Histone 3 antibody (acetylated, N-Term)

Catalog No. ABIN2668440

This Rabbit Polyclonal antibody specifically detects Histone 3 in WB, ChIP, DB, ChIP-seq and MeDIP. It exhibits reactivity toward Human. It has been mentioned in 11+ publications

Quick Overview for Histone 3 antibody (acetylated, N-Term) (ABIN2668440)

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

Reactivity: Human

Host: Rabbit

Clonality: Polyclonal

Conjugate: This Histone 3 antibody is un-conjugated

Application: Western Blotting (WB), Chromatin Immunoprecipitation (ChIP), Dot Blot (DB), ChIP DNA-Sequencing (ChIP-seq), Methylated DNA Immunoprecipitation (MeDIP)

Product Details anti-Histone 3 Antibody

Binding Specificity: acetylated, N-Term

Purpose: Histone H3ac (pan-acetyl) antibody (pAb)

Purification: Unpurified

Immunogen: This Histone H3 acetyl antibody was raised against a peptide including acetyl-lysines contained in the N-terminal tail of histone H3.

Application Details

Application Notes: ChIP-Seq: 5 µL per ChIP ChIP: 10 µL per ChIP WB*: 1:500 - 1:5,000 dilution *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

Handling

Format: Liquid

Buffer: Rabbit serum containing 30 % glycerol 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 (ABIN2668440)

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).

Xiao, Shi, Fan, Zhang, Wu, Lan, Minze, Fu, Ghobrial, Liu, Li: "GITR subverts Foxp3(+) Tregs to boost Th9 immunity through regulation of histone acetylation." in: Nature communications, Vol. 6, pp. 8266, (2015) (PubMed).

Lehmann, Hoffmann, Koch, Ulrich, Schulz, Niegisch: "Histone deacetylase 8 is deregulated in urothelial cancer but not a target for efficient treatment." in: Journal of experimental & clinical cancer research : CR, Vol. 33, pp. 59, (2014) (PubMed).

Winston, Li, Sarna: "Chronic prenatal stress epigenetically modifies spinal cord BDNF expression to induce sex-specific visceral hypersensitivity in offspring." in: Neurogastroenterology and motility : the official journal of the European Gastrointestinal Motility Society, Vol. 26, Issue 5, pp. 715-30, (2014) (PubMed).

Stilger, Sullivan: "Elongator protein 3 (Elp3) lysine acetyltransferase is a tail-anchored mitochondrial protein in Toxoplasma gondii." in: The Journal of biological chemistry, Vol. 288, Issue 35, pp. 25318-29, (2013) (PubMed).

Saladi, Wong, Trivedi, Marathe, Keenen, Aras, Liew, Setaluri, de la Serna: "BRG1 promotes survival of UV-irradiated melanoma cells by cooperating with MITF to activate the melanoma inhibitor of apoptosis gene." in: Pigment cell & melanoma research, Vol. 26, Issue 3, pp. 377-91, (2013) (PubMed).

Bartholomeeusen, Fujinaga, Xiang, Peterlin: "Histone deacetylase inhibitors (HDACis) that release the positive transcription elongation factor b (P-TEFb) from its inhibitory complex also activate HIV transcription." in: The Journal of biological chemistry, Vol. 288, Issue 20, pp. 14400-7, (2013) (PubMed).

Clifford, John, Brightling, Knox: "Abnormal histone methylation is responsible for increased vascular endothelial growth factor 165a secretion from airway smooth muscle cells in asthma." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 189, Issue 2, pp. 819-31, (2012) (PubMed).

Larsson, Ulfhammer, Magnusson, Bergh, Lunke, El-Osta, Medcalf, Svensson, Karlsson, Jern: "Role of histone acetylation in the stimulatory effect of valproic acid on vascular endothelial tissue-type plasminogen activator expression." in: PLoS ONE, Vol. 7, Issue 2, pp. e31573, (2012) (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).

Siudeja, Srinivasan, Xu, Rana, de Jong, Nollen, Jackowski, Sanford, Hayflick, Sibon: "Impaired Coenzyme A metabolism affects histone and tubulin acetylation in Drosophila and human cell models of pantothenate kinase associated neurodegeneration." in: EMBO molecular medicine, Vol. 3, Issue 12, pp. 755-66, (2011) (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, 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. Lysine N-e-acetylation is a dynamic, reversible and tightly regulated protein and histone modification that plays a major role in chromatin remodeling and in the regulation of gene expression in various cellular functions. Acetylation of histone H3 occurs at several different lysine positions in the histone tail, and is performed by Histone Acetyltransferases (HATs) such as CBP/p300. Acetylation of histones is often associated with transcriptional activation.

Molecular Weight: 17 kDa

Gene ID: 3020

NCBI Accession: NP_003522