Visit our FAQ
Toll Free Phone (USA and Canada Only): (888) 526-5351
Direct Phone: (734) 975-3888
Product Categories
Research Area
Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.
Lysine acetylation is an evolutionarily conserved post-translational modification that is found in prokaryotes and eukaryotes at histone and non-histone protein sites.1 Transfer of an acetyl group from acetyl-coenzyme A (acetyl-CoA) to the amino side chain of lysine is catalyzed by lysine acetyltransferases (KATs), including 13 canonical KATs from the GCN5, p300, and MYST families. Acetyl lysine removal is catalyzed by two major groups of lysine deacetylases (KDACs), the zinc-dependent histone deacetylases (HDACs) and the NAD+-dependent sirtuin deacetylases. Histone acetylation is associated with active gene transcription, and dysregulation of histone acetylation is associated with various diseases including cancer, Huntington's and Alzheimer's diseases, and amyotrophic lateral sclerosis (ALS).2,3,4 Non-histone protein acetylation is linked to various cellular processes including autophagy, DNA replication, lipid storage, mitochondrial fission and fusion, and protein synthesis, among others.1 Cayman’s Acetyl Lysine Monoclonal Antibody (Clone RM101) can be used for immunocytochemistry (ICC), immunohistochemistry (IHC), immunoprecipitation (IP), chromatin immunoprecipitation (ChIP), and Western blot (WB) applications.
WARNING This product is not for human or veterinary use.
1. Functions and mechanisms of non-
2. Histone modifications and cancer. Cold Spring Harb. Perspect. 8(4), a019521 (2016).
3. Histone acetylation in neuronal (dys)function. Biomol. Concepts 7(2), 103-116 (2016).
4. Epigenetics in amyotrophic lateral sclerosis: A role for histone post-