PRMT1 from rat

Methyl transferases catalyze the addition of methyl groups to nitrogen, carbon, sulfur, and oxygen atoms of small molecules, lipids, proteins, and nucleic acids. Eight mammalian protein arginine methