Render Target: SSR
Render Timestamp:
4/6/2025, 7:29:20 PM EDT
4/6/2025, 11:29:20 PM UTC
Commit: 461ca8d8fe5b1efd4c01fc87e5b5eb592e2d154a
XML generation date: 2025-03-07 13:20:16.953
Product last modified at: 2025-02-17T07:00:13.942Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Acetyl-Histone H3 (Lys23) (F1Y4B) Rabbit mAb #86664

Filter:
  • WB
  • IF
Western Blotting Image 1: Acetyl-Histone H3 (Lys23) (F1Y4B) Rabbit mAb
Western blot analysis of extracts from HeLa cells, untreated (-) or treated with Trichostatin A (TSA) #9950 (1 μM, 18 hr; +), using Acetyl-Histone H3 (Lys23) (F1Y4B) Rabbit mAb (upper) or β-Actin (D6A8) Rabbit mAb #8457 (lower).

To Purchase # 86664

Supporting Data

REACTIVITY H M R Mk
SENSITIVITY Endogenous
MW (kDa) 17
Source/Isotype Rabbit IgG
Application Key:
  • WB-Western Blotting 
  • IF-Immunofluorescence 
Species Cross-Reactivity Key:
  • H-Human 
  • M-Mouse 
  • R-Rat 
  • Mk-Monkey 
  • Related Products

Product Information

Product Usage Information

Application Dilution
Western Blotting 1:1000
Immunofluorescence (Immunocytochemistry) 1:100 - 1:400

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

Acetyl-Histone H3 (Lys23) (F1Y4B) Rabbit mAb recognizes endogenous levels of histone H3 protein when acetylated at Lys23. This antibody does not show any significant cross-reactivity with other acetylated histone residues based on our histone peptide array analyses.

Species Reactivity:

Human, Mouse, Rat, Monkey

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding acetyl-Lys23 of human histone H3 protein.

Background

The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1,2). Histone acetylation occurs mainly on the amino-terminal tail domains of histones H2A (Lys5), H2B (Lys5, 12, 15, and 20), H3 (Lys9, 14, 18, 23, 27, 36, and 56), and H4 (Lys5, 8, 12, and 16) and is important for the regulation of histone deposition, transcriptional activation, DNA replication, recombination, and DNA repair (1-3). Hyper-acetylation of the histone tails neutralizes the positive charge of these domains and is believed to weaken histone-DNA and nucleosome-nucleosome interactions, thereby destabilizing chromatin structure and increasing the accessibility of DNA to various DNA-binding proteins (4,5). In addition, acetylation of specific lysine residues creates docking sites for a protein module called the bromodomain, which binds to acetylated lysine residues (6). Many transcription and chromatin regulatory proteins contain bromodomains and may be recruited to gene promoters, in part, through binding of acetylated histone tails. Histone acetylation is mediated by histone acetyltransferases (HATs), such as CBP/p300, GCN5L2, PCAF, and Tip60, which are recruited to genes by DNA-bound protein factors to facilitate transcriptional activation (3). Deacetylation, which is mediated by histone deacetylases (HDAC and sirtuin proteins), reverses the effects of acetylation and generally facilitates transcriptional repression (7,8).

Pathways

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