D-Lactyl Lysine Rabbit Polyclonal Antibody

D-lactyl lysine (abbreviated as K-Dla) is a novel acylative post-translational modification recently discovered on proteins. Unlike L-lactylation, which is driven by L-lactate from glycolysis, D-lactylation occurs primarily through a distinct metabolic pathway: it does not directly derive from D-lactate but instead is formed by the non-enzymatic covalent attachment of a D-lactyl group to lysine residues on proteins via S-D-lactoyl glutathione (SLG), an intermediate of the glyoxalase pathway. This process is significantly triggered under specific physiological conditions, such as during immune cell activation. For example, when NF-κB signaling leads to the downregulation of the key enzyme GLO2, its substrate SLG accumulates within cells, thereby massively inducing D-lactylation modification. This modification is considered a self-regulatory "braking" mechanism of the cell—for instance, by modifying RelA, a key protein in the NF-κB pathway, it suppresses excessive inflammatory responses to restore immune homeostasis. In addition, D-lactate secreted by gut microbiota can also induce D-lactylation in host cells, thereby regulating gene transcription and being associated with the development and progression of various diseases, including hepatocellular carcinoma. Currently, this newly discovered modification opens new perspectives for understanding the connections among cellular metabolism, microbiota, and host epigenetic regulation.