullination of histones H3 (G) and H4 (H) on TG in recalcified PRP. All the figures are representative of at least 3 independent experiments.

    Techniques Used: Coagulation, Activation Assay, Recombinant

    Individual human histones H3 and H4, but not octameric core histones, trigger TG in PRP. TG performed in recalcified PRP containing individual human histone proteins was compared with that of recombinant core histone octamers (A) or purified calf thymus histones (B). CThist, mixture of purified calf thymus histones; rOctamer, octameric core histone reconstituted with recombinant human histone proteins. Panels A and B are representative of 3 independent experiments.
    Figure Legend Snippet: Individual human histones H3 and H4, but not octameric core histones, trigger TG in PRP. TG performed in recalcified PRP containing individual human histone proteins was compared with that of recombinant core histone octamers (A) or purified calf thymus histones (B). CThist, mixture of purified calf thymus histones; rOctamer, octameric core histone reconstituted with recombinant human histone proteins. Panels A and B are representative of 3 independent experiments.

    Techniques Used: Recombinant, Purification

    histone h3 3  (New England Biolabs)


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    New England Biolabs histone h3 3
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    New England Biolabs recombinant histones h3 3
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    New England Biolabs human histone h3 3
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    New England Biolabs human h3 3
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    New England Biolabs recombinant human histones h3
    Fluorescence and immunofluorescence microscopy of stimulated human neutrophils for NETs formation. Stimulated normal human neutrophils were seeded on poly-l-lysine–coated slides and incubated at 37°C + 5% CO2 for 3 hours. After incubation, the preparations were fixed using 4% paraformaldehyde and stained using 2.5 μM Sytox Green, a DNA staining dye. Unstimulated neutrophils did not form NETs (A) and were intact after treatment with DNAase (20 μM) (B). Robust NET release after stimulation with 600 nM PMA (C) or 5 μM A23187 (E) as shown by the bright and scattered Sytox Green signal pattern. Digestion of PMA-stimulated (D) and A23187-stimulated (F) NETs after treatment with DNAase (20 μg/mL), indicating the extracellular location of NETs. (G) Dual immunofluorescence staining of NETs by Sytox Green (2.5 μM) for DNA and citrillunated histone <t>H3</t> (red). A23187, calcium ionophore.
    Recombinant Human Histones H3, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Fluorescence and immunofluorescence microscopy of stimulated human neutrophils for NETs formation. Stimulated normal human neutrophils were seeded on poly-l-lysine–coated slides and incubated at 37°C + 5% CO2 for 3 hours. After incubation, the preparations were fixed using 4% paraformaldehyde and stained using 2.5 μM Sytox Green, a DNA staining dye. Unstimulated neutrophils did not form NETs (A) and were intact after treatment with DNAase (20 μM) (B). Robust NET release after stimulation with 600 nM PMA (C) or 5 μM A23187 (E) as shown by the bright and scattered Sytox Green signal pattern. Digestion of PMA-stimulated (D) and A23187-stimulated (F) NETs after treatment with DNAase (20 μg/mL), indicating the extracellular location of NETs. (G) Dual immunofluorescence staining of NETs by Sytox Green (2.5 μM) for DNA and citrillunated histone H3 (red). A23187, calcium ionophore.

    Journal: Blood

    Article Title: In vitro activation of coagulation by human neutrophil DNA and histone proteins but not neutrophil extracellular traps

    doi: 10.1182/blood-2016-06-722298

    Figure Lengend Snippet: Fluorescence and immunofluorescence microscopy of stimulated human neutrophils for NETs formation. Stimulated normal human neutrophils were seeded on poly-l-lysine–coated slides and incubated at 37°C + 5% CO2 for 3 hours. After incubation, the preparations were fixed using 4% paraformaldehyde and stained using 2.5 μM Sytox Green, a DNA staining dye. Unstimulated neutrophils did not form NETs (A) and were intact after treatment with DNAase (20 μM) (B). Robust NET release after stimulation with 600 nM PMA (C) or 5 μM A23187 (E) as shown by the bright and scattered Sytox Green signal pattern. Digestion of PMA-stimulated (D) and A23187-stimulated (F) NETs after treatment with DNAase (20 μg/mL), indicating the extracellular location of NETs. (G) Dual immunofluorescence staining of NETs by Sytox Green (2.5 μM) for DNA and citrillunated histone H3 (red). A23187, calcium ionophore.

    Article Snippet: Recombinant human histones H3 and H4 were from New England Biolabs (Ipswich, MA); TRAP6 was from R&D Systems (Minneapolis, MN).

    Techniques: Fluorescence, Immunofluorescence, Microscopy, Incubation, Staining

    hnDNA and individual human histone H3 and H4 trigger coagulation in plasma. TG in recalcified normal PFP (A) and normal PRP (B) containing hnDNA. TG in recalcified FXII-deficient (FXII-Def), FXI-deficient (FXI-Def), or FVII-deficient (FVII-Def) PFP in the presence or absence of 30 µg/mL of hnDNA (C). No TG was observed in any individual deficient plasma after recalcification in the absence of DNA, represented by a single flat curve (PFP no DNA, panel C). Quantification of FXIa-AT after activation of the contact system by hnDNA in the synthetic contact system activation assay as described in “Methods” (D). TG in recalcified PRP containing recombinant human histone H3 (rH3) (E) or recombinant human histone H4 (rH4) (F). Effect of citrullination of histones H3 (G) and H4 (H) on TG in recalcified PRP. All the figures are representative of at least 3 independent experiments.

    Journal: Blood

    Article Title: In vitro activation of coagulation by human neutrophil DNA and histone proteins but not neutrophil extracellular traps

    doi: 10.1182/blood-2016-06-722298

    Figure Lengend Snippet: hnDNA and individual human histone H3 and H4 trigger coagulation in plasma. TG in recalcified normal PFP (A) and normal PRP (B) containing hnDNA. TG in recalcified FXII-deficient (FXII-Def), FXI-deficient (FXI-Def), or FVII-deficient (FVII-Def) PFP in the presence or absence of 30 µg/mL of hnDNA (C). No TG was observed in any individual deficient plasma after recalcification in the absence of DNA, represented by a single flat curve (PFP no DNA, panel C). Quantification of FXIa-AT after activation of the contact system by hnDNA in the synthetic contact system activation assay as described in “Methods” (D). TG in recalcified PRP containing recombinant human histone H3 (rH3) (E) or recombinant human histone H4 (rH4) (F). Effect of citrullination of histones H3 (G) and H4 (H) on TG in recalcified PRP. All the figures are representative of at least 3 independent experiments.

    Article Snippet: Recombinant human histones H3 and H4 were from New England Biolabs (Ipswich, MA); TRAP6 was from R&D Systems (Minneapolis, MN).

    Techniques: Coagulation, Activation Assay, Recombinant

    Individual human histones H3 and H4, but not octameric core histones, trigger TG in PRP. TG performed in recalcified PRP containing individual human histone proteins was compared with that of recombinant core histone octamers (A) or purified calf thymus histones (B). CThist, mixture of purified calf thymus histones; rOctamer, octameric core histone reconstituted with recombinant human histone proteins. Panels A and B are representative of 3 independent experiments.

    Journal: Blood

    Article Title: In vitro activation of coagulation by human neutrophil DNA and histone proteins but not neutrophil extracellular traps

    doi: 10.1182/blood-2016-06-722298

    Figure Lengend Snippet: Individual human histones H3 and H4, but not octameric core histones, trigger TG in PRP. TG performed in recalcified PRP containing individual human histone proteins was compared with that of recombinant core histone octamers (A) or purified calf thymus histones (B). CThist, mixture of purified calf thymus histones; rOctamer, octameric core histone reconstituted with recombinant human histone proteins. Panels A and B are representative of 3 independent experiments.

    Article Snippet: Recombinant human histones H3 and H4 were from New England Biolabs (Ipswich, MA); TRAP6 was from R&D Systems (Minneapolis, MN).

    Techniques: Recombinant, Purification