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Histone 3 (H3) (H3K4me3) anticorps Primary Antibody

H3 Reactivité: Humain, Souris, Saccharomyces cerevisiae ChIP-seq, ChIP, CUT&RUN, DB, ICC, IF, WB Hôte: Lapin Polyclonal
Pubmed (74)
N° du produit ABIN2668472
$530.83
Plus frais de port $45.00 et $22.00 pour carboglace
100 μL
local_shipping Destination: Etats-Unis
Envoi sous 1 à 2 jours ouvrables
  • Antigène
    Épitope
    H3K4me3
    Reactivité
    Humain, Souris, Saccharomyces cerevisiae
    Hôte
    Lapin
    Clonalité
    Polyclonal
    Conjugué
    Inconjugué
    Application
    ChIP DNA-Sequencing (ChIP-seq), Chromatin Immunoprecipitation (ChIP), Cleavage Under Targets and Release Using Nuclease (CUT&RUN), Dot Blot (DB), Immunocytochemistry (ICC), Immunofluorescence (IF), Western Blotting (WB)
    Purification
    None
    Immunogène
    This Histone H3 trimethylLys4 antibody was raised against a peptide including trimethyllysine 4 of histone H3.
  • Indications d'application
    Optimal working dilution should be determined by the investigator.
    Restrictions
    For Research Use only
  • Format
    Liquid
    Agent conservateur
    Sodium azide
    Précaution d'utilisation
    This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
    Conseil sur la manipulation

    Avoid repeated freeze/thaw cycles and keep on ice when not in storage.

    Stock
    -20 °C
    Stockage commentaire
    Antibodies in solution can be stored at -20 °C for 2 years.
    Date de péremption
    6 months
  • Brahma, Henikoff: "RSC-Associated Subnucleosomes Define MNase-Sensitive Promoters in Yeast." dans: Molecular cell, Vol. 73, Issue 2, pp. 238-249.e3, 2019 (PubMed).

    Pan, Guan, Liu, Li, Wang, Wu, Zhou, Zhang, Ren, Zhang, Li, Yang, Hao, Yuan, Yuan, Wang, Ju, Mao, Li, Qu, Tang, Liu: "SIRT6 safeguards human mesenchymal stem cells from oxidative stress by coactivating NRF2." dans: Cell research, Vol. 26, Issue 2, pp. 190-205, 2016 (PubMed).

    Toth, Papp, Brulois, Choi, Gao, Jung: "LANA-Mediated Recruitment of Host Polycomb Repressive Complexes onto the KSHV Genome during De Novo Infection." dans: PLoS pathogens, Vol. 12, Issue 9, pp. e1005878, 2016 (PubMed).

    Lowe, Gemma, Rakyan, Holland: "Sexually dimorphic gene expression emerges with embryonic genome activation and is dynamic throughout development." dans: BMC genomics, Vol. 16, pp. 295, 2015 (PubMed).

    Weirich, Kudithipudi, Kycia, Jeltsch: "Somatic cancer mutations in the MLL3-SET domain alter the catalytic properties of the enzyme." dans: Clinical epigenetics, Vol. 7, Issue 1, pp. 36, 2015 (PubMed).

    Valdez, Li, Murray, Ji, Liu, Popat, Champlin, Andersson: "Comparison of the cytotoxicity of cladribine and clofarabine when combined with fludarabine and busulfan in AML cells: Enhancement of cytotoxicity with epigenetic modulators." dans: Experimental hematology, Vol. 43, Issue 6, pp. 448-61.e2, 2015 (PubMed).

    Brown, Esterhazy, Sarde, London, Pullabhatla, Osma-Garcia, Al-Bader, Ortiz, Elgueta, Arno, de Rinaldis, Mucida, Lord, Noelle: "Retinoic acid is essential for Th1 cell lineage stability and prevents transition to a Th17 cell program." dans: Immunity, Vol. 42, Issue 3, pp. 499-511, 2015 (PubMed).

    Sabò, Kress, Pelizzola, de Pretis, Gorski, Tesi, Morelli, Bora, Doni, Verrecchia, Tonelli, Fagà, Bianchi, Ronchi, Low, Müller, Guccione, Campaner, Amati: "Selective transcriptional regulation by Myc in cellular growth control and lymphomagenesis." dans: Nature, Vol. 511, Issue 7510, pp. 488-92, 2014 (PubMed).

    Fereres, Simón, Mohd-Sarip, Verrijzer, Busturia: "dRYBP counteracts chromatin-dependent activation and repression of transcription." dans: PLoS ONE, Vol. 9, Issue 11, pp. e113255, 2014 (PubMed).

    Putiri, Tiedemann, Liu, Choi, Robertson: "Impact of human MLL/COMPASS and polycomb complexes on the DNA methylome." dans: Oncotarget, Vol. 5, Issue 15, pp. 6338-52, 2014 (PubMed).

