Histone 3 anticorps (H3K9me3)

N° du produit ABIN2668470

Cet anticorps Lapin Polyclonal détecte spécifiquement Histone 3 dans WB, IHC, IF, ChIP, ICC, DB, ChIP-seq et CUT&Tag. Il présente une réactivité avec des échantillons de Humain et Schizosaccharomyces pombe. Il a été cité dans 33+ publications.

Aperçu rapide pour Histone 3 anticorps (H3K9me3) (ABIN2668470)

Antigène: Histone 3 (H3) (Histone H3 (H3))

Reactivité: Humain, Schizosaccharomyces pombe

Hôte: Lapin

Clonalité: Polyclonal

Conjugué: Cet anticorp Histone 3 est non-conjugé

Application: Western Blotting (WB), Immunohistochemistry (IHC), Immunofluorescence (IF), Chromatin Immunoprecipitation (ChIP), Immunocytochemistry (ICC), Dot Blot (DB), ChIP DNA-Sequencing (ChIP-seq), Cleavage Under Targets and Tagmentation (CUT&Tag)

Détail du produit anti-Histone 3 anticorps

Épitope: H3K9me3

Fonction: Histone H3K9me3 antibody (pAb)

Purification: Unpurified

Immunogène: This Histone H3 trimethyl Lys9 antibody was raised against a peptide including trimethyl-lysine 9 of histone H3.

Information d'application

Indications d'application: ChIP: 2 - 10 µL per ChIP ChIP-Seq: 10 µL each ICC/IF: 1:500 - 1:1,000 dilution WB*: 1:1,000 - 1:5,000 dilution CUT&Tag: 1 µL per 50 µL reaction *This antibody has been validated for CUT&Tag using Active Motif's CUT&Tag-IT Assay Kit, Catalog No. 53160. *Note: many chromatin-bound proteins are not soluble in a low salt nuclear extract and fractionate to the pellet. Therefore, we recommend a High Salt / Sonication Protocol when preparing nuclear extracts for Western blot.

Restrictions: For Research Use only

Stockage

Format: Liquid

Buffer: Rabbit serum containing 30 % glycerol and 0.035 % sodium azide.

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 by aliquoting items into single-use fractions,Keep all reagents on ice when not in storage

Stock: -20 °C

Stockage commentaire: Some products may be shipped at room temperature. This will not affect their stability or performance. Avoid repeated freeze/thaw cycles by aliquoting items into single-use fractions for storage at -20°C for up to 2 years. Keep all reagents on ice when not in storage.

Date de péremption: 24 months

Références pour anticorps anti-Histone 3 (ABIN2668470)

Egan, Yuan, Craske, Labhart, Guler, Arnott, Maile, Busby, Henry, Kelly, Tindell, Jhunjhunwala, Zhao, Hatton, Bryant, Classon, Trojer: "An Alternative Approach to ChIP-Seq Normalization Enables Detection of Genome-Wide Changes in Histone H3 Lysine 27 Trimethylation upon EZH2 Inhibition." dans: PLoS ONE, Vol. 11, Issue 11, pp. e0166438, (2016) (PubMed).

Thompson, Dulberg, Moon, Foster, Chen, Karimi, Lorincz: "hnRNP K coordinates transcriptional silencing by SETDB1 in embryonic stem cells." dans: PLoS genetics, Vol. 11, Issue 1, pp. e1004933, (2015) (PubMed).

Postberg, Kanders, Forcob, Willems, Orth, Hensel, Weil, Wirth, Jenke: "CpG signalling, H2A.Z/H3 acetylation and microRNA-mediated deferred self-attenuation orchestrate foetal NOS3 expression." dans: Clinical epigenetics, Vol. 7, Issue 1, pp. 9, (2015) (PubMed).

Cabrera, Olcese, Horabin: "A balancing act: heterochromatin protein 1a and the Polycomb group coordinate their levels to silence chromatin in Drosophila." dans: Epigenetics & chromatin, Vol. 8, pp. 17, (2015) (PubMed).

Soyer, Möller, Schotanus, Connolly, Galazka, Freitag, Stukenbrock: "Chromatin analyses of Zymoseptoria tritici: Methods for chromatin immunoprecipitation followed by high-throughput sequencing (ChIP-seq)." dans: Fungal genetics and biology : FG & B, Vol. 79, pp. 63-70, (2015) (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).

Soyer, El Ghalid, Glaser, Ollivier, Linglin, Grandaubert, Balesdent, Connolly, Freitag, Rouxel, Fudal: "Epigenetic control of effector gene expression in the plant pathogenic fungus Leptosphaeria maculans." dans: PLoS genetics, Vol. 10, Issue 3, pp. e1004227, (2014) (PubMed).

