Histone 3 anticorps (N-Term)

N° du produit ABIN2668390

Il existe 9+ publications pour ce produit. L’anticorps anti-Histone 3 Monoclonal Souris est utilisé pour la détection de Histone 3 dans des échantillons de Humain. Il a été validé pour IF, ChIP, ICC et ChIP-seq.

Aperçu rapide pour Histone 3 anticorps (N-Term) (ABIN2668390)

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

Reactivité: Humain

Hôte: Souris

Clonalité: Monoclonal

Conjugué: Cet anticorp Histone 3 est non-conjugé

Application: Immunofluorescence (IF), Chromatin Immunoprecipitation (ChIP), Immunocytochemistry (ICC), ChIP DNA-Sequencing (ChIP-seq)

Clone: MABI 0301

Détail du produit anti-Histone 3 anticorps

Épitope: N-Term

Fonction: Histone H3 antibody (mAb) (Clone MABI 0301)

Purification: Protein G Chromatography

Immunogène: This Histone H3 antibody (mAb) was raised against a peptide containing the N-terminus of histone H3.

Isotype: IgG2b

Information d'application

Indications d'application: ChIP-Seq: 4 μg per ChIP ChIP: 5 - 10 μg per ChIP ICC/IF: 1 μg/mL dilution For Histone H3, we also offer AbFlex Histone H3 Recombinant Antibody (rAb). For details, see Catalog No. 91297.

Restrictions: For Research Use only

Stockage

Concentration: 0.54 μg/μL

Buffer: PBS pH 7.5 containing 30 % glycerol. 0.3M NaCl, 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 (ABIN2668390)

Bulusu, Tumanov, Michalopoulou, van den Broek, MacKay, Nixon, Dhayade, Schug, Vande Voorde, Blyth, Gottlieb, Vazquez, Kamphorst: "Acetate Recapturing by Nuclear Acetyl-CoA Synthetase 2 Prevents Loss of Histone Acetylation during Oxygen and Serum Limitation." dans: Cell reports, Vol. 18, Issue 3, pp. 647-658, (2017) (PubMed).

Pacaud, Cheray, Nadaradjane, Vallette, Cartron: "Histone H3 phosphorylation in GBM: a new rational to guide the use of kinase inhibitors in anti-GBM therapy." dans: Theranostics, Vol. 5, Issue 1, pp. 12-22, (2015) (PubMed).

Wagner, Ciszewski, Kania: "L- and D-lactate enhance DNA repair and modulate the resistance of cervical carcinoma cells to anticancer drugs via histone deacetylase inhibition and hydroxycarboxylic acid receptor 1 activation." dans: Cell communication and signaling : CCS, Vol. 13, pp. 36, (2015) (PubMed).

Zhan, Kost-Alimova, Shi, Leo, Bardenhagen, Shepard, Appikonda, Vangamudi, Zhao, Tieu, Jiang, Heffernan, Marszalek, Toniatti, Draetta, Tyler, Barton, Jones, Palmer, Geck Do, Andersen: "Development of novel cellular histone-binding and chromatin-displacement assays for bromodomain drug discovery." dans: Epigenetics & chromatin, Vol. 8, pp. 37, (2015) (PubMed).

Fukuda, Mitani, Miyashita, Umezawa, Akutsu: "Chromatin condensation of Xist genomic loci during oogenesis in mice." dans: Development (Cambridge, England), Vol. 142, Issue 23, pp. 4049-55, (2015) (PubMed).

van de Werken, van der Heijden, Eleveld, Teeuwssen, Albert, Baarends, Laven, Peters, Baart: "Paternal heterochromatin formation in human embryos is H3K9/HP1 directed and primed by sperm-derived histone modifications." dans: Nature communications, Vol. 5, pp. 5868, (2014) (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).

Ohmori, Takai, Ishijima, Suzuki, Moriguchi, Philipsen, Yamamoto, Ohneda: "Regulation of GATA factor expression is distinct between erythroid and mast cell lineages." dans: Molecular and cellular biology, Vol. 32, Issue 23, pp. 4742-55, (2012) (PubMed).

Cerf, Tian, Craighead: "Ordered arrays of native chromatin molecules for high-resolution imaging and analysis." dans: ACS nano, Vol. 6, Issue 9, pp. 7928-34, (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. Each histone contains two domains. First, a main globular domain (C-terminal) forming the core of the nucleosome is involved in histone-histone interactions and in binding to the DNA. Secondly, an N-terminal tail is subject to post-translational modifications. 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.

Poids moléculaire: 17 kDa

ID gène: 3020

NCBI Accession: NP_003522