(CPP-CARM1) on the Cloned Mouse Embryonic Development
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Anti-H3r2me2(Asym) Antibody
FOR RESEARCH USE ONLY! 01/20 Anti-H3R2me2(asym) Antibody CATALOG NO.: A2025-100 (100 µl) BACKGROUND DESCRIPTION: Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a replication-dependent histone that is a member of the histone H3 family. Transcripts from this gene lack poly A tails; instead, they contain a palindromic termination element. This gene is located separately from the other H3 genes that are in the histone gene cluster on chromosome 6p22-p21.3. H3.4; H3/g; H3FT; H3t; HIST3H3; Histone H3; HIST1H3A ALTERNATE NAMES: ANTIBODY TYPE: Polyclonal HOST/ISOTYPE: Rabbit / IgG IMMUNOGEN: A synthetic methylated peptide targeting residues around Arginine 2 of human Histone H3 MOLECULAR WEIGHT: 17 kDa PURIFICATION: Affinity purified FORM: Liquid FORMULATION: In PBS with 0.02% sodium azide, 50% glycerol, pH 7.3 SPECIES REACTIVITY: Human, Mouse, Rat STORAGE CONDITIONS: Store at -20ºC. Avoid freeze / thaw cycles APPLICATIONS AND USAGE: WB 1:500 - 1:2000, IHC 1:50 - 1:200, IF 1:50 - 1:200 Note: This information is only intended as a guide. The optimal dilutions must be determined by the user Western blot analysis of H3R2me2(asym) expression in Dot-blot analysis of methylation peptides using Anti- HeLa cells and H3 protein. -
Searching for Inhibitors of the Protein Arginine Methyl Transferases: Synthesis and Characterisation of Peptidomimetic Ligands
SEARCHING FOR INHIBITORS OF THE PROTEIN ARGININE METHYL TRANSFERASES: SYNTHESIS AND CHARACTERISATION OF PEPTIDOMIMETIC LIGANDS by ASTRID KNUHTSEN B. Sc., Aarhus University, 2009 M. Sc., Aarhus University, 2012 A DISSERTATION SUBMITTED IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY in THE FACULTY OF GRADUATE AND POSTDOCTORAL STUDIES (Pharmaceutical Sciences) THE UNIVERSITY OF BRITISH COLUMBIA (Vancouver) March 2016 © Astrid Knuhtsen, 2016 UNIVERSITY OF COPENH AGEN FACULTY OF HEALTH A ND MEDICAL SCIENCES PhD Thesis Astrid Knuhtsen Searching for Inhibitors of the Protein Arginine Methyl Transferases: Synthesis and Characterisation of Peptidomimetic Ligands December 2015 This thesis has been submitted to the Graduate School of The Faculty of Health and Medical Sciences, University of Copenhagen ii Thesis submission: 18th of December 2015 PhD defense: 11th of March 2016 Astrid Knuhtsen Department of Drug Design and Pharmacology Faculty of Health and Medical Sciences University of Copenhagen Universitetsparken 2 DK-2100 Copenhagen Denmark and Faculty of Pharmaceutical Sciences University of British Columbia 2405 Wesbrook Mall BC V6T 1Z3, Vancouver Canada Supervisors: Principal Supervisor: Associate Professor Jesper Langgaard Kristensen Department of Drug Design and Pharmacology, University of Copenhagen, Denmark Co-Supervisor: Associate Professor Daniel Sejer Pedersen Department of Drug Design and Pharmacology, University of Copenhagen, Denmark Co-Supervisor: Assistant Professor Adam Frankel Faculty of Pharmaceutical -
[Dimethyl Arg17] Antibody NBP2-59162
Product Datasheet Histone H3 [Dimethyl Arg17] Antibody NBP2-59162 Unit Size: 100 ul Store at -20C. Avoid freeze-thaw cycles. Protocols, Publications, Related Products, Reviews, Research Tools and Images at: www.novusbio.com/NBP2-59162 Updated 5/13/2021 v.20.1 Earn rewards for product reviews and publications. Submit a publication at www.novusbio.com/publications Submit a review at www.novusbio.com/reviews/destination/NBP2-59162 Page 1 of 3 v.20.1 Updated 5/13/2021 NBP2-59162 Histone H3 [Dimethyl Arg17] Antibody Product Information Unit Size 100 ul Concentration Please see the vial label for concentration. If unlisted please contact technical services. Storage Store at -20C. Avoid freeze-thaw cycles. Clonality Polyclonal Preservative 0.05% Sodium Azide Isotype IgG Purity Whole Antiserum Buffer Serum Target Molecular Weight 15 kDa Product Description Host Rabbit Gene ID 126961 Gene Symbol H3C14 Species Human Immunogen The exact sequence of the immunogen to this Histone H3 [Dimethyl Arg17] antibody is proprietary. Product Application Details Applications Western Blot, Chromatin Immunoprecipitation, Dot Blot, ELISA Recommended Dilutions Western Blot 1:250, Chromatin Immunoprecipitation 10 - 15 uL/IP, ELISA 1:1000 - 1:3000, Dot Blot 1:20000 Page 2 of 3 v.20.1 Updated 5/13/2021 Images Western Blot: Histone H3 [Dimethyl Arg17] Antibody [NBP2-59162] - Histone extracts of HeLa cells (15 ug) were analysed by Western blot using the antibody against H3R17me2(asym) diluted 1:250 in TBS- Tween containing 5% skimmed milk. Observed molecular weight is ~17 kDa. Chromatin Immunoprecipitation: Histone H3 [Dimethyl Arg17] Antibody [NBP2-59162] - ChIP assays were performed using human osteosarcoma (U2OS) cells, the antibody against H3R17me2(asym) and optimized PCR primer sets for qPCR. -
Asymmetric Expression of Lincget Biases Cell Fate in Two-Cell Mouse Embryos
UC Riverside UC Riverside Previously Published Works Title Asymmetric Expression of LincGET Biases Cell Fate in Two-Cell Mouse Embryos. Permalink https://escholarship.org/uc/item/3100h0cm Journal Cell, 175(7) ISSN 0092-8674 Authors Wang, Jiaqiang Wang, Leyun Feng, Guihai et al. Publication Date 2018-12-01 DOI 10.1016/j.cell.2018.11.039 Peer reviewed eScholarship.org Powered by the California Digital Library University of California Article Asymmetric Expression of LincGET Biases Cell Fate in Two-Cell Mouse Embryos Graphical Abstract Authors Jiaqiang Wang, Leyun Wang, Guihai Feng, ..., Zhonghua Liu, Wei Li, Qi Zhou Correspondence [email protected] (W.L.), [email protected] (Q.Z.) In Brief An endogenous retrovirus-associated nuclear long noncoding RNA biases cell fate in mouse two-cell embryos. Highlights Data Resources d LincGET is asymmetrically expressed in the nucleus of two- GSE110419 to four-cell mouse embryos d LincGET overexpression biases blastomere fate toward inner cell mass (ICM) d LincGET physically binds to CARM1 d LincGET/CARM1 activates ICM-specific genes Wang et al., 2018, Cell 175, 1887–1901 December 13, 2018 ª 2018 Elsevier Inc. https://doi.org/10.1016/j.cell.2018.11.039 Article Asymmetric Expression of LincGET Biases Cell Fate in Two-Cell Mouse Embryos Jiaqiang Wang,1,2,3,4,8 Leyun Wang,1,8 Guihai Feng,1,8 Yukai Wang,1,8 Yufei Li,1,2 Xin Li,5,6 Chao Liu,1,2 Guanyi Jiao,1,2 Cheng Huang,1,2 Junchao Shi,7 Tong Zhou,7 Qi Chen,7 Zhonghua Liu,4 Wei Li,1,2,3,* and Qi Zhou1,2,3,9,* 1State Key Laboratory of Stem Cell and Reproductive -
Arsenite Exposure Inhibits Histone Acetyltransferase P300 For
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`:^!PGUUFZ! 2EHFIV!RG!DGPEDGD!IBG!G[MJFCHG!PJ@PG@IH?IEJ@!?@D!IEKG!JQ!FJDECK!?HFG@EIG! ?PPJHDE@T!IJ!IBG!G[MHGFFEJ@!JQ!&HQ7Z!9G!FI?HIGD!JCH!G[MJFCHG!G[MGHEKG@IF!REIB!IRJ! IEKG!MJE@IF!]a!?@D!7b!B^!?@D!QJCH!PJ@PG@IH?IEJ@F!]4V!7V!cV!?@D!W4!d<^Z!"QIGH!a!B! IHG?IKG@IV!IBG!?KJC@I!JQ!&HQ7!FBJRGD!DJFG:GQQGPI!HGU?IEJ@FBEMF!REIB!IBG! PJ@PG@IH?IEJ@F!JQ!FJDECK!?HFG@EIG!E@!=JIB!PGUU!UE@GF!?@D!IBGHG!RGHG!FET@EQEP?@I! DEQQGHG@PG!=GIRGG@!7!d<!?@D!c!d<!THJCMFZ!(BG!?KJC@I!JQ!&HQ7!?QIGH!7b!B!G[MJFCHG! ?UFJ!FBJRGD!DJFG:GQQGPI!HGU?IEJ@FBEMF!REIB!IBG!PJ@PG@IH?IEJ@F!JQ!FJDECK!?HFG@EIGZ! -JRGOGHV!PJKM?HGD!REIB!a!B!THJCMFV!7b!B!THJCMF!FBJRGD!DEQQGHG@I!M?IIGH@!JQ!&HQ7! ii G[MHGFFEJ@!=GIRGG@!IRJ!PGUU!UE@GFV!RBEPB!KETBI!=G!P?CFGD!=>!;JIW1!U?PNE@TZ! -
Establishment and Optimization of the Chrop Approach, Combining Chip and MS-Based Proteomics
PhD degree in Molecular Medicine European School of Molecular Medicine (SEMM), University of Milan and University of Naples “Federico II” Faculty of Medicine Settore disciplinare: BIO/10 Establishment and optimization of the ChroP approach, combining ChIP and MS-based proteomics, for the characterization of the chromatome at distinct functional domains Monica Soldi IFOM-IEO Campus, Milan Matricola n. R08407 Supervisor: Dr. Tiziana Bonaldi IFOM-IEO Campus, Milan Added co-Supervisor: Dr. Gioacchino Natoli IFOM-IEO Campus, Milan Anno accademico 2011-2012 To my family: Andrea and Paolo! 1 TABLE OF CONTENT FIGURE AND TABLE INDEX ....................................................................................... 5 LIST OF ABBREVIATIONS ....................................................................................... 8 1. ABSTRACT .............................................................................................................. 10 2. INTRODUCTION .................................................................................................... 13 2.1. Chromatin, epigenetics and histone post-translational modifications ............... 13 2.2. Mass Spectrometry analysis and MS-based proteomics ...................................... 17 2.2.1. Basic concepts of Mass Spectrometry........................................................... 19 2.2.2. Different MS approaches for hPTMs analysis: from “Bottom Up” to “Top Down”, via “Middle Down” .................................................................................. 25 -
Stepwise Histone Modifications Are Mediated by Multiple Enzymes That
ARTICLE Received 4 Apr 2013 | Accepted 29 Oct 2013 | Published 26 Nov 2013 DOI: 10.1038/ncomms3841 Stepwise histone modifications are mediated by multiple enzymes that rapidly associate with nascent DNA during replication Svetlana Petruk1, Kathryn L. Black1, Sina K. Kovermann2, Hugh W. Brock2 & Alexander Mazo1 The mechanism of epigenetic inheritance following DNA replication may involve dissociation of chromosomal proteins from parental DNA and reassembly on daughter strands in a specific order. Here we investigated the behaviour of different types of chromosomal proteins using newly developed methods that allow assessment of the assembly of proteins during DNA replication. Unexpectedly, most chromatin-modifying proteins tested, including methylases, demethylases, acetyltransferases and a deacetylase, are found in close proximity to PCNA or associate with short nascent DNA. Histone modifications occur in a temporal order following DNA replication, mediated by complex activities of different enzymes. In contrast, components of several major nucleosome-remodelling complexes are dissociated from parental DNA, and are later recruited to nascent DNA following replication. Epigenetic inheritance of gene expression patterns may require many aspects of chromatin structure to remain in close proximity to the replication complex followed by reassembly on nascent DNA shortly after replication. 1 Department of Biochemistry and Molecular Biology and Kimmel Cancer Center, Thomas Jefferson University, 1020 Locust Street, Philadelphia, Pennsylvania 19107, USA. 2 Department of Zoology, University of British Columbia, 6270 University Boulevard, Vancouver, British Columbia, Canada V6T 1Z4. Correspondence and requests for materials should be addressed to A.M. (email: [email protected]). NATURE COMMUNICATIONS | 4:2841 | DOI: 10.1038/ncomms3841 | www.nature.com/naturecommunications 1 & 2013 Macmillan Publishers Limited. -
Crosstalk Between Histone Modifications Indicates That
9348–9360 Nucleic Acids Research, 2017, Vol. 45, No. 16 Published online 20 June 2017 doi: 10.1093/nar/gkx550 Crosstalk between histone modifications indicates that inhibition of arginine methyltransferase CARM1 activity reverses HIV latency Zheng Zhang1,†, Bryan C. Nikolai1,†, Leah A. Gates1, Sung Yun Jung2, Edward B. Siwak3, Bin He1,4, Andrew P. Rice3, Bert W. O’Malley1 and Qin Feng1,* 1Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA, 2Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA, 3Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX, USA and 4Department of Medicine-Hematology & Oncology, Baylor College of Medicine, Houston, TX, USA Received February 06, 2017; Revised May 25, 2017; Editorial Decision June 13, 2017; Accepted June 15, 2017 ABSTRACT INTRODUCTION In eukaryotic cells, the gene expression status Human immunodeficiency virus (HIV) is a retrovirus that is strictly controlled by epigenetic modifications causes acquired immunodeficiency syndrome. HIV infec- on chromatin. The repressive status of chromatin tion of CD4+ helper T lymphocytes is a multistep process, largely contributes to HIV latency. Studies have involving fusion and entry through interaction with CD4 re- shown that modification of histone H3K27 acts as ceptor and CCR5 co-receptor, reverse transcription of HIV viral RNA into double-stranded viral DNA, and integra- a key molecular switch for activation or suppression tion of viral DNA into -
H3r17me2(Asym)K18ac Polyclonal Antibody
H3R17me2(asym)K18ac polyclonal antibody Cat. No. C15410171 Specificity: Human, mouse, wide range expected Type: Polyclonal Purity: Affinity purified polyclonal antibody in PBS containing ChIP-grade / ChIP-seq-grade 0.05% azide and 0.05% ProClin 300. Source: Rabbit Storage: Store at -20°C; for long storage, store at -80°C. Lot #: A1922-001P Avoid multiple freeze-thaw cycles. Size: 50 µg/ 53 µl Precautions: This product is for research use only. Not for use in diagnostic or therapeutic procedures. Concentration: 0.94 µg/µl Description: Polyclonal antibody raised in rabbit against the region of histone H3 containing the asymmetrically dimethylated R17 and the acetylated lysine 18 (H3R17me2(asym)K18ac), using a KLH-conjugated synthetic peptide. Applications Suggested dilution Results ChIP* 1 µg per IP Fig 1, 2 ELISA 1:1,000 Fig 3 Dot blotting 1:20,000 Fig 4 Western blotting 1:1,000 Fig 5 IF 1:500 Fig 6 * Please note that the optimal antibody amount per ChIP should be determined by the end-user. We recommend testing 1-5 µg per IP. Target description Histones are the main constituents of the protein part of chromosomes of eukaryotic cells. They are rich in the amino acids arginine and lysine and have been greatly conserved during evolution. Histones pack the DNA into tight masses of chromatin. Two core histones of each class H2A, H2B, H3 and H4 assemble and are wrapped by 146 base pairs of DNA to form one octameric nucleosome. Histone tails undergo numerous post-translational modifications, which either directly or indirectly alter chromatin structure to facilitate transcriptional activation or repression or other nuclear processes. -
The Role of the Arginine Methyltransferase CARM1 in Global Transcriptional Regulation
Western University Scholarship@Western Electronic Thesis and Dissertation Repository 4-23-2014 12:00 AM The role of the arginine methyltransferase CARM1 in global transcriptional regulation. Niamh Coughlan The University of Western Ontario Supervisor Dr. Joseph Torchia The University of Western Ontario Graduate Program in Biochemistry A thesis submitted in partial fulfillment of the equirr ements for the degree in Doctor of Philosophy © Niamh Coughlan 2014 Follow this and additional works at: https://ir.lib.uwo.ca/etd Part of the Biochemistry Commons Recommended Citation Coughlan, Niamh, "The role of the arginine methyltransferase CARM1 in global transcriptional regulation." (2014). Electronic Thesis and Dissertation Repository. 