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Active Motif core histones
Core Histones, supplied by Active Motif, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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core histones - by Bioz Stars, 2021-07
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Immunohistochemistry:

Article Title: Integrative study of EZH2 mutational status, copy number, protein expression and H3K27 trimethylation in AML/MDS patients
Article Snippet: ImmunohistochemistryProtein expression of EZH2 and H3K27me3 in primary patient cells and normal BM cells from healthy donors was assessed by IHC on formalin-fixed, EDTA-decalcified, paraffin-embedded BM core biopsies. .. The Ezh2 (AC22) mouse monoclonal antibody #3147 (Cell Signaling Technology, Danvers, MA, USA) and the histone H3K27me3 rabbit polyclonal antibody #39,155 (Active Motif, Carlsbad, CA, USA) were used for IHC. .. For EZH2 protein expression analyses, 12 control age- and sex-matched BM biopsy samples were retrieved from the archives.

Agarose Gel Electrophoresis:

Article Title: Acetylation on histone H3 lysine 9 mediates a switch from transcription initiation to elongation
Article Snippet: Briefly, the recombinant Drosophila ACF1/ISWI/NAP-1 assembly system ( ) was used for assembly of recombinant histones (New England Biolabs), modified histones (Active Motif), or HeLa core chromatin (Active Motif) onto the 4xERE-E4 ( ) or the 4xERE-E4-G48 biotinylated fragment. .. The quality of nucleosome assembly was checked by MNase partial digestion using the Chromatin Assembly Kit from Active Motif, followed by agarose gel electrophoresis and ethidium bromide staining. .. Either 120 or 60 μl of Dynabeads® M280 streptavidin beads (Invitrogen) were used to immobilize biotinylated histone peptides (Epicypher) or chromatinized DNA pulldowns, respectively.

Staining:

Article Title: Acetylation on histone H3 lysine 9 mediates a switch from transcription initiation to elongation
Article Snippet: Briefly, the recombinant Drosophila ACF1/ISWI/NAP-1 assembly system ( ) was used for assembly of recombinant histones (New England Biolabs), modified histones (Active Motif), or HeLa core chromatin (Active Motif) onto the 4xERE-E4 ( ) or the 4xERE-E4-G48 biotinylated fragment. .. The quality of nucleosome assembly was checked by MNase partial digestion using the Chromatin Assembly Kit from Active Motif, followed by agarose gel electrophoresis and ethidium bromide staining. .. Either 120 or 60 μl of Dynabeads® M280 streptavidin beads (Invitrogen) were used to immobilize biotinylated histone peptides (Epicypher) or chromatinized DNA pulldowns, respectively.

Incubation:

Article Title: Identification of small molecules that inhibit the histone chaperone Asf1 and its chromatin function
Article Snippet: Beads were washed 4 times with 1 ml of wash buffer, and then equilibrated with 1 ml histone binding buffer [30 mM HEPES-KOH (pH 7.5), 5% glycerol, 100 mM NaCl, 0.1% Triton X-100, 0.1 mM EDTA, and 0.1 mg/ml BSA]. .. Beads were incubated with 1.25 μg of calf-thymus histone H3 (Roche 11 034 758 001) or 3 μg of HeLa core histones (purified with Active Motif core histone purification kit; 40025), in the presence or absence of Asf1 inhibitor candidates (InterBioScreen Ltd, Russia), for 1 hr at room temperature, with rotation. .. Beads were washed 4 times with 1 ml of histone binding buffer.

Article Title: Psip1/Ledgf p52 Binds Methylated Histone H3K36 and Splicing Factors and Contributes to the Regulation of Alternative Splicing
Article Snippet: For histone pulldowns, 1 µg of T7 tagged SRSF1, purified from 293T cells, was incubated with T7 beads in GST lysis buffer for 1 hr at 4°C. .. After washing unbound proteins in same buffer, 1 µg of GST-p52 and 1 µg HeLa core histones (Active motif, cat. 53501) were added and incubated for 3 hrs. ..

Purification:

Article Title: Identification of small molecules that inhibit the histone chaperone Asf1 and its chromatin function
Article Snippet: Beads were washed 4 times with 1 ml of wash buffer, and then equilibrated with 1 ml histone binding buffer [30 mM HEPES-KOH (pH 7.5), 5% glycerol, 100 mM NaCl, 0.1% Triton X-100, 0.1 mM EDTA, and 0.1 mg/ml BSA]. .. Beads were incubated with 1.25 μg of calf-thymus histone H3 (Roche 11 034 758 001) or 3 μg of HeLa core histones (purified with Active Motif core histone purification kit; 40025), in the presence or absence of Asf1 inhibitor candidates (InterBioScreen Ltd, Russia), for 1 hr at room temperature, with rotation. .. Beads were washed 4 times with 1 ml of histone binding buffer.

Article Title: Propofol Inhibits SIRT2 Deacetylase through a Conformation-specific, Allosteric Site *
Article Snippet: Visual molecular dynamics ( ) and PyMOL ( ) were used for other structural analyses and preparation of structural images, and sequence alignments were performed with ClustalW2 ( , ). .. At a final concentration of 50 μg/ml, recombinant human SIRT2 or recombinant human SIRT1 was photolabeled with 4 μ m [3 H]AziP m ± propofol with and without 2 m m ADP-ribose, 100 m m nicotinamide, and 250 ng/μl of core histones purified from HeLa cell chromatin (histones were purchased form Active Motif, Carlsbad, CA). .. Prior to these experiments, histone acetylation was confirmed by Western blot with an acetyl lysine antibody (Cell Signaling Technology, Danvers, MA).

other:

Article Title: Distinctive patterns of epigenetic marks are associated with promoter regions of mouse LINE-1 and LTR retrotransposons
Article Snippet: The histone modifications like H3K4me2 and H3K9me3 are known to be associated with active and inactive promoters of protein-coding genes, respectively.

Concentration Assay:

Article Title: Propofol Inhibits SIRT2 Deacetylase through a Conformation-specific, Allosteric Site *
Article Snippet: Visual molecular dynamics ( ) and PyMOL ( ) were used for other structural analyses and preparation of structural images, and sequence alignments were performed with ClustalW2 ( , ). .. At a final concentration of 50 μg/ml, recombinant human SIRT2 or recombinant human SIRT1 was photolabeled with 4 μ m [3 H]AziP m ± propofol with and without 2 m m ADP-ribose, 100 m m nicotinamide, and 250 ng/μl of core histones purified from HeLa cell chromatin (histones were purchased form Active Motif, Carlsbad, CA). .. Prior to these experiments, histone acetylation was confirmed by Western blot with an acetyl lysine antibody (Cell Signaling Technology, Danvers, MA).

Recombinant:

Article Title: Propofol Inhibits SIRT2 Deacetylase through a Conformation-specific, Allosteric Site *
Article Snippet: Visual molecular dynamics ( ) and PyMOL ( ) were used for other structural analyses and preparation of structural images, and sequence alignments were performed with ClustalW2 ( , ). .. At a final concentration of 50 μg/ml, recombinant human SIRT2 or recombinant human SIRT1 was photolabeled with 4 μ m [3 H]AziP m ± propofol with and without 2 m m ADP-ribose, 100 m m nicotinamide, and 250 ng/μl of core histones purified from HeLa cell chromatin (histones were purchased form Active Motif, Carlsbad, CA). .. Prior to these experiments, histone acetylation was confirmed by Western blot with an acetyl lysine antibody (Cell Signaling Technology, Danvers, MA).

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  • 95
    Active Motif core histone h4
    Characterization of tailless nucleosomes. ( A ) SDS-PAGE of <t>histone</t> proteins. Lane 1: molecular weight markers. Lane 2: tailless core <t>histones</t> from oligonucleosomes that were treated with trypsin. Lane 3: core histones. Lane 4: histone proteins from crude micrococcal nuclease digestion of nuclei. ( B ) EMSA profile for ER binding to the cERE in the tailless nucleosomes (ΔN) . Lanes 1–8: Tailless nucleosomes treated with increasing concentrations of ER (0, 10, 20, 30, 40, 50, 60 and 80 nM, respectively). ( C ) The binding profile of ER to tailless nucleosomes.
    Core Histone H4, supplied by Active Motif, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/core histone h4/product/Active Motif
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    core histone h4 - by Bioz Stars, 2021-07
    95/100 stars
      Buy from Supplier

    95
    Active Motif hela core histones
    In vivo function of chromatin mediated by Asf1 is affected by Asf1 inhibitors. (A) Role of Asf1 isomers in H3K56 acetylation. <t>HeLa</t> cells were treated with siRNAs (200 pmol) targeting Asf1a and Asf1b, either separately or simultaneously, for 24 hr (left panel) and 72 hr (right panel). Depletion of Asf1 and the effect on H3K56 acetylation was determined by immunoblotting assay with whole cell extracts and specific antibodies recognizing Asf1a, Asf1b, and H3K56Ac. (B) Asf1 inhibitors specifically reduced the level of H3K56 acetylation. HeLa cells were treated with each of the Asf1a inhibitors (40 μM) for 24 hr and whole cell lysate was prepared for immunoblotting, and probed with specific antibodies recognizing different histone modification. <t>H3</t> and actin served as loading controls. (C) HSV-1 yield was decreased by treatment of #2-03 and #2-32. Vero cells treated with DMSO (control) or 80 μM of each compound were infected with HSV-1 and viral yields in the culture supernatants were determined using plaque assay. Error bars represent the standard deviations of three independent experiments. Significance of difference was evaluated (*P < 0.05, **P < 0.005).
    Hela Core Histones, supplied by Active Motif, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hela core histones/product/Active Motif
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hela core histones - by Bioz Stars, 2021-07
    95/100 stars
      Buy from Supplier

    Image Search Results


    Characterization of tailless nucleosomes. ( A ) SDS-PAGE of histone proteins. Lane 1: molecular weight markers. Lane 2: tailless core histones from oligonucleosomes that were treated with trypsin. Lane 3: core histones. Lane 4: histone proteins from crude micrococcal nuclease digestion of nuclei. ( B ) EMSA profile for ER binding to the cERE in the tailless nucleosomes (ΔN) . Lanes 1–8: Tailless nucleosomes treated with increasing concentrations of ER (0, 10, 20, 30, 40, 50, 60 and 80 nM, respectively). ( C ) The binding profile of ER to tailless nucleosomes.

    Journal: Nucleic Acids Research

    Article Title: Nucleosome dynamics: HMGB1 relaxes canonical nucleosome structure to facilitate estrogen receptor binding

    doi: 10.1093/nar/gks815

    Figure Lengend Snippet: Characterization of tailless nucleosomes. ( A ) SDS-PAGE of histone proteins. Lane 1: molecular weight markers. Lane 2: tailless core histones from oligonucleosomes that were treated with trypsin. Lane 3: core histones. Lane 4: histone proteins from crude micrococcal nuclease digestion of nuclei. ( B ) EMSA profile for ER binding to the cERE in the tailless nucleosomes (ΔN) . Lanes 1–8: Tailless nucleosomes treated with increasing concentrations of ER (0, 10, 20, 30, 40, 50, 60 and 80 nM, respectively). ( C ) The binding profile of ER to tailless nucleosomes.

    Article Snippet: Antibodies for the core histones (H2A, H2B and H3) and the polyclonal HMGB1 antibody were purchased from Millipore, and the antibody for core histone H4 was purchased from Active Motif.

