Acetyl-Histone H4 (Lys12) (D2W6O) Rabbit mAb (BSA and Azide Free) #50814

Filter:

WB
ELISA
IF
F

Supporting Data

REACTIVITY	H M R Mk
SENSITIVITY	Endogenous
MW (kDa)	11
Source/Isotype	Rabbit IgG

Application Key:

WB-Western Blotting
ELISA-ELISA
IF-Immunofluorescence
F-Flow Cytometry

Species Cross-Reactivity Key:

H-Human
M-Mouse
R-Rat
Mk-Monkey

Product Information

Product Usage Information

This product is the carrier free version of product #13944. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.

This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.

BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.

Formulation

Supplied in 1X PBS (10 mM Na₂HPO₄, 3 mM KCl, 2 mM KH₂PO₄, and 140 mM NaCl (pH 7.8)). BSA and Azide Free.

For standard formulation of this product see product #13944

Storage

Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.

Specificity / Sensitivity

Acetyl-Histone H4 (Lys12) (D2W6O) Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of histone H4 protein only when acetylated at Lys12. This antibody does not cross-react with other acetyl-histone proteins.

Species Reactivity:

Human, Mouse, Rat, Monkey

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic acetylated peptide corresponding to residues surrounding Lys12 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).

Database Links

UniProt ID: P62805

Entrez-Gene Id: 8359

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For Research Use Only. Not For Use In Diagnostic Procedures.

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