2013. https://ir.lib.uwo.ca/etd/2013 This Dissertation/Thesis is brought to you for free and open access by Scholarship@Western. It has been accepted for inclusion in Electronic Thesis and Dissertation Repository by an authorized administrator of Scholarship@Western. For more information, please contact [email protected]. THE ROLE OF THE ARGININE METHYLTRANSFERASE CARM1 IN GLOBAL TRANSCRIPTIONAL REGULATION (Thesis format: Integrated Article) by Niamh Coughlan Graduate Program in Biochemistry A thesis submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy The School of Graduate and Postdoctoral Studies The University of Western Ontario London, Ontario, Canada © Niamh Coughlan 2014 Abstract Arginine methylation is a prevalent post-translational modification that is found on many nuclear and cytoplasmic proteins, and has been implicated in the regulation of gene expression. CARM1 is a member of the protein arginine methyltransferase (PRMT) family of proteins, and is a key protein responsible for arginine methylation of a subset of proteins involved in transcription. -
Anti-H3r8me2(Asym) Antibody
FOR RESEARCH USE ONLY! 01/20 Anti-H3R8me2(asym) Antibody CATALOG NO.: A2047-100 (100 µl) BACKGROUND DESCRIPTION: Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a replication-dependent histone that is a member of the histone H3 family. Transcripts from this gene lack poly A tails; instead, they contain a palindromic termination element. This gene is located separately from the other H3 genes that are in the histone gene cluster on chromosome 6p22-p21.3. H3.4; H3/g; H3FT; H3t; HIST3H3; Histone H3; HIST1H3A ALTERNATE NAMES: ANTIBODY TYPE: Polyclonal HOST/ISOTYPE: Rabbit / IgG IMMUNOGEN: A synthetic methylated peptide targeting residues around Arginine 8 of human histone H3 MOLECULAR WEIGHT: 18 kDa PURIFICATION: Affinity purified FORM: Liquid FORMULATION: In PBS with 0.02% sodium azide, 50% glycerol, pH7.3 SPECIES REACTIVITY: Human, Mouse, Rat STORAGE CONDITIONS: Store at -20ºC. Avoid freeze / thaw cycles APPLICATIONS AND USAGE: WB 1:500 - 1:2000, IF 1:50 - 1:200 Note: This information is only intended as a guide. The optimal dilutions must be determined by the user Western blot analysis of H3R8me2(asym) expression in Dot-blot analysis of methylation peptides using Anti- HeLa cells and H3 protein. -
The Role of BCL-3 Feedback Loops in Regulating NF-Κb Signalling
The role of BCL-3 feedback loops in regulating NF-κB signalling A thesis submitted to the University of Manchester for the degree of Doctor of Philosophy in the Faculty of Engineering and Physical Sciences 2012 Thomas Walker School of Chemical Engineering and Analytical Sciences Integrative Systems Biology Contents Contents……………………………………………………………………………….... 1 Word count………………………………………………………………………………. 9 List of figures……………………………………………………………………………. 9 List of tables…………………………………………………………………………….. 11 Abbreviations………………………………………………………………………........ 11 Abstract………………………………………………………………………………...... 15 Declaration & Copyright Statement…………………………………………..…...... 16 Acknowledgements……………………………………………………………..……… 17 Chapter 1 Introduction……………………………………………………………………..……….. 18 1.1. The inflammatory response…………………………………………………………...……………. 18 1.1.1. PAMPs: initial indicators of infection…………………………………………………………….. 18 1.1.2. The inflammatory response………………………………………………………………………. 19 1.1.3. Cytokines…………………………………………………………………………………………… 19 1.1.3.1. The TNF family of cytokines…………………………………………………………..... 20 1.1.3.2. The TNFR family………………………………………………………………………… 20 1.1.3.3. Diverse cell types produce and are responsive to TNF α……………………………. 21 1.1.4. Fibroblasts as inflammation mediators……………………………………………………………. 21 1.2. NF-κB transcription factors………………………………………………………………………… 22 1.2.1. NF-κB subunits and dimer combinations……………………………………………………..... 22 1.2.2. Canonical NF-κB signalling………………………………………………………………………. 23 1.2.3. p50 homodimers………………………………………………………………………………….