gst tagged hdac proteins  (Worthington Biochemical)


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    Name:
    Nuclease Micrococcal
    Description:
    Chromatographically purified to be essentially homogeneous chromatographically and electrophoretically SDS PAGE A lyophilized powder
    Catalog Number:
    ls004796
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    Size:
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    Source:
    Staphylococcus aureus (Strain Foggi)
    Cas Number:
    9013.53.0
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    Structured Review

    Worthington Biochemical gst tagged hdac proteins
    AtTRB2 also interacts with HDA6, a RPD3-type histone deacetylase. ( A ) Western blot analysis showing the different patterns of interaction between AtTRB proteins and various <t>HDAC</t> proteins. PAGE shows the purified HDAC proteins used in this assay (first panel). ( B ) Scheme of various HDA6 truncated proteins fused to <t>GST.</t> HDA6 protein comprises three predicted regions: a conserved HDAC domain in the N-terminal region, a glutamate-rich region in the center of the protein and an aspartate-rich region in the C-terminal region. ( C ) Pull-down assay to map the regions of HDA6 that interact with AtTRB2. PAGE shows the purified HDA6-truncated proteins shown in (B). ( D ) Schematic map indicating the region of HDA6 involved in binding to AtTRB2. ( E ) Western blots demonstrating the interaction between AtTRB2 and HDA6 in vivo . Empty control and IP with IgG were used as negative controls. ( F ) HDA6-associated telomeric repeat signal was detected in an AtTRB2-dependent manner. ( G ) Quantification of multiple independent T-ChIP experiments as shown in (F). T-ChiP analysis was performed and values were calculated as described in the legend to Figure 4 .
    Chromatographically purified to be essentially homogeneous chromatographically and electrophoretically SDS PAGE A lyophilized powder
    https://www.bioz.com/result/gst tagged hdac proteins/product/Worthington Biochemical
    Average 90 stars, based on 87 article reviews
    Price from $9.99 to $1999.99
    gst tagged hdac proteins - by Bioz Stars, 2020-05
    90/100 stars

    Images

    1) Product Images from "Telomere-binding protein regulates the chromosome ends through the interaction with histone deacetylases in Arabidopsis thaliana"

    Article Title: Telomere-binding protein regulates the chromosome ends through the interaction with histone deacetylases in Arabidopsis thaliana

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkw067

    AtTRB2 also interacts with HDA6, a RPD3-type histone deacetylase. ( A ) Western blot analysis showing the different patterns of interaction between AtTRB proteins and various HDAC proteins. PAGE shows the purified HDAC proteins used in this assay (first panel). ( B ) Scheme of various HDA6 truncated proteins fused to GST. HDA6 protein comprises three predicted regions: a conserved HDAC domain in the N-terminal region, a glutamate-rich region in the center of the protein and an aspartate-rich region in the C-terminal region. ( C ) Pull-down assay to map the regions of HDA6 that interact with AtTRB2. PAGE shows the purified HDA6-truncated proteins shown in (B). ( D ) Schematic map indicating the region of HDA6 involved in binding to AtTRB2. ( E ) Western blots demonstrating the interaction between AtTRB2 and HDA6 in vivo . Empty control and IP with IgG were used as negative controls. ( F ) HDA6-associated telomeric repeat signal was detected in an AtTRB2-dependent manner. ( G ) Quantification of multiple independent T-ChIP experiments as shown in (F). T-ChiP analysis was performed and values were calculated as described in the legend to Figure 4 .
    Figure Legend Snippet: AtTRB2 also interacts with HDA6, a RPD3-type histone deacetylase. ( A ) Western blot analysis showing the different patterns of interaction between AtTRB proteins and various HDAC proteins. PAGE shows the purified HDAC proteins used in this assay (first panel). ( B ) Scheme of various HDA6 truncated proteins fused to GST. HDA6 protein comprises three predicted regions: a conserved HDAC domain in the N-terminal region, a glutamate-rich region in the center of the protein and an aspartate-rich region in the C-terminal region. ( C ) Pull-down assay to map the regions of HDA6 that interact with AtTRB2. PAGE shows the purified HDA6-truncated proteins shown in (B). ( D ) Schematic map indicating the region of HDA6 involved in binding to AtTRB2. ( E ) Western blots demonstrating the interaction between AtTRB2 and HDA6 in vivo . Empty control and IP with IgG were used as negative controls. ( F ) HDA6-associated telomeric repeat signal was detected in an AtTRB2-dependent manner. ( G ) Quantification of multiple independent T-ChIP experiments as shown in (F). T-ChiP analysis was performed and values were calculated as described in the legend to Figure 4 .

    Techniques Used: Histone Deacetylase Assay, Western Blot, Polyacrylamide Gel Electrophoresis, Purification, Pull Down Assay, Binding Assay, In Vivo, Chromatin Immunoprecipitation

    Related Articles

    DNA Extraction:

    Article Title: Natural Single-Nucleosome Epi-Polymorphisms in Yeast
    Article Snippet: .. We followed the protocol of Liu et al. for both nucleosomal DNA isolation and ChIP, except that incubation time with micrococcal nuclease (Worthington Biochemical) prior to immunopurification was increased to 30 min at 37°C to obtain mononucleosomes. .. ChIP was performed using 3 µl of anti-H3K14Ac polyclonal antibody (Upstate, 07–353).

