Tri-Methyl-Ezh2 (Lys509) (F1D1Q) Rabbit mAb recognizes endogenous levels of Ezh2 protein only when tri-methylated on Lys509.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding tri-methylated Lys509 of human Ezh2 protein.

The polycomb group (PcG) proteins are involved in maintaining the silenced state of several developmentally regulated genes and contribute to the maintenance of cell identity, cell cycle regulation, and oncogenesis (1,2). Enhancer of zeste homolog 2 (Ezh2), a member of this large protein family, contains four conserved regions including domain I, domain II, and a cysteine-rich amino acid stretch that precedes the carboxy-terminal SET domain (3). The SET domain has been linked with histone methyltransferase (HMTase) activity. Moreover, mammalian Ezh2 is a member of a histone deacetylase complex that functions in gene silencing, acting at the level of chromatin structure (4). Ezh2 complexes methylate histone H3 at Lys9 and 27 in vitro, which is thought to be involved in targeting transcriptional regulators to specific loci (5). Ezh2 is deregulated in various tumor types, and its role, both as a primary effector and as a mediator of tumorigenesis, has become a subject of increased interest (6).

Recent studies have identified methylated lysine residues within the highly conserved, disordered loop of Ezh2 and shown that methylation of these residues increases PRC2 histone methyltransferase activity (7).