β-Hydroxybutyryl Lysine Rabbit Polyclonal Antibody

β-Hydroxybutyryl lysine (abbreviated as Kbhb) is a recently discovered histone lysine acylation modification driven by the ketone body metabolite β-hydroxybutyrate (BHB), which directly links metabolic status to gene expression regulation. Unlike the well-known acetylation and crotonylation, Kbhb formation depends on the covalent attachment of β-hydroxybutyryl groups to histone lysine residues by BHB through specific enzymes such as p300/CBP acyltransferases, while its removal is mediated by deacylases including HDAC1/2 and SIRT3. Functionally, Kbhb possesses a unique structural feature—its additional hydroxyl group enables it to exert distinctly different roles in epigenetic regulation compared to acetylation. Notably, under physiological conditions with significantly elevated ketone levels, such as starvation, fasting, or prolonged exercise, Kbhb is extensively deposited at the promoters and enhancers of active genes, thereby reprogramming gene expression networks. Studies have revealed that a hallmark function of Kbhb is to drive cellular adaptation to metabolic stress by enhancing the transcription of specific genes, such as those involved in oxidative metabolism and antioxidant responses. For example, in the livers of fasted mice, Kbhb modification levels are markedly increased, which in turn upregulates fatty acid oxidation and ketogenesis-related pathways. At the pathological level, dysregulation of this modification is closely associated with various diseases, including cancer, metabolic syndrome, and heart failure, thus positioning Kbhb as a novel molecular bridge connecting nutritional status, epigenetic memory, and disease pathogenesis.