    Titration:

    Article Title: Cell Cycle- and Chaperone-Mediated Regulation of H3K56ac Incorporation in Yeast
    Article Snippet: .. 40 units of micrococcal nuclease (Worthington Biochemical) were added, and the spheroplasts were incubated at 37°C for 20 minutes–this was determined in initial titrations to yield > 80% mononucleosomal DNA, but to repeat these results an independent titration should be carried out as a preliminary study. .. The digestion was halted by shifting the reactions to 4°C and adding 0.5 M EDTA to a final concentration of 10 mM.

    Concentration Assay:

    Article Title: Elucidating combinatorial histone modifications and crosstalks by coupling histone-modifying enzyme with biotin ligase activity
    Article Snippet: .. Nuclei were then resuspended in MNase Cutting Buffer containing 3 mM CaCl2 and 2 mM p -chloromercuri-phenylsulfonic acid (pCMPS, Toronto Research Labs; as phosphatase inhibitor), and digested with micrococcal nuclease (MNase, Worthington) at 37°C for 30 min at a concentration of 10U/107 cells. .. Digestion of chromatin by MNase was stopped by addition of EGTA to a final concentration of 5 mM, and equal volume of 2 x Lysis Buffer (30 mM HEPES, pH 7.9, 220 mM KCl, 3 mM MgCl2 , 2 mM EDTA, 0.4% Triton X-100, 20% glycerol) was added to the digested chromatin.

    Incubation:

    Article Title: Cell Cycle- and Chaperone-Mediated Regulation of H3K56ac Incorporation in Yeast
    Article Snippet: .. 40 units of micrococcal nuclease (Worthington Biochemical) were added, and the spheroplasts were incubated at 37°C for 20 minutes–this was determined in initial titrations to yield > 80% mononucleosomal DNA, but to repeat these results an independent titration should be carried out as a preliminary study. .. The digestion was halted by shifting the reactions to 4°C and adding 0.5 M EDTA to a final concentration of 10 mM.

    Article Title: A Key Role for Chd1 in Histone H3 Dynamics at the 3? Ends of Long Genes in Yeast
    Article Snippet: .. 25–40 units (depending on yeast strain and cell density) of micrococcal nuclease (Worthington Biochemical) were added and spheroplasts were incubated at 37°C for 20 minutes. .. The digestion was halted by shifting the reactions to 4°C and adding 0.5 M EDTA to a final concentration of 10 mM.

    Article Title: Natural Single-Nucleosome Epi-Polymorphisms in Yeast
    Article Snippet: .. We followed the protocol of Liu et al. for both nucleosomal DNA isolation and ChIP, except that incubation time with micrococcal nuclease (Worthington Biochemical) prior to immunopurification was increased to 30 min at 37°C to obtain mononucleosomes. .. ChIP was performed using 3 µl of anti-H3K14Ac polyclonal antibody (Upstate, 07–353).

    Article Title: Development and Application of High-Content Biological Screening for Modulators of NET Production
    Article Snippet: .. Neutrophils were pre-incubated at 37°C in 5% CO2 for 30 min prior to stimulation and further incubation at 37°C in 5% CO2 for up to 4 h. Post-incubation samples were treated for 10 min with 1 unit/ml micrococcal nuclease (MNase; Worthington 4789), centrifuged for 10 min at 1,800 rcf and 150 µl of supernatant was transferred to a black 96-well plate (Costar 3915). .. NET-DNA was stained with 1 µM Sytox green® (Invitrogen S7020) and quantified with a fluorometer (Berthold Twinkle2 LB970; ex:485 nm/em:525 nm).

    ChIP-sequencing:

    Article Title: Epigenomic landscapes of retinal rods and cones
    Article Snippet: .. Nucleosomes for native ChIP-seq were prepared by digesting 1–2 million nuclei with 0.025 units/µl micrococcal nuclease (LS004798, Worthington, Lakewood, NJ) at 37°C for 15 min. .. Library preparation and sequencing Libraries for RNA-seq, MethylC-seq, ChIP-seq, and ATAC-seq were prepared as previously described, with slight modifications ( ; ; ; ).

    Chromatin Immunoprecipitation:

    Article Title: Natural Single-Nucleosome Epi-Polymorphisms in Yeast
    Article Snippet: .. We followed the protocol of Liu et al. for both nucleosomal DNA isolation and ChIP, except that incubation time with micrococcal nuclease (Worthington Biochemical) prior to immunopurification was increased to 30 min at 37°C to obtain mononucleosomes. .. ChIP was performed using 3 µl of anti-H3K14Ac polyclonal antibody (Upstate, 07–353).

