Histone H4 (Lactyl K5) Recombinant Rabbit mAb (S-3220-73)

Histone H4 (Lactyl K5), denoted as H4K5la, is a specific post-translational modification where a lactyl group derived from cellular lactate is covalently attached to the 5th lysine residue of the histone H4 N-terminal tail. As a critical component of the recently discovered "histone lactylation" code, this mark functions as a direct epigenetic sensor linking high glycolytic flux and lactate accumulation to chromatin regulation. Unlike the well-studied acetylation at the same site (H4K5ac), which is generally associated with active transcription and nucleosome assembly during DNA replication, H4K5la has been increasingly implicated in distinct pathological and physiological contexts, such as the pro-inflammatory activation of microglia following ischemic stroke, where it promotes the transcription of key immunometabolic genes (e.g., HK1, Fads2) to drive fatty acid-dependent inflammatory responses. The dynamic deposition of H4K5la, potentially regulated by specific writers like GCN5 in response to metabolic stress, establishes a unique mechanistic bridge between cellular metabolism (particularly the Warburg effect or hypoxia-induced glycolysis) and the fine-tuning of gene expression programs involved in inflammation, tissue injury, and potentially tumor progression, offering novel therapeutic targets for diseases characterized by metabolic-epigenetic dysregulation.