PRMT8 (protein arginine methyltransferase 8), an arginine methyltransferase that exhibits type I PRMT activity, catalyzing the formation of omega-NG-monomethylated and asymmetrically omega-NG, NG-dimethylated arginine residues. Its N-terminal end harbors a myristoylation motif, and the myristoylation results in its association with the plasma membrane. Unlike other members of PRMTs, it is largely expressed in the brain. It was also found that the N-terminal domain may function as an autoregulator that may be displaced by interaction with one or more physiological inducers.
1. Lee J, et al: PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family. J Biol Chem 280(38):32890-6. 2005.
2. Sayegh J, et al: Regulation of protein arginine methyl-transferase 8 (PRMT8) activity by its N-terminal domain. J Biol Chem. 282(50):36444-53, 2007.
Sample Enzyme Activity Plot. For specific information on a given lot, see related technical data sheet.
Sample Purity Data. For specific information on a given lot, see related technical data sheet.
Storage, Stability, and Shipping:
Store product at –70oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
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