Acetylated Lysine Antibody: FITC

Post-translational modifications (PTMs) of proteins are essential regulators of cellular function and biological signaling. Among these, lysine acetylation has emerged as a pivotal modification with profound implications in neuroscience and neurodegenerative disease research. This reversible process, mediated by histone acetyltransferases (HATs) and histone deacetylases (HDACs), modulates the acetylation status of lysine residues on both histone and non-histone proteins. The N-terminal tails of core histones—H2A, H2B, H3, and H4—are rich in lysine residues that undergo dynamic acetylation. This modification alters chromatin structure and directly influences gene expression, impacting key neuronal processes such as synaptic plasticity, memory formation, and neurodevelopment. Beyond chromatin remodeling, lysine Nε-acetylation functions as a critical intracellular signaling mechanism. It regulates diverse cellular pathways including gene transcription, cell cycle progression, apoptosis, DNA repair, and cytoskeletal dynamics—all of which are highly relevant to the pathophysiology of neurodegenerative disorders. Disruption in the regulation of protein acetylation has been implicated in several neurological diseases, including Alzheimer’s disease, Huntington’s disease, and other polyglutamine expansion disorders. Aberrant HDAC activity, in particular, contributes to neurotoxicity and neuronal dysfunction, making HDAC inhibitors promising therapeutic candidates in both oncology and neurology. As research advances, acetylated lysine is increasingly recognized not only as a biomarker of disease progression but also as a potential target for therapeutic intervention. Understanding the acetylation landscape in the nervous system is therefore critical for developing novel strategies to combat neurodegeneration and promote brain health.

1. Yang X.J. (2005) Oncogene. 24:1653-1662. 2. Hassig C.A. and Schreiber S.L. (1997) Curr. Opin. Chem. Biol. 1 (3) : 300-308. 3. Yang X.J. (2004) Bioessays 26:1076-1087. 4. Hughes R.E. (2002) Curr. Biol. 12: R141-R143. 5. Vigushin D.M. and Coombes R.C. (2004) Curr. Cancer Drug Targets 4: 205-218. 6. Chan H.M. et al. (2001) Nat. Cell Biol. 3: 667-674. 7. Martinez-Balbas M.A. et al. (2000) EMBO J. 19: 662-671.