Minkovsky, Sahakyan, Rankin-Gee, Bonora, Patel, Plath: "The Mbd1-Atf7ip-Setdb1 pathway contributes to the maintenance of X chromosome inactivation." dans: Epigenetics & chromatin, Vol. 7, pp. 12, (2014) (PubMed).

Rangasamy: "Distinctive patterns of epigenetic marks are associated with promoter regions of mouse LINE-1 and LTR retrotransposons." dans: Mobile DNA, Vol. 4, Issue 1, pp. 27, (2013) (PubMed).

Maksakova, Thompson, Goyal, Jones, Singh, Karimi, Lorincz: "Distinct roles of KAP1, HP1 and G9a/GLP in silencing of the two-cell-specific retrotransposon MERVL in mouse ES cells." dans: Epigenetics & chromatin, Vol. 6, Issue 1, pp. 15, (2013) (PubMed).

Thijssen, Tobi, Balog, Schouten, Kremer, El Bouazzaoui, Henneman, Putter, Eline Slagboom, Heijmans, van der Maarel: "Chromatin remodeling of human subtelomeres and TERRA promoters upon cellular senescence: commonalities and differences between chromosomes." dans: Epigenetics, Vol. 8, Issue 5, pp. 512-21, (2013) (PubMed).

Karimi-Aghcheh, Bok, Phatale, Smith, Baker, Lichius, Omann, Zeilinger, Seiboth, Rhee, Keller, Freitag, Kubicek: "Functional analyses of Trichoderma reesei LAE1 reveal conserved and contrasting roles of this regulator." dans: G3 (Bethesda, Md.), Vol. 3, Issue 2, pp. 369-78, (2013) (PubMed).

Connolly, Smith, Freitag: "The Fusarium graminearum histone H3 K27 methyltransferase KMT6 regulates development and expression of secondary metabolite gene clusters." dans: PLoS genetics, Vol. 9, Issue 10, pp. e1003916, (2013) (PubMed).

Murata, Narita, Sugimoto, Kawashima, Kanda, Tsurumi: "Contribution of myocyte enhancer factor 2 family transcription factors to BZLF1 expression in Epstein-Barr virus reactivation from latency." dans: Journal of virology, Vol. 87, Issue 18, pp. 10148-62, (2013) (PubMed).

Wiemann, Sieber, von Bargen, Studt, Niehaus, Espino, Huß, Michielse, Albermann, Wagner, Bergner, Connolly, Fischer, Reuter, Kleigrewe, Bald, Wingfield, Ophir, Freeman, Hippler, Smith, Brown, Proctor et al.: "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen Fusarium fujikuroi reveal complex regulation of secondary metabolism and novel metabolites. ..." dans: PLoS pathogens, Vol. 9, Issue 6, pp. e1003475, (2013) (PubMed).

Jamieson, Rountree, Lewis, Stajich, Selker: "Regional control of histone H3 lysine 27 methylation in Neurospora." dans: Proceedings of the National Academy of Sciences of the United States of America, Vol. 110, Issue 15, pp. 6027-32, (2013) (PubMed).

Murphy, Cipriany, Wallin, Ju, Szeto, Hagarman, Benitez, Craighead, Soloway: "Single-molecule analysis of combinatorial epigenomic states in normal and tumor cells." dans: Proceedings of the National Academy of Sciences of the United States of America, Vol. 110, Issue 19, pp. 7772-7, (2013) (PubMed).

Woellmer, Arteaga-Salas, Hammerschmidt: "BZLF1 governs CpG-methylated chromatin of Epstein-Barr Virus reversing epigenetic repression." dans: PLoS pathogens, Vol. 8, Issue 9, pp. e1002902, (2012) (PubMed).

Seiboth, Karimi, Phatale, Linke, Hartl, Sauer, Smith, Baker, Freitag, Kubicek: "The putative protein methyltransferase LAE1 controls cellulase gene expression in Trichoderma reesei." dans: Molecular microbiology, Vol. 84, Issue 6, pp. 1150-64, (2012) (PubMed).

Duncan, Barwick, Jin, Rago, Kapoor-Vazirani, Powell, Chi, Bigner, Vertino, Yan: "A heterozygous IDH1R132H/WT mutation induces genome-wide alterations in DNA methylation." dans: Genome research, Vol. 22, Issue 12, pp. 2339-55, (2012) (PubMed).

Détails sur Histone 3

Antigène: Histone 3 (H3) (Histone H3 (H3))

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. The methylation of histones can occur on two different residues: arginine or lysine. Histone methylation can be associated with transcriptional activation or repression, depending on the methylated residue. Lysine 9 of histone H3 can be mono-, di- or trimethylated by different histone methyltransferases (HMTs) such as SuvH39H1 or G9a. This methylated lysine can be demethylated by histone demethylases as JMJD1A, LSD1 or JMJD2C. Methylation of this residue is mainly associated with transcriptional repression.

Poids moléculaire: 17 kDa

ID gène: 3020

NCBI Accession: NP_003522