histones  (ABclonal)

 
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  • 90
    Name:
    Histone H4 Antibody
    Description:
    Polyclonal
    Catalog Number:
    a1131
    Modification:
    Polyclonal
    Price:
    [130.0, 220.0, 380.0]
    Applications:
    IHC,Western Blot
    Host:
    Rabbit
    Size:
    50 ul 100 ul 200 ul
    Category:
    Antibody
    Antibody Type:
    Primary antibody
    Reactivity:
    Human Rat
    Buy from Supplier


    Structured Review

    ABclonal histones
    Polyclonal
    https://www.bioz.com/result/histones/product/ABclonal
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    histones - by Bioz Stars, 2020-09
    90/100 stars

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    other:

    Article Title: HMGB1-TLR4 signaling participates in renal ischemia reperfusion injury and could be attenuated by dexamethasone-mediated inhibition of the ERK/NF-κB pathway
    Article Snippet: Polyclonal rabbit antibodies against ERK (Cell Signal Technology, Danvers, MA, USA, 1:2000), p-ERK (CST, 1:2000), p38 (CST, 1:2000), p-p38 (CST, 1:500), JNK (CST, 1:1000), p-JNK (CST, 1:400), p65 (CST, 1:500), p-p65 (CST, 1:500), Acep65 (Acetyl NF-κB p65 (Acetyl-Lys310), CST, 1:1000), IκΒ-α (Abclonal, 1:1000), p-IκΒ-α (Abclonal, 1:500), HMGB1 (Abcam, 1:1000), TLR-4 (Abcam, 1:500), KIM-1 (Abcam, 1:500), β-actin (Abmart, Shanghai, China, 1:1000), and histones (Abclonal, 1:2000) were used as primary antibodies.

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  • 94
    ABclonal co immunoprecipitation assays anti h2a
    NRP proteins physically interact with <t>H2A</t> and H2A.Z in vivo. a and b α-H2A.Z co-immunopurification assays; α-H2A.Z <t>immunoprecipitation</t> lanes (=H2A.Z IP) show co-purification of H2A.Z with NRP1 ( a ) and NRP2 ( b ). c α-H2A co-immunopurification assays; α-H2A immunoprecipitation lanes (=H2A IP), show co-purification of H2A with NRP1 and NRP2. We show empty beads as a negative control. d NRPs co-immunopurification assays; α-Myc immunoprecipitation lanes (=Myc IP) show co-purification of NRP1 and NRP2 with both unmodified and monoubiquitinated H2A.Z. For each Western blot, the antibody used for detection is indicated either at the bottom, in the case of a and b , or to the right, in the case of c and d . In all cases, protein extracts from the same plants are included to confirm the identity of the co-precipitating band (=Input). We included ARP6 as a positive control. All co-immunopurification assays were repeated with similar results. Source data are provided as a Source Data file.
    Co Immunoprecipitation Assays Anti H2a, supplied by ABclonal, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/co immunoprecipitation assays anti h2a/product/ABclonal
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    co immunoprecipitation assays anti h2a - by Bioz Stars, 2020-09
    94/100 stars
      Buy from Supplier

    92
    ABclonal histone h3
    Metformin decreases H3K27me3 and expression of polycomb repressor complex 2 in ovarian cancer cells. The protein expression of (A) H3K27me3 and (B) EZH2, SUZ12 and EED in A2780, SKOV3 and ES2 cells were assayed by western blot analysis. Met, metformin; Glu, glucose; H3K27me3, <t>histone</t> H3 lysine 27 trimethylated; H3, histone H3; EZH2, histone-lysine N-methyltransferase EZH2; SUZ12, polycomb protein SUZ12; EED, polycomb protein EED.
    Histone H3, supplied by ABclonal, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/histone h3/product/ABclonal
    Average 92 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    histone h3 - by Bioz Stars, 2020-09
    92/100 stars
      Buy from Supplier

    Image Search Results


    NRP proteins physically interact with H2A and H2A.Z in vivo. a and b α-H2A.Z co-immunopurification assays; α-H2A.Z immunoprecipitation lanes (=H2A.Z IP) show co-purification of H2A.Z with NRP1 ( a ) and NRP2 ( b ). c α-H2A co-immunopurification assays; α-H2A immunoprecipitation lanes (=H2A IP), show co-purification of H2A with NRP1 and NRP2. We show empty beads as a negative control. d NRPs co-immunopurification assays; α-Myc immunoprecipitation lanes (=Myc IP) show co-purification of NRP1 and NRP2 with both unmodified and monoubiquitinated H2A.Z. For each Western blot, the antibody used for detection is indicated either at the bottom, in the case of a and b , or to the right, in the case of c and d . In all cases, protein extracts from the same plants are included to confirm the identity of the co-precipitating band (=Input). We included ARP6 as a positive control. All co-immunopurification assays were repeated with similar results. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: NAP1-RELATED PROTEIN1 and 2 negatively regulate H2A.Z abundance in chromatin in Arabidopsis

