Anti-acetyl Lysine antibody [7F8]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Acetyl lysine often referred to as acetylated lysine is a modification of the amino acid lysine where an acetyl group is transferred to the lysine residue. This modification impacts the mass of the lysine residue slightly altering its properties. Acetyl lysine occurs in histone proteins and this modification is an important regulator of chromatin structure and function. The acetylation of lysine residues happens frequently in the nucleus of eukaryotic cells where histone acetylases (HATs) facilitate this process. Known alternatively as lysine acetylation it represents an important post-translational modification impacting gene expression regulation.

Biological function summary

Acetylation adds an acetyl group to the lysine which changes its positive charge reducing chromatin compaction and enhancing gene transcription. The acetyl lysine modification is not acting alone; it forms part of larger histone modification complexes. By altering chromatin structure acetyl lysine regulates the accessibility of transcription factors to DNA influencing various biological processes like DNA repair replication and cell cycle progression. The interaction between acetyl lysine and chromatin remodeling complexes plays a significant role in epigenetic regulation.

Pathways

Acetyl lysine is central to epigenetic regulatory pathways significantly impacting gene expression and cellular growth pathways. The acetylation process involves histone acetylases (HATs) such as the p300/CBP complex which adds acetyl groups to specific lysines on histones increasing transcriptional activity. Conversely histone deacetylases (HDACs) remove acetyl groups decreasing transcription. The balance of these modifications involves critical pathways such as the TGF-beta signaling pathway and the NF-kB pathway linking acetyl lysine with numerous cellular activities and protein interactions.

Associated diseases and disorders

Dysregulation of acetyl lysine levels is associated with cancer and neurodegenerative diseases. In cancer the aberrant acetylation of lysine impacts expression of oncogenes and tumor suppressor genes contributing to carcinogenesis. Proteins like p53 which relies on acetylation for activation become functionally impaired. Also in neurodegenerative disorders such as Alzheimer's disease histone acetylation imbalances disrupt neuronal function and gene expression. The involvement of the sirtuin family of proteins which act as NAD+-dependent deacetylases connects lysine acetylation to these diseases highlighting its importance in maintaining normal cellular functions and its role in pathological states.