epitope mapping near the N-terminus of G9a of human origin
recommended for detection of G9a of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine and porcine
G9a Background Information Distinct modifications of histone tails, such as acetylation, phosphorlation and methylation, regulate nuclear processes, such as control of transcription and mitotic chromosome condensation (1). Histone methyltransferases (HMTases) are among the different groups of enzymes known to catalyze the covalent modification (1). G9a, a SET domain-containing protein, is a novel mammalian lysine-preferring HMTase (1). G9a, also known as BAT8, NG36 or HMTase (for mammalian histone methyltransferase), has strong HMTase activity towards histone H3 lysine 9 methylation in vitro (2–4). G9a plays a dominant role in euchromatic histone H3 lysine 9 methylation, is essential for early embryogenesis and is involved in the transcriptional repression of developmental genes (2). Like SUV39H, G9a transfers methyl groups to the lysine residues of histone H3, but with a 10-20-fold higher activity than SUV39H1 (1). G9a also adds methyl groups to lysine 27 as well as lysine 9 in histone H3 (1). G9a localizes in the nucleus, indicating that it may contribute to the organization of the higher order chromatin structure of non-centromeric loci (1). The human G9a gene maps to chromosome 6p21.3 (3,5,6).