    doi: 10.1038/s41467-020-16691-x

    Figure Lengend Snippet: NRP proteins physically interact with H2A and H2A.Z in vivo. a and b α-H2A.Z co-immunopurification assays; α-H2A.Z immunoprecipitation lanes (=H2A.Z IP) show co-purification of H2A.Z with NRP1 ( a ) and NRP2 ( b ). c α-H2A co-immunopurification assays; α-H2A immunoprecipitation lanes (=H2A IP), show co-purification of H2A with NRP1 and NRP2. We show empty beads as a negative control. d NRPs co-immunopurification assays; α-Myc immunoprecipitation lanes (=Myc IP) show co-purification of NRP1 and NRP2 with both unmodified and monoubiquitinated H2A.Z. For each Western blot, the antibody used for detection is indicated either at the bottom, in the case of a and b , or to the right, in the case of c and d . In all cases, protein extracts from the same plants are included to confirm the identity of the co-precipitating band (=Input). We included ARP6 as a positive control. All co-immunopurification assays were repeated with similar results. Source data are provided as a Source Data file.

    Article Snippet: Co-immunoprecipitation assays Anti-H2A or anti-H2A.Z polyclonal antibodies were raised in rabbits using the following peptides: SGKGAKGLIMGKPSGSDKDKDKKKPIT-C/AGKGGKGLVAAKTMAANKDKDKDKKKPIS-C for H2A.Z and the peptides C-RGKTLGSGSAKKATTR and C-RGKTLGSGVAKKSTSR for H2A as an antigen (AbClonal, China).

    Techniques: In Vivo, Immu-Puri, Immunoprecipitation, Copurification, Negative Control, Western Blot, Positive Control

    Genome-wide localization of NRP1. a Quantification of 9xMyc-NRP1 binding to FLC and BSU1 occupancy levels in Columbia (WT) and nrp1-1 nrp2-2 double mutant. Error bars represent standard error from three biological replicates. Two-tailed, paired Student’s t test was used to determine p -value. At1g76840 , which has almost no reads in ChIP-Seq analysis, is shown as a control. b Genome-wide distribution of H2A.Z in wild-type (turquoise) and NRP1-9xMyc in wild-type (blue). In both cases, peaks were defined using Narrow Peaks. The magenta line represents differential H2A.Z occupancy between nrp1-1 nrp2-2 and Columbia. c H2A.Z occupancy levels in Columbia (WT) and nrp1-1 nrp2-2 double mutant background plotted over highly significant, likelihood ratio > 1000, NRP1-9xmyc ChIP-Seq peaks. Source data underlying Fig. 4a, b are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: NAP1-RELATED PROTEIN1 and 2 negatively regulate H2A.Z abundance in chromatin in Arabidopsis

    doi: 10.1038/s41467-020-16691-x

    Figure Lengend Snippet: Genome-wide localization of NRP1. a Quantification of 9xMyc-NRP1 binding to FLC and BSU1 occupancy levels in Columbia (WT) and nrp1-1 nrp2-2 double mutant. Error bars represent standard error from three biological replicates. Two-tailed, paired Student’s t test was used to determine p -value. At1g76840 , which has almost no reads in ChIP-Seq analysis, is shown as a control. b Genome-wide distribution of H2A.Z in wild-type (turquoise) and NRP1-9xMyc in wild-type (blue). In both cases, peaks were defined using Narrow Peaks. The magenta line represents differential H2A.Z occupancy between nrp1-1 nrp2-2 and Columbia. c H2A.Z occupancy levels in Columbia (WT) and nrp1-1 nrp2-2 double mutant background plotted over highly significant, likelihood ratio > 1000, NRP1-9xmyc ChIP-Seq peaks. Source data underlying Fig. 4a, b are provided as a Source Data file.

    Article Snippet: Co-immunoprecipitation assays Anti-H2A or anti-H2A.Z polyclonal antibodies were raised in rabbits using the following peptides: SGKGAKGLIMGKPSGSDKDKDKKKPIT-C/AGKGGKGLVAAKTMAANKDKDKDKKKPIS-C for H2A.Z and the peptides C-RGKTLGSGSAKKATTR and C-RGKTLGSGVAKKSTSR for H2A as an antigen (AbClonal, China).

    Techniques: Genome Wide, Binding Assay, Mutagenesis, Two Tailed Test, Chromatin Immunoprecipitation

    nrp1-1 nrp2-2 double mutants display overaccumulation of H2A.Z. a Boxplot of log2 ratio of H2AZ/Input in Columbia and nrp1-1 nrp2-2 over H2A.Z peaks defined in Columbia. *** indicates p -value of

    Journal: Nature Communications

    Article Title: NAP1-RELATED PROTEIN1 and 2 negatively regulate H2A.Z abundance in chromatin in Arabidopsis

    doi: 10.1038/s41467-020-16691-x

    Figure Lengend Snippet: nrp1-1 nrp2-2 double mutants display overaccumulation of H2A.Z. a Boxplot of log2 ratio of H2AZ/Input in Columbia and nrp1-1 nrp2-2 over H2A.Z peaks defined in Columbia. *** indicates p -value of

    Article Snippet: Co-immunoprecipitation assays Anti-H2A or anti-H2A.Z polyclonal antibodies were raised in rabbits using the following peptides: SGKGAKGLIMGKPSGSDKDKDKKKPIT-C/AGKGGKGLVAAKTMAANKDKDKDKKKPIS-C for H2A.Z and the peptides C-RGKTLGSGSAKKATTR and C-RGKTLGSGVAKKSTSR for H2A as an antigen (AbClonal, China).

