Description
Product Usage Information
Western Blotting: 1:1000
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at -20°C. Do not aliquot the antibody.
Protocol
Available protocols: Western Blotting
Specificity / Sensitivity
Benzoyl Lysine (F5U6Z) Rabbit Monoclonal Antibody recognizes a broad range of benzoyl lysine (Kbz) containing proteins and peptides. This antibody does not cross-react with free sodium benzoate.
Species Reactivity: All Species Expected
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide containing lysine benzoylation flanked by degenerate amino acids at positions N- and C-terminal to the modified lysine.
Background
Benzoyl lysine (Kbz) or lysine benzoylation is a reversible post-translational modification (PTM) that occurs on the ε-amine group of the lysine side chain. Kbz is derived from benzoyl-coenzyme A (benzoyl-CoA), an intermediate generated from the breakdown of sodium benzoate, a common food preservative, within mitochondria to form hippurate for excretion (1). In bacteria, benzoyl-CoA can be generated during the breakdown of diverse aromatic molecules beyond sodium benzoate to eventually form acetyl-CoA for energy (2). Enzymes that utilize benzoyl-CoA to form Kbz include KAT7 in humans and GcnE in , and enzymes that remove Kbz include SIRT2 and SIRT3 in humans and Hst2 in (3-6). Because the compounds that induce Kbz can have broad and conflicting effects, such as sodium benzoate impacting insulin secretion, and because many of the lysine benzoylation regulatory enzymes have shared roles in modulating other modifications such as acetylation, it can be challenging to discern Kbz-specific effects from Kbz-independent responses (1,7). Kbz was initially discovered on histone proteins, yet Kbz-modified substrates extend into non-histone substrates, including alcohol dehydrogenase B (AdhB) in and ATP-citrate lyase (ACLY) in humans (4,5,8). In the former case, AdhB competes with aflatoxin generation by converting the aflatoxin precursor acetaldehyde to ethanol. Mutation of a Kbz-modified site on AdhB to a non-lysine residue prevents Kbz formation and attenuates AdhB enzymatic activity, leading to increased aflatoxin production by the fungus (4). In the latter case, treating cells with sodium benzoate to elevate ACLY benzoylation or expressing an ACLY transgene encoded with a Kbz site using non-natural amino acids leads to reduced ACLY enzymatic activity (5).
