Anti-L-Lactyl-Histone H2B (Lys15) Rabbit mAb

Histone & Histone Modification Antibodies

Ambient temperature

14

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 H2B (Lys15) Rabbit mAb detects histone H2B only when it is L-lactylated at Lys15.

Lactyl

L-lactylated human histone H2B (Lys15) peptide

Stable for 12 months from date of receipt/reconstitution.

Nucleus