    Immu-Puri:

    Article Title: Natural Single-Nucleosome Epi-Polymorphisms in Yeast
    Article Snippet: .. We followed the protocol of Liu et al. for both nucleosomal DNA isolation and ChIP, except that incubation time with micrococcal nuclease (Worthington Biochemical) prior to immunopurification was increased to 30 min at 37°C to obtain mononucleosomes. .. ChIP was performed using 3 µl of anti-H3K14Ac polyclonal antibody (Upstate, 07–353).

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    Worthington Biochemical gst tagged hdac proteins
    AtTRB2 also interacts with HDA6, a RPD3-type histone deacetylase. ( A ) Western blot analysis showing the different patterns of interaction between AtTRB proteins and various <t>HDAC</t> proteins. PAGE shows the purified HDAC proteins used in this assay (first panel). ( B ) Scheme of various HDA6 truncated proteins fused to <t>GST.</t> HDA6 protein comprises three predicted regions: a conserved HDAC domain in the N-terminal region, a glutamate-rich region in the center of the protein and an aspartate-rich region in the C-terminal region. ( C ) Pull-down assay to map the regions of HDA6 that interact with AtTRB2. PAGE shows the purified HDA6-truncated proteins shown in (B). ( D ) Schematic map indicating the region of HDA6 involved in binding to AtTRB2. ( E ) Western blots demonstrating the interaction between AtTRB2 and HDA6 in vivo . Empty control and IP with IgG were used as negative controls. ( F ) HDA6-associated telomeric repeat signal was detected in an AtTRB2-dependent manner. ( G ) Quantification of multiple independent T-ChIP experiments as shown in (F). T-ChiP analysis was performed and values were calculated as described in the legend to Figure 4 .
    Gst Tagged Hdac Proteins, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gst tagged hdac proteins/product/Worthington Biochemical
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gst tagged hdac proteins - by Bioz Stars, 2020-05
    90/100 stars
      Buy from Supplier

    Image Search Results


    AtTRB2 also interacts with HDA6, a RPD3-type histone deacetylase. ( A ) Western blot analysis showing the different patterns of interaction between AtTRB proteins and various HDAC proteins. PAGE shows the purified HDAC proteins used in this assay (first panel). ( B ) Scheme of various HDA6 truncated proteins fused to GST. HDA6 protein comprises three predicted regions: a conserved HDAC domain in the N-terminal region, a glutamate-rich region in the center of the protein and an aspartate-rich region in the C-terminal region. ( C ) Pull-down assay to map the regions of HDA6 that interact with AtTRB2. PAGE shows the purified HDA6-truncated proteins shown in (B). ( D ) Schematic map indicating the region of HDA6 involved in binding to AtTRB2. ( E ) Western blots demonstrating the interaction between AtTRB2 and HDA6 in vivo . Empty control and IP with IgG were used as negative controls. ( F ) HDA6-associated telomeric repeat signal was detected in an AtTRB2-dependent manner. ( G ) Quantification of multiple independent T-ChIP experiments as shown in (F). T-ChiP analysis was performed and values were calculated as described in the legend to Figure 4 .

    Journal: Nucleic Acids Research

    Article Title: Telomere-binding protein regulates the chromosome ends through the interaction with histone deacetylases in Arabidopsis thaliana

    doi: 10.1093/nar/gkw067

    Figure Lengend Snippet: AtTRB2 also interacts with HDA6, a RPD3-type histone deacetylase. ( A ) Western blot analysis showing the different patterns of interaction between AtTRB proteins and various HDAC proteins. PAGE shows the purified HDAC proteins used in this assay (first panel). ( B ) Scheme of various HDA6 truncated proteins fused to GST. HDA6 protein comprises three predicted regions: a conserved HDAC domain in the N-terminal region, a glutamate-rich region in the center of the protein and an aspartate-rich region in the C-terminal region. ( C ) Pull-down assay to map the regions of HDA6 that interact with AtTRB2. PAGE shows the purified HDA6-truncated proteins shown in (B). ( D ) Schematic map indicating the region of HDA6 involved in binding to AtTRB2. ( E ) Western blots demonstrating the interaction between AtTRB2 and HDA6 in vivo . Empty control and IP with IgG were used as negative controls. ( F ) HDA6-associated telomeric repeat signal was detected in an AtTRB2-dependent manner. ( G ) Quantification of multiple independent T-ChIP experiments as shown in (F). T-ChiP analysis was performed and values were calculated as described in the legend to Figure 4 .

    Article Snippet: In vitro histone binding assay A total of 1–5 μg of GST and GST-tagged HDAC proteins were incubated with 1–5 μg of calf thymus total histones (Worthington) in binding buffer (50 mM Tris–HCl, pH 7.5, 1M NaCl, 1% NP-40, 0.5 mM EDTA, 1 mM phenylmethyl sulphonyl fluoride (PMSF) with protease inhibitors (Roche)) at 4°C for 3 h, followed by an additional incubation for 1 h with glutathione beads (GE Healthcare), as described previously ( ).

    Techniques: Histone Deacetylase Assay, Western Blot, Polyacrylamide Gel Electrophoresis, Purification, Pull Down Assay, Binding Assay, In Vivo, Chromatin Immunoprecipitation