Acetylation of proteins can occur as a co-translational or posttranslational
modification (PTM) (1). Co-translational acetylation
occurs at the N-terminus of approximately 85% of mammalian proteins,
is irreversible, and is thought to be important in protein stability,
localization, and synthesis (1). Post-translational acetylation
occurs on the epsilon amino group of lysine residues as a reversible
and highly dynamic PTM that is known to be a key regulator in
multiple cellular events, including chromatin structure, transcription,
metabolism , signal transduction, and cytoskeletal regulation (2-3).
Identification and enrichment of acetylated proteins have been hindered
by a lack of high affinity Ac-K antibodies. Here, we present
validation data for two newly developed Ac-K antibodies, 7B5A1
and 19C4B2.1, and their usefulness in enriching and detecting
acetylated proteins in both cell and tissue lysates.