    Dhimolea, Wadia, Murray, Settles, Treitman, Sonnenschein, Shioda, Soto: "Prenatal exposure to BPA alters the epigenome of the rat mammary gland and increases the propensity to neoplastic development." dans: PLoS ONE, Vol. 9, Issue 7, pp. e99800, 2014 (PubMed).

    Konsavage, Yochum: "The myc 3' wnt-responsive element suppresses colonic tumorigenesis." dans: Molecular and cellular biology, Vol. 34, Issue 9, pp. 1659-69, 2014 (PubMed).

    Asmar, Hother, Kulosman, Treppendahl, Nielsen, Ralfkiaer, Pedersen, Møller, Ralfkiaer, de Nully Brown, Grønbæk: "Diffuse large B-cell lymphoma with combined TP53 mutation and MIR34A methylation: Another "double hit" lymphoma with very poor outcome?" dans: Oncotarget, Vol. 5, Issue 7, pp. 1912-25, 2014 (PubMed).

    DAnselmi, Masiello, Cucina, Proietti, Dinicola, Pasqualato, Ricci, Dobrowolny, Catizone, Palombo, Bizzarri: "Microenvironment promotes tumor cell reprogramming in human breast cancer cell lines." dans: PLoS ONE, Vol. 8, Issue 12, pp. e83770, 2014 (PubMed).

    Kelso, Baumgart, Eickhoff, Albert, Antrecht, Lemcke, Klebl, Meisterernst: "Cyclin-dependent kinase 7 controls mRNA synthesis by affecting stability of preinitiation complexes, leading to altered gene expression, cell cycle progression, and survival of tumor cells." dans: Molecular and cellular biology, Vol. 34, Issue 19, pp. 3675-88, 2014 (PubMed).

    Belyea, Xu, Pentz, Medrano, Li, Hu, Turner, Legallo, Jones, Tario, Liang, Gross, Sequeira-Lopez, Gomez: "Identification of renin progenitors in the mouse bone marrow that give rise to B-cell leukaemia." dans: Nature communications, Vol. 5, pp. 3273, 2014 (PubMed).

    Amatori, Ballarini, Faversani, Belloni, Fusar, Bosari, Pelicci, Minucci, Fanelli: "PAT-ChIP coupled with laser microdissection allows the study of chromatin in selected cell populations from paraffin-embedded patient samples." dans: Epigenetics & chromatin, Vol. 7, pp. 18, 2014 (PubMed).

    Kumar, Duester: "Retinoic acid controls body axis extension by directly repressing Fgf8 transcription." dans: Development (Cambridge, England), Vol. 141, Issue 15, pp. 2972-7, 2014 (PubMed).

    Rafehi, Balcerczyk, Lunke, Kaspi, Ziemann, Kn, Okabe, Khurana, Ooi, Khan, Du, Chang, Haviv, Keating, Karagiannis, El-Osta: "Vascular histone deacetylation by pharmacological HDAC inhibition." dans: Genome research, Vol. 24, Issue 8, pp. 1271-84, 2014 (PubMed).

    Feng, Zhang, Shea, Creighton, Coarfa, Hilsenbeck, Lanz, He, Wang, Fu, Nardone, Song, Bradner, Mitsiades, Mitsiades, Osborne, Schiff, OMalley: "An epigenomic approach to therapy for tamoxifen-resistant breast cancer." dans: Cell research, Vol. 24, Issue 7, pp. 809-19, 2014 (PubMed).

  • Antigène
    Autre désignation
    Histone H3
    Sujet
    Histone H3 is one of the core components of the nucleosome. The nucleosome is the smallest subunit of chromatin and consists of 147 base pairs of DNA wrapped around an octamer of core histone proteins (two each of Histone H2A, Histone H2B, Histone H3 and Histone H4). Histone H1 is a linker histone, present at the interface between the nucleosome core and DNA entry/exit points. Histone H1 is responsible for establishing higher-order chromatin structure. Chromatin is subject to a variety of chemical modifications, including post-translational modifications of the histone proteins and the methylation of cytosine residues in the DNA. Reported histone modifications include acetylation, methylation, phosphorylation, ubiquitylation, glycosylation, ADP-ribosylation, carbonylation and SUMOylation, these modifications play a major role in regulating gene expression. Histone methylation can be associated with transcriptional activation or repression, depending on the methylated residue. Lysine 4 of histone H3 can be mono-, di- or trimethylated by different histone methyltransferases (HMTs) such as SET1 or ASH1. Methylation of Lys4 is often associated with transcriptional activation. The demethylase LSD1 is able to demethylate histone H3 Lys4.
    Poids moléculaire
    17 kDa
    ID gène
    3020
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