Symmetric-Di-Methyl-Histone H3 (Arg8) Rabbit

Symmetric -Di-methyl-Histone H3 (Arg8) rabbit pAb ( H3R8me2(sy) pAb) www.ptm-biolab.com.cn Cat#: PTM-672 [email protected] Species: Rabbit 0571-2883 3567 Size: 100 μl Form: supplied in liquid form Recommend Species Swissprot Molecular Application Immunogen dilution Reactivity ID Weight H3R8me2(sy) WB, Dot, ELISA 1:2000 for WB H, M, R, Mk P68431 17 KDa -KLH **Species reactivity is determined by WB. Kept at -20oC after reconstituted. *** Anti-rabbit secondary antibodies must be used to detect this antibody. Source/Purification: This product is produced by immunizing rabbits with a synthetic di-methyl(sy) peptide corresponding to residues surrounding Arg8 of human histone H3. Antibodies are purified by protein A-conjugated agarose followed by di-methylated(sy) histone H3 (Arg8) peptide affinity chromatography. Recommended Applications: ELISA, Dot blot, Western blot. Recommended antibody dilution: WB: 1:2000 NOTE: For WB, incubate membrane with diluted antibody in 5% nonfat milk, 1 x TBS, 0.1% Tween- 20 for two hours at room temperature with gentle shaking. Prepare working dilution immediately before use. Use at an assay dependent concentration. Optimal dilutions/concentrations should be determined by the end user. Not yet tested in other applications Scientific Description: Proteins post-translational Modification (PTM) is an important reversible event controlling protein activity. The amino-terminal tails of core histones undergo multiple modifications in multiple sites, termed as “histone code” or “epigenetic code”. Lysine methylation or arginine methylation in core histones is a major determinant for the formation of active and inactive regions of the genome and therefore plays vital roles in multiple cellular events. In most species, arginine methylation occurs primarily on histones H3 (Arg2, 8, 17, 26) and H4 (Arg8) and has been implicated in both transcriptional activation and silencing. Arginine methylation in histones is carried out by the arginine N-methyltransferase (PRMT), which catalyzes the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine. Arginine methylation in histones is impaired in the pathologies of cancer and other diseases and therefore, enzymes regulating histone arginine methylation have become promising targets for anti-cancer drugs. For research purposes only. Not intended to be used for therapeutic or diagnostic purposes in humans or animals. This product may not be resold or modified for resale without the prior written approval of PTM BIO, LLC. A No. Peptide No. Peptide lane 1 H3R8me2(sy) lane 2 H3R2me1 lane 3 H3R2me2(sy) lane 4 H3R2me2(asy) lane 5 H3R8me2(asy) lane 6 H3K9me2 lane 7 H3R8un Figure A: Dot blotting analysis on indicated amount of peptides using histone H3R8me2(sy) rabbit pAb. The list of peptides is included in the table on the right. B Figure B: Western blotting analysis on 30 μg of crude proteins from HeLa, C2C12, COS-7 whole cell lysates and 200 ng recombinant histone H3 proteins using symmetric di-methyl-histone H3 (Arg8) rabbit pAb (1:2000). Storage & Stability: The antibody is kept in PBS with 50% glycerol and 0.01% sodium azide. Upon receipt, please centrifuge the antibody at 12,000 x g for 20 seconds and store the antibody at -20°C. Avoid repeated freeze/thaw cycles. Stable for 12 months from date of receipt. Leave the antibody at room temperature for 2 minutes and gently mixed using pipette before usage. 12,000 x g Pipet up and down Cut the pipette tip 20 seconds multiple times Schematic diagram for reconstitution instructions Application Key: WB-western ChIP-chromatin immunoprecipitation IP-immunoprecipitation Modification Key: me-methyl sy-symmetric asy-asymmetric cr-crotonyl hib-2ohibutyryl bhb-3ohbutyryl Species Cross-Reactivity Key: H-human M-mouse R-rat Mk-monkey All-all species expected .

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Four Enzymes Cooperate to Displace Histone H1 During the First Minute of Hormonal Gene Activation
Downloaded from genesdev.cshlp.org on September 26, 2021 - Published by Cold Spring Harbor Laboratory Press Four enzymes cooperate to displace histone H1 during the first minute of hormonal gene activation Guillermo Pablo Vicent,1,2 A. Silvina Nacht,1 Jofre Font-Mateu, Giancarlo Castellano, Laura Gaveglia, Cecilia Ballare´, and Miguel Beato Centre de Regulacio´ Geno` mica (CRG), Universitat Pompeu Fabra (UPF), E-08003 Barcelona, Spain Gene regulation by external signals requires access of transcription factors to DNA sequences of target genes, which is limited by the compaction of DNA in chromatin. Although we have gained insight into how core histones and their modifications influence this process, the role of linker histones remains unclear. Here we show that, within the first minute of progesterone action, a complex cooperation between different enzymes acting on chromatin mediates histone H1 displacement as a requisite for gene induction and cell proliferation. First, activated progesterone receptor (PR) recruits the chromatin remodeling complexes NURF and ASCOM (ASC-2 [activating signal cointegrator-2] complex) to hormone target genes. The trimethylation of histone H3 at Lys 4 by the MLL2/MLL3 subunits of ASCOM, enhanced by the hormone-induced displacement of the H3K4 demethylase KDM5B, stabilizes NURF binding. NURF facilitates the PR-mediated recruitment of Cdk2/CyclinA, which is required for histone H1 displacement. Cooperation of ATP-dependent remodeling, histone methylation, and kinase activation, followed by H1 displacement, is a prerequisite for the subsequent displacement of histone H2A/H2B catalyzed by PCAF and BAF. Chromatin immunoprecipitation (ChIP) and sequencing (ChIP-seq) and expression arrays show that H1 displacement is required for hormone induction of most hormone target genes, some of which are involved in cell proliferation.
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