Anti-L-Lactyl-Histone H4 (Lys5) Mouse mAb

Primary Antibodies

Histone H4

Store at -20°C. Avoid freeze/thaw cycles.

Stable for 12 months from date of receipt/reconstitution.

Histones, fundamental proteins involved in chromatin structure and gene regulation, are subject to a wide array of enzyme-catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitination, and numerous others. Histone L-lactylation, a recently discovered post-translational modification induced by lactate has emerged as a significant addition to this repertoire. The extent and dynamics of this modification are highly reliant on lactate levels within the cellular microenvironment and can be modulated through the introduction of extracellular lactate in cultured cells or the stimulation of intracellular glycolysis. The introduction of lysine L-lactylation is mediated by the acetyltransferase p300, while the removal of lactylation marks from histones has been attributed to Class I histone deacetylases (HDAC 1-3). Histone lactylation has been implicated in various biological processes, including inflammation, fibrosis, differentiation, and cancer progression.

Anti-L-Lactyl-Histone H4 (Lys5) Mouse mAb detects histone H4 only when it is L-lactylated at Lys5.

Lactyl

L-lactylated human histone H4 (Lys5) peptide

Lactate, previously recognized solely as an energy source and metabolic byproduct, has now emerged as a crucial player in cancer biology, especially within the scope of the Warburg effect and its intricate interplay with various cellular processes, including angiogenesis, hypoxia, polarization of macrophages, and T cell activation. Recent investigations have unveiled an unprecedented function of lactate in the realm of histone modification, specifically through lysine L-lactylation, which exerts regulatory control over gene expression. The extent and dynamics of this modification are highly reliant on lactate levels within the cellular microenvironment and can be modulated through the introduction of extracellular lactate in cultured cells or the stimulation of intracellular glycolysis. The acetyltransferase p300 is responsible for introducing lysine L-lactylation, while Class I histone deacetylases (HDAC 1-3) have been identified as an eraser of the lactylation marks on histones.