Asymmetric dimethylation of arginine side chains in proteins is a frequent posttranslational modification, catalyzed by type I protein arginine methyltransferases (PRMTs). PRMT8 is a membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA). PRMT8 can form dimers with PRMT2 or PRMT1 and interacts with FYN kinase. PRMT8 is brain specific and it is a vertebrate restricted paralogue of PRMT1. In the past, arginine methylation was mainly observed on abundant proteins such as RNA-binding proteins and histones, but recent advances have revealed a plethora of arginine-methylated proteins implicated in a variety of cellular processes including signal transduction, epigenetic regulation and DNA repair pathways. PRMT8 has been shown to be critical for proper neuronal development and its expression is regionally restricted in the adult suggesting that PRMT8 is chiefly involved in the somatosensory and limbic systems, and a part of the motor nervous system development and maintenance.
Synonyms: Protein arginine N-methyltransferase 8, Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4, Protein arginine methyltransferase 8
Application: This Anti-PRMT8 Antibody is validated for use in Western Blotting and Immunohistochemistry for the detection of PRMT8.
Other Notes: Concentration: Please refer to lot specific datasheet.