    Techniques:

    Metformin decreases H3K27me3 and expression of polycomb repressor complex 2 in ovarian cancer cells. The protein expression of (A) H3K27me3 and (B) EZH2, SUZ12 and EED in A2780, SKOV3 and ES2 cells were assayed by western blot analysis. Met, metformin; Glu, glucose; H3K27me3, histone H3 lysine 27 trimethylated; H3, histone H3; EZH2, histone-lysine N-methyltransferase EZH2; SUZ12, polycomb protein SUZ12; EED, polycomb protein EED.

    Journal: International Journal of Oncology

    Article Title: Metformin inhibits ovarian cancer via decreasing H3K27 trimethylation

    doi: 10.3892/ijo.2018.4343

    Figure Lengend Snippet: Metformin decreases H3K27me3 and expression of polycomb repressor complex 2 in ovarian cancer cells. The protein expression of (A) H3K27me3 and (B) EZH2, SUZ12 and EED in A2780, SKOV3 and ES2 cells were assayed by western blot analysis. Met, metformin; Glu, glucose; H3K27me3, histone H3 lysine 27 trimethylated; H3, histone H3; EZH2, histone-lysine N-methyltransferase EZH2; SUZ12, polycomb protein SUZ12; EED, polycomb protein EED.

    Article Snippet: Histone H3 (cat. no. 2348), H3K27me3 (cat. no. 2363), EED (cat. no. 5371) antibodies were purchased from ABclonal Biotech Co., Ltd. (Woburn, MA, USA). β-actin antibody (cat. no. 66009-1-Ig) was purchased from Proteintech, Inc. (Chicago, IL, USA).

    Techniques: Expressing, Western Blot

    Metformin inhibits H3K27me3 through the AMPK pathway. (A) Metformin activates AMPK of ovarian cancer cells in normoglycemic condition. (B) 2-DG activates AMPK and suppresses H3K27me3, PRC2 of ovarian cancer cells in normoglycemic condition. (C) Compound C inhibits the effect of metformin on PRC2 and H3K27me3 when ovarian cancer cells were cultured in normoglycemic condition. The protein expression of p-AMPKα, AMPKα, H3K27me3, EZH2, SUZ12 and EED in A2780, SKOV3 and ES2 cells were assayed by western blot analysis. The expression was normalized to β-actin. Met, metformin; Glu, glucose; p-AMPKα, phospho-AMPKα; AMPKα, AMP-activated protein kinase; 2-DG, 2-deoxy-D-glucose; EZH2, histone-lysine N-methyltransferase EZH2;SUZ12, polycomb protein SUZ12; EED, polycomb protein EED; 2-DG, dorsomorphin 2HCl; H3K27me3, histone H3 lysine 27 trimethylation.

    Journal: International Journal of Oncology

    Article Title: Metformin inhibits ovarian cancer via decreasing H3K27 trimethylation

    doi: 10.3892/ijo.2018.4343

    Figure Lengend Snippet: Metformin inhibits H3K27me3 through the AMPK pathway. (A) Metformin activates AMPK of ovarian cancer cells in normoglycemic condition. (B) 2-DG activates AMPK and suppresses H3K27me3, PRC2 of ovarian cancer cells in normoglycemic condition. (C) Compound C inhibits the effect of metformin on PRC2 and H3K27me3 when ovarian cancer cells were cultured in normoglycemic condition. The protein expression of p-AMPKα, AMPKα, H3K27me3, EZH2, SUZ12 and EED in A2780, SKOV3 and ES2 cells were assayed by western blot analysis. The expression was normalized to β-actin. Met, metformin; Glu, glucose; p-AMPKα, phospho-AMPKα; AMPKα, AMP-activated protein kinase; 2-DG, 2-deoxy-D-glucose; EZH2, histone-lysine N-methyltransferase EZH2;SUZ12, polycomb protein SUZ12; EED, polycomb protein EED; 2-DG, dorsomorphin 2HCl; H3K27me3, histone H3 lysine 27 trimethylation.

    Article Snippet: Histone H3 (cat. no. 2348), H3K27me3 (cat. no. 2363), EED (cat. no. 5371) antibodies were purchased from ABclonal Biotech Co., Ltd. (Woburn, MA, USA). β-actin antibody (cat. no. 66009-1-Ig) was purchased from Proteintech, Inc. (Chicago, IL, USA).

    Techniques: Cell Culture, Expressing, Western Blot