β-Hydroxybutyryl Lysine (E6H5Q) Rabbit mAb recognizes a broad range of β-hydroxybutyryl lysine (Kbhb) containing proteins and peptides. This antibody does not cross-react with free β-hydroxybutyrate, and does not cross-react with peptides or proteins containing α-hydroxyisobutyrylated, acetylated, butyrylated, carboxymethylated, carboxyethylated, crotonylated, propionylated, or succinylated lysines.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide containing lysine β-hydroxybutyrylation flanked by degenerate amino acids at positions N- and C-terminal to the modified lysine.

Lysine β-hydroxybutyrylation (Kbhb) is a reversible post-translational modification (PTM) that shares multiple regulatory enzymes with cellular acetylation machinery, including EP300 and HDAC1 (1). While acetylation is derived from acetyl-coenzyme-A (CoA), β-hydroxybutyrylation is derived from β-hydroxybutyryl-CoA, an intermediate generated from the metabolite β-hydroxybutyrate that is upregulated during nutrient limiting conditions such as starvation, ketogenic diets, and in diseases such as diabetes (2). The elucidation of the enzymes responsible for charging β-hydroxybutyrate with CoA to form β-hydroxybutyryl-CoA remains an active research area (3).

Notable bhb-modified substrates identified through proteomic investigations include histones, as well as non-histone substrates such as FASN and TP53 (4-6). In models where cells are incubated with excess β-hydroxybutyrate to induce this PTM, protein sites displaying upregulated bhb levels differ from sites displaying upregulated acetylation levels, suggesting potential differences in Kbhb-induced pathways and crosstalk between distinct modification types.