Histone 3 anticorps (H3K27me3)

N° du produit ABIN2668416

Cet anticorps Lapin Polyclonal détecte spécifiquement Histone 3 dans WB, IHC, IF, ChIP, ICC, DB, ChIP-seq, CUT&Tag et CUT&RUN. Il présente une réactivité avec des échantillons de Humain, Souris et Singe. Il a été cité dans 39+ publications.

Aperçu rapide pour Histone 3 anticorps (H3K27me3) (ABIN2668416)

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

Reactivité: Humain, Souris, Singe

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), Cleavage Under Targets and Release Using Nuclease (CUT&RUN)

Détail du produit anti-Histone 3 anticorps

Épitope: H3K27me3

Fonction: Histone H3K27me3 antibody (pAb)

Purification: Protein A Chromatography

Immunogène: This antibody was raised against a peptide including trimethyl-lysine 27 of histone H3.

Isotype: IgG

Information d'application

Indications d'application: ChIP: 5 - 10 μg per ChIP ChIP-Seq: 5 μg each ICC/IF: 2 μg/mL dilution IHC(FFPE): 2 μg/mL dilution WB*: 0.5 - 2 μg/mL dilution CUT&Tag: 1 μg per 50 µL reaction* CUT&RUN: 1 μg 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 WB. For H3K27me3, we also offer AbFlex H3K27me3 Recombinant Antibody (rAb). For details, see Catalog No. 91167.

Restrictions: For Research Use only

Stockage

Concentration: 1 μg/μL

Buffer: Purified IgG in PBS ( pH 7.5) with 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 (ABIN2668416)

Su, Wang, Lee, Stephens, Papazyan, Voronina, Krautkramer, Raman, Thorpe, Boersma, Kuznetsov, Miller, Taverna, Phillips, Denu: "Reader domain specificity and lysine demethylase-4 family function." dans: Nature communications, Vol. 7, pp. 13387, (2016) (PubMed).

Matsuda, Kobayashi-Ishihara, Fujikawa, Ishida, Watanabe, Yamagishi: "Epigenetic heterogeneity in HIV-1 latency establishment." dans: Scientific reports, Vol. 5, pp. 7701, (2015) (PubMed).

Lay, Liu, Kelly, Witt, Farnham, Jones, Berman: "The role of DNA methylation in directing the functional organization of the cancer epigenome." dans: Genome research, Vol. 25, Issue 4, pp. 467-77, (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).

Harr, Luperchio, Wong, Cohen, Wheelan, Reddy: "Directed targeting of chromatin to the nuclear lamina is mediated by chromatin state and A-type lamins." dans: The Journal of cell biology, Vol. 208, Issue 1, pp. 33-52, (2015) (PubMed).

She, Baroux: "Chromatin dynamics in pollen mother cells underpin a common scenario at the somatic-to-reproductive fate transition of both the male and female lineages in Arabidopsis." dans: Frontiers in plant science, Vol. 6, pp. 294, (2015) (PubMed).

Sakamoto, Akiyama, Shimada, Zhu, Yuasa, Tanaka: "DNA Methylation in the Exon 1 Region and Complex Regulation of Twist1 Expression in Gastric Cancer Cells." dans: PLoS ONE, Vol. 10, Issue 12, pp. e0145630, (2015) (PubMed).

Sakashita, Kawabata, Jincho, Tajima, Kumamoto, Kobayashi, Matsui, Kono: "Sex Specification and Heterogeneity of Primordial Germ Cells in Mice." dans: PLoS ONE, Vol. 10, Issue 12, pp. e0144836, (2015) (PubMed).

Piper, Barry, Harvey, McLeay, Smith, Harris, Mason, Stringer, Day, Wray, Gronostajski, Bailey, Boyd, Richards: "NFIB-mediated repression of the epigenetic factor Ezh2 regulates cortical development." dans: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 34, Issue 8, pp. 2921-30, (2014) (PubMed).

Taberlay, Statham, Kelly, Clark, Jones: "Reconfiguration of nucleosome-depleted regions at distal regulatory elements accompanies DNA methylation of enhancers and insulators in cancer." dans: Genome research, Vol. 24, Issue 9, pp. 1421-32, (2014) (PubMed).

Ohno, Kanayama, Moore, Ray, Negishi: "The roles of co-chaperone CCRP/DNAJC7 in Cyp2b10 gene activation and steatosis development in mouse livers." dans: PLoS ONE, Vol. 9, Issue 12, pp. e115663, (2014) (PubMed).

Bowman, Deaton, Domingues, Wang, Sadreyev, Kingston, Bender: "H3K27 modifications define segmental regulatory domains in the Drosophila bithorax complex." dans: eLife, Vol. 3, pp. e02833, (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).

Looney, Zhang, Chen, Lee, Chari, Mao, Pelizzola, Zhang, Lister, Baker, Fernandes, Gaetz, Foshay, Clift, Zhang, Li, Vallender, Wagner, Qin, Michelini, Bugarija, Park, Aryee, Stricker, Zhou, White, Ren et al.: "Systematic mapping of occluded genes by cell fusion reveals prevalence and stability of cis-mediated silencing in somatic cells. ..." dans: Genome research, Vol. 24, Issue 2, pp. 267-80, (2014) (PubMed).

Le Dily, Baù, Pohl, Vicent, Serra, Soronellas, Castellano, Wright, Ballare, Filion, Marti-Renom, Beato: "Distinct structural transitions of chromatin topological domains correlate with coordinated hormone-induced gene regulation." dans: Genes & development, Vol. 28, Issue 19, pp. 2151-62, (2014) (PubMed).

Lee, Wagner, Xiao, Kim, Feng, Lazar, Moore: "Nutrient-sensing nuclear receptors coordinate autophagy." dans: Nature, Vol. 516, Issue 7529, pp. 112-5, (2014) (PubMed).

Papazyan, Voronina, Chapman, Luperchio, Gilbert, Meier, Mackintosh, Shabanowitz, Tackett, Reddy, Coyne, Hunt, Liu, Taverna: "Methylation of histone H3K23 blocks DNA damage in pericentric heterochromatin during meiosis." dans: eLife, Vol. 3, pp. e02996, (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).

Kuwahara, Suzuki, Tofukuji, Yamada, Kanoh, Matsumoto, Maruyama, Kometani, Kurosaki, Ohara, Nakayama, Yamashita: "The Menin-Bach2 axis is critical for regulating CD4 T-cell senescence and cytokine homeostasis." dans: Nature communications, Vol. 5, pp. 3555, (2014) (PubMed).

Hu, Garruss, Gao, Morgan, Cook, Smith, Shilatifard: "The Mll2 branch of the COMPASS family regulates bivalent promoters in mouse embryonic stem cells." dans: Nature structural & molecular biology, Vol. 20, Issue 9, pp. 1093-7, (2013) (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, it 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, they play a major role in regulating gene expression.Histone H3K27 can be mono-, di- or trimethylated by different histone methyltransferases, such as EZH2 or NSD3. While histone methylation can be associated with transcriptional activation or repression, methylation of Lysine 27 of histone H3 is mainly associated with transcriptional repression.

Poids moléculaire: 17 kDa

ID gène: 3020

NCBI Accession: NP_003522