Histone 3 antibody (N-Term)

Catalog No. ABIN2668390

There are 9+ publications for this product available. The Mouse Monoclonal anti-Histone 3 antibody is suitable to detect Histone 3 in samples from Human. It has been validated for IF, ChIP, ICC and ChIP-seq.

Quick Overview for Histone 3 antibody (N-Term) (ABIN2668390)

Target: Histone 3 (H3) (Histone H3 (H3))

Reactivity: Human

Host: Mouse

Clonality: Monoclonal

Conjugate: This Histone 3 antibody is un-conjugated

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

Clone: MABI 0301

Product Details anti-Histone 3 Antibody

Binding Specificity: N-Term

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

Purification: Protein G Chromatography

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

Isotype: IgG2b

Application Details

Application Notes: 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

Handling

Concentration: 0.54 μg/μL

Buffer: PBS pH 7.5 containing 30 % glycerol. 0.3M NaCl, and 0.035 % sodium azide.

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Handling Advice: Avoid repeated freeze/thaw cycles by aliquoting items into single-use fractions,Keep all reagents on ice when not in storage

Storage: -20 °C

Storage Comment: 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.

Expiry Date: 24 months

References for anti-Histone 3 antibody (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." in: 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." in: 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." in: 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." in: Epigenetics & chromatin, Vol. 8, pp. 37, (2015) (PubMed).

Fukuda, Mitani, Miyashita, Umezawa, Akutsu: "Chromatin condensation of Xist genomic loci during oogenesis in mice." in: 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." in: 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." in: 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." in: 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." in: ACS nano, Vol. 6, Issue 9, pp. 7928-34, (2012) (PubMed).

Target Details for Histone 3

Target: Histone 3 (H3) (Histone H3 (H3))

Alternative Name: Histone H3

Background: 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.

Molecular Weight: 17 kDa

Gene ID: 3020

NCBI Accession: NP_003522