Anti-L-Lactyl-Histone H3 (Lys14) Rabbit mAb

WB, ICC/IF, ChIP

Histone H3

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 H3 (Lys14) Rabbit mAb detects endogenous levels of histone H3 when it is lactylated at Lys14.

Lactyl

L-lactylated human histone H3 (Lys14) peptide

Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. The Warburg effect, which originally described increased production of lactate in cancer, is associated with diverse cellular processes such as angiogenesis, hypoxia, polarization of macrophages and activation of T cells. This phenomenon is intimately linked to several diseases including neoplasia, sepsis and autoimmune diseases. Lactate, which is converted from pyruvate in tumour cells, is widely known as an energy source and metabolic by-product. Zhang et al. (Nature, 2019) reveal that histone lactylation is a previously unknown histone modification, derived from the cellular metabolite lactate.