    Techniques: SDS Page, Molecular Weight, Binding Assay

    Fractionation and EMSA characterization of canonical (N) and HMGB1-restructured nucleosomes (N’/N″). ( A ) Sedimentation profiles. Fractions from a sucrose gradient and their relative counts per minute (CPM) for the canonical nucleosome (closed square) and HMGB1-restructured nucleosome (open circle). The arrow marks with M and D represent the position of mono- and dinucleosome in a sucrose gradient when co-sedimented with canonical nucleosomes and HMGB1-restructured nucleosomes. ( B ) EMSA profiles. EMSA bands for the canonical nucleosome (N), fractions 14–19 and HMGB1-restructured nucleosomes (N′/N″), fractions 14–19. EMSA of canonical nucleosome (N) (Lane 1, fraction 17) and HMGB1-restructured nucleosomes (N′/N″), (Lane 2, fraction 17) run on the same gel. ( C ) The effect of anti-histone antibodies (αH2A, αH2B, αH3, αH4) on canonical (N) and HMGB1-restructured nucleosomes (N′/N″). Lane 1: N; Lanes 2–5: N treated with αH2A, αH2B, αH3 and αH4, respectively. Lane 6: N′/N′; Lanes 7–10: N′/N″ treated with αH2A, αH2B, αH3 and αH4, respectively. ( D ) Atomic force microscopy of N and N′/N″. (A) Canonical mononucleosomes (N) on spermidine-treated mica. (B) HMGB1-restructured nucleosomes (N′/N″) seen as mononucleosomes on spermidine-treated mica. DNA tails, where visible, are indicated by arrows. Insets showing enlarged view of distinct mononucleosomes in both (A) and (B). Scale bar = 20 nm.

    Journal: Nucleic Acids Research

    Article Title: Nucleosome dynamics: HMGB1 relaxes canonical nucleosome structure to facilitate estrogen receptor binding

    doi: 10.1093/nar/gks815

    Figure Lengend Snippet: Fractionation and EMSA characterization of canonical (N) and HMGB1-restructured nucleosomes (N’/N″). ( A ) Sedimentation profiles. Fractions from a sucrose gradient and their relative counts per minute (CPM) for the canonical nucleosome (closed square) and HMGB1-restructured nucleosome (open circle). The arrow marks with M and D represent the position of mono- and dinucleosome in a sucrose gradient when co-sedimented with canonical nucleosomes and HMGB1-restructured nucleosomes. ( B ) EMSA profiles. EMSA bands for the canonical nucleosome (N), fractions 14–19 and HMGB1-restructured nucleosomes (N′/N″), fractions 14–19. EMSA of canonical nucleosome (N) (Lane 1, fraction 17) and HMGB1-restructured nucleosomes (N′/N″), (Lane 2, fraction 17) run on the same gel. ( C ) The effect of anti-histone antibodies (αH2A, αH2B, αH3, αH4) on canonical (N) and HMGB1-restructured nucleosomes (N′/N″). Lane 1: N; Lanes 2–5: N treated with αH2A, αH2B, αH3 and αH4, respectively. Lane 6: N′/N′; Lanes 7–10: N′/N″ treated with αH2A, αH2B, αH3 and αH4, respectively. ( D ) Atomic force microscopy of N and N′/N″. (A) Canonical mononucleosomes (N) on spermidine-treated mica. (B) HMGB1-restructured nucleosomes (N′/N″) seen as mononucleosomes on spermidine-treated mica. DNA tails, where visible, are indicated by arrows. Insets showing enlarged view of distinct mononucleosomes in both (A) and (B). Scale bar = 20 nm.

    Article Snippet: Antibodies for the core histones (H2A, H2B and H3) and the polyclonal HMGB1 antibody were purchased from Millipore, and the antibody for core histone H4 was purchased from Active Motif.

    Techniques: Fractionation, Sedimentation, Microscopy

    In vivo function of chromatin mediated by Asf1 is affected by Asf1 inhibitors. (A) Role of Asf1 isomers in H3K56 acetylation. HeLa cells were treated with siRNAs (200 pmol) targeting Asf1a and Asf1b, either separately or simultaneously, for 24 hr (left panel) and 72 hr (right panel). Depletion of Asf1 and the effect on H3K56 acetylation was determined by immunoblotting assay with whole cell extracts and specific antibodies recognizing Asf1a, Asf1b, and H3K56Ac. (B) Asf1 inhibitors specifically reduced the level of H3K56 acetylation. HeLa cells were treated with each of the Asf1a inhibitors (40 μM) for 24 hr and whole cell lysate was prepared for immunoblotting, and probed with specific antibodies recognizing different histone modification. H3 and actin served as loading controls. (C) HSV-1 yield was decreased by treatment of #2-03 and #2-32. Vero cells treated with DMSO (control) or 80 μM of each compound were infected with HSV-1 and viral yields in the culture supernatants were determined using plaque assay. Error bars represent the standard deviations of three independent experiments. Significance of difference was evaluated (*P < 0.05, **P < 0.005).

    Journal: BMB Reports

    Article Title: Identification of small molecules that inhibit the histone chaperone Asf1 and its chromatin function

    doi: 10.5483/BMBRep.2015.48.12.063

    Figure Lengend Snippet: In vivo function of chromatin mediated by Asf1 is affected by Asf1 inhibitors. (A) Role of Asf1 isomers in H3K56 acetylation. HeLa cells were treated with siRNAs (200 pmol) targeting Asf1a and Asf1b, either separately or simultaneously, for 24 hr (left panel) and 72 hr (right panel). Depletion of Asf1 and the effect on H3K56 acetylation was determined by immunoblotting assay with whole cell extracts and specific antibodies recognizing Asf1a, Asf1b, and H3K56Ac. (B) Asf1 inhibitors specifically reduced the level of H3K56 acetylation. HeLa cells were treated with each of the Asf1a inhibitors (40 μM) for 24 hr and whole cell lysate was prepared for immunoblotting, and probed with specific antibodies recognizing different histone modification. H3 and actin served as loading controls. (C) HSV-1 yield was decreased by treatment of #2-03 and #2-32. Vero cells treated with DMSO (control) or 80 μM of each compound were infected with HSV-1 and viral yields in the culture supernatants were determined using plaque assay. Error bars represent the standard deviations of three independent experiments. Significance of difference was evaluated (*P < 0.05, **P < 0.005).

    Article Snippet: Beads were incubated with 1.25 μg of calf-thymus histone H3 (Roche 11 034 758 001) or 3 μg of HeLa core histones (purified with Active Motif core histone purification kit; 40025), in the presence or absence of Asf1 inhibitor candidates (InterBioScreen Ltd, Russia), for 1 hr at room temperature, with rotation.

    Techniques: In Vivo, Modification, Infection, Plaque Assay

    Overall experimental workflow as illustrated by the identification of H4 (P62805) isoform S1acK8acK12acK20me2 . (a) UV chromatogram from first dimension RPLC separation of 7.5 μg of HeLa core histone mixture. (b) MS-only total ion current (TIC) chromatogram from WCX-HILIC-MS/MS analysis of H4 fraction from the first dimension. (c) Representative mass spectrum (only charge state 13 shown) at retention time 136.54 min from WCX-HILIC-MS/MS analysis of H4 fraction from the first dimension. (d) Representative deconvoluted CID spectrum for precursor ion m / z 877.12 with matching fragments marked with 'triangles'. The inset is the matching fragment mapping on the protein amino acid sequence with PTMs color-coded. CID, collision induced dissociation; PTMS, post-translation modifications; RPLC, reversed phase liquid chromatography; WCX-HILIC-MS/MS, weak cation exchange-hydrophilic interaction liquid chromatography-tandem mass spectrometry.

    Journal: Genome Biology

    Article Title: Enhanced top-down characterization of histone post-translational modifications

    doi: 10.1186/gb-2012-13-10-r86

    Figure Lengend Snippet: Overall experimental workflow as illustrated by the identification of H4 (P62805) isoform S1acK8acK12acK20me2 . (a) UV chromatogram from first dimension RPLC separation of 7.5 μg of HeLa core histone mixture. (b) MS-only total ion current (TIC) chromatogram from WCX-HILIC-MS/MS analysis of H4 fraction from the first dimension. (c) Representative mass spectrum (only charge state 13 shown) at retention time 136.54 min from WCX-HILIC-MS/MS analysis of H4 fraction from the first dimension. (d) Representative deconvoluted CID spectrum for precursor ion m / z 877.12 with matching fragments marked with 'triangles'. The inset is the matching fragment mapping on the protein amino acid sequence with PTMs color-coded. CID, collision induced dissociation; PTMS, post-translation modifications; RPLC, reversed phase liquid chromatography; WCX-HILIC-MS/MS, weak cation exchange-hydrophilic interaction liquid chromatography-tandem mass spectrometry.

    Article Snippet: One-dimensional analyses of HeLa core histones using RPLC or WCX-HILIC under the mass spectrometric conditions above were also carried out for the purpose of comparison with two-dimensional analysis.

    Techniques: Mass Spectrometry, Hydrophilic Interaction Liquid Chromatography, Sequencing, Liquid Chromatography

    Increase of detection dynamic range with 2D separation . Representative mass spectra (charge state 14+) for chromatographic peaks shown in Figure 1. (a) Isoforms of H4 observed from RPLC separation of HeLa core histones; (b to f) isoforms of H4 observed from 2D RP/WCX-HILIC separation of histone H4. Isoforms identified from the most abundant peaks as marked with the dotted lines together with P scores (top, RPLC; bottom: WCX-HILIC) are noted above (b). RPLC, reversed phase liquid chromatography; WCX-HILIC, weak cation exchange-hydrophilic interaction liquid chromatography.

    Journal: Genome Biology

    Article Title: Enhanced top-down characterization of histone post-translational modifications

    doi: 10.1186/gb-2012-13-10-r86

    Figure Lengend Snippet: Increase of detection dynamic range with 2D separation . Representative mass spectra (charge state 14+) for chromatographic peaks shown in Figure 1. (a) Isoforms of H4 observed from RPLC separation of HeLa core histones; (b to f) isoforms of H4 observed from 2D RP/WCX-HILIC separation of histone H4. Isoforms identified from the most abundant peaks as marked with the dotted lines together with P scores (top, RPLC; bottom: WCX-HILIC) are noted above (b). RPLC, reversed phase liquid chromatography; WCX-HILIC, weak cation exchange-hydrophilic interaction liquid chromatography.

    Article Snippet: One-dimensional analyses of HeLa core histones using RPLC or WCX-HILIC under the mass spectrometric conditions above were also carried out for the purpose of comparison with two-dimensional analysis.

    Techniques: Hydrophilic Interaction Liquid Chromatography, Liquid Chromatography

    Inhibition of Asf1a-mediated nucleosome assembly by small molecule inhibitors. DNA supercoiling induced by nucleosome assembly was analyzed in the presence of inhibitors (lane 6-11) at final concentration of 100 μM. GST (lane 4) or GST-Asf1a (lane 5-11), 0.5 μg of each, was added to core histones (0.33 μg, purified from HeLa cells) and relaxed plasmid DNA (0.1 μg), as described in Materials and Methods. Migration of DNA isoforms are indicated. R: relaxed DNA; S: supercoiled DNA.

    Journal: BMB Reports

    Article Title: Identification of small molecules that inhibit the histone chaperone Asf1 and its chromatin function

    doi: 10.5483/BMBRep.2015.48.12.063

    Figure Lengend Snippet: Inhibition of Asf1a-mediated nucleosome assembly by small molecule inhibitors. DNA supercoiling induced by nucleosome assembly was analyzed in the presence of inhibitors (lane 6-11) at final concentration of 100 μM. GST (lane 4) or GST-Asf1a (lane 5-11), 0.5 μg of each, was added to core histones (0.33 μg, purified from HeLa cells) and relaxed plasmid DNA (0.1 μg), as described in Materials and Methods. Migration of DNA isoforms are indicated. R: relaxed DNA; S: supercoiled DNA.

    Article Snippet: Meanwhile, 0.33 μg of HeLa core histones and 0.5 μg of purified GST or GST-hASF1a were incubated for 30 min at 37℃ in nucleosome assembly buffer [10 mM Tris-HCl (pH 7.5), 125 mM NaCl, 2 mM MgCl2 , 0.5 mM DTT.

    Techniques: Inhibition, Concentration Assay, Purification, Plasmid Preparation, Migration