In the nucleus, DNA is tightly packed into nucleosomes generating an environment which is highly repressive towards DNA processes such as transcription. Acetylation of lysine residues within proteins has emerged as an important mechanism used by cells to overcome this repression. The acetylation of non-histone proteins such as transcription factors, as well as histones appears to be involved in this process. Acetylation may result in structural transitions as well as specific signaling within discrete chromatin domains. The role of acetylation in intracellular signaling has been inferred from the binding of acetylated peptides by the conserved bromodomain. Furthermore, recent findings suggest that bromodomain/acetylated-lysine recognition can serve as a regulatory mechanism in protein-protein interactions in numerous cellular processes such as chromatin remodeling and transcriptional activation.
Acetyl-lysine containing proteins including histones, from sodium butyrate or Trichostatin A treated cells, p53 acetylated in vitro by p300 or PCAF, and chemically acetylated BSA.
Broad species reactivity expected.
A mixture of chemically acetylated antigens.
Anti-acetyl-Lysine Antibody is a high quality Rabbit Polyclonal Antibody for the detection of acetyl-Lysine & has been validated in WB & IP.
Immunoprecipitation: 5 μL of a previous lot immunoprecipitated in vitro acetylated recombinant p300.
Western Blot Analysis: A 1:1000 dilution of the previous lot of the antibody detected:
• Acetylated histones and to a lesser degree, other proteins in RIPA lysate from trichostatin A (5 μM) treated Cos-1 cells. Trichostatin A, an inhibitor of deacetylases also, was used to increase the level of acetylated histones. (Panel B).
• GST-p53 (100 ng) acetylated in vitro with either recombinant p300 or PCAF. (Panel C).
Epigenetics & Nuclear Function
Research Sub Category
Evaluated by western blot on acid-extracted proteins from sodium butyrate treated HeLa cells, chemically acetylated BSA, acetylated histones and to a lesser degree, other proteins in trichostatin A treated Cos-1 cell lysate.
Western Blot Analysis: 1:1000-1:2000 dilution of this antibody detected:
• Acetylated histones in acid-extracted proteins from sodium butyrate (5 mM) treated HeLa cells. Sodium butyrate, an inhibitor of deacetylases, was used to increase the level of acetylated histones. (Panel A).
• Chemically acetylated BSA (10 ng) in a dot blot assay.
Dependent upon the molecular weight of the lysine acetylated protein being detected.
Rabbit IgG serum containing 0.05% sodium azide and 30% glycerol.
Storage and Stability
Stable for 1 year at from date of receipt.
TSA-treated HeLa and NIH/3T3 cells, osteosarcoma tissue.
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
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