Anti-L-Lactyllysine Rabbit pAb (BSA and Azide Free)

Primary Antibodies

Ambient temperature

Multiple

Post-Translational Modificaiton

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. This BSA-, glycerol-, and azide-free antibody is particularly suitable for applications such as mass cytometry.

Anti-L-Lactyllysine Rabbit pAb (BSA and Azide Free) detects proteins post-translationally modified by L-lactylation on lysine residues. This pan antibody recognizes L-lactylated lysine independent of its surrounding sequences.

Lactyl

L-lactylated lysine peptides

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.
This BSA-, glycerol-, and azide-free antibody is particularly suitable for applications such as mass cytometry.