Product Usage Information
Immunofluorescence (Immunocytochemistry): 1:800
Flow Cytometry (Fixed/Permeabilized): 1:50
Storage
Supplied in PBS (pH 7.2), less than 0.1% sodium azide and 2 mg/ml BSA. Store at 4°C. Do not aliquot the antibody. Protect from light. Do not freeze.
Protocol
Available protocols: Immunofluorescence (Immunocytochemistry), Flow Cytometry (Fixed/Permeabilized)
Specificity / Sensitivity
Acetyl-Histone H4 (Lys16) (E2B8W) Rabbit Monoclonal Antibody (Alexa Fluor
Species Reactivity: Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding acetylated Lys16 of human histone H4 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).
Alternate Names
H4; H4 clustered histone 1; H4 histone family, member A; H4-16; H4/A; H4/B; H4/C; H4/D; H4/E; H4/G; H4/H; H4/I; H4/J; H4/K; H4/M; H4/N; H4/O; H4C1; H4C11; H4C12; H4C13; H4C14; H4C15; H4C2; H4C3; H4C4; H4C5; H4C6; H4C8; H4C9; H4F2; H4FA; H4FB; H4FC; H4FD; H4FE; H4FG; H4FH; H4FI; H4FJ; H4FK; H4FM; H4FN; H4FO; HIST1H4A; HIST1H4B; HIST1H4C; HIST1H4D; HIST1H4E; HIST1H4F; HIST1H4H; HIST1H4I; HIST1H4J; HIST1H4K; HIST1H4L; HIST2H4; HIST2H4A; HIST2H4B; HIST4H4; histone 1, H4a; histone cluster 1 H4 family member a; histone cluster 1, H4a; Histone H4
