Anti-L-Lactyl-Histone H3 (Lys27) Rabbit pAb

Primary Antibodies

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 (Lys27) Rabbit pAb detects histone H3 only when it is L-lactylated at Lys27.

Lactyl

L-lactylated human histone H3 (Lys27) peptide

Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation and novel acylations directly affect the accessibility of chromatin to transcription factors and other epigenetic regulators, altering genome stability, gene transcription, etc. Histone acetylation occurs primarily at multiple lysine residues on the aminoterminal of core histones, in response to various stimuli and plays vital roles in the regulation of gene expression, DNA damage repair, chromatin dynamics, etc. Mostly, histone H2A is primarily acetylated at Lys5, 9, 15, and 36; H2B is primarily acetylated at Lys5, 12, 15, 16, and 20. Histone H3 is primarily acetylated at Lys4, 9, 14, 18, 23, 27, 56, and 79. Histone H4 is primarily acetylated at Lys5, 8, 12, 16, and 20. Histone acetyltransferases (HATs) and histone deacetylases (HDACs) are major regulating factors.