Histone H4 antibody (acetylated)

Catalog No. ABIN2668867

There are 8+ publications for this product available. The Rabbit Polyclonal anti-Histone H4 antibody is suitable to detect Histone H4 in samples from Human and Mouse. It has been validated for WB, IF, ICC, ChIP and DB.

Quick Overview for Histone H4 antibody (acetylated) (ABIN2668867)

Target: Histone H4 (HISTH4)

Reactivity: Human, Mouse

Host: Rabbit

Clonality: Polyclonal

Conjugate: This Histone H4 antibody is un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF), Immunocytochemistry (ICC), Chromatin Immunoprecipitation (ChIP), Dot Blot (DB)

Product Details anti-Histone H4 Antibody

Binding Specificity: acetylated

Purpose: Histone H4ac (pan-acetyl) antibody (pAb)

Purification: Unpurified

Immunogen: This Histone H4 pan-acetyl antibody was raised against a peptide containing the amino terminal region of Tetrahymena histone H2A acetylated at multiple lysines. (The immunogen has a high degree of homology to mammalian histone H4, so the antibody recognizes acetylated histone H4 in HeLa extracts).

Application Details

Application Notes: ChIP: 5 - 10 µL per ChIP ICC/IF: 1:500 - 1:2,000 dilution WB: 1:1,000 - 1:10,000 dilution

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 H4 antibody (ABIN2668867)

Kungulovski, Nunna, Thomas, Zanger, Reinhardt, Jeltsch: "Targeted epigenome editing of an endogenous locus with chromatin modifiers is not stably maintained." in: Epigenetics & chromatin, Vol. 8, pp. 12, (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).

Li, Wu, Kim, Zhao, Hearn, Zhang, Meistrich, Mills: "Chd5 orchestrates chromatin remodelling during sperm development." in: Nature communications, Vol. 5, pp. 3812, (2014) (PubMed).

Walker, LaFerla, Oddo, Brewer: "Reversible epigenetic histone modifications and Bdnf expression in neurons with aging and from a mouse model of Alzheimer's disease." in: Age (Dordrecht, Netherlands), Vol. 35, Issue 3, pp. 519-31, (2013) (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).

Fazzio, Panning: "Condensin complexes regulate mitotic progression and interphase chromatin structure in embryonic stem cells." in: The Journal of cell biology, Vol. 188, Issue 4, pp. 491-503, (2010) (PubMed).

Gray, Pett, Ward, Winder, Stanley, Roberts, Scarpini, Coleman: "In vitro progression of human papillomavirus 16 episome-associated cervical neoplasia displays fundamental similarities to integrant-associated carcinogenesis." in: Cancer research, Vol. 70, Issue 10, pp. 4081-91, (2010) (PubMed).

Target Details for Histone H4

Target: Histone H4 (HISTH4)

Alternative Name: Histone H4

Background: Histone H4 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 H4 occurs at several different lysine positions in the histone tail, and is performed by Histone Acetyltransferases (HATs) such as Hat1 or Gcn5. Acetylation of histones is often associated with transcriptional activation.

Molecular Weight: 8 kDa

Gene ID: 121504

NCBI Accession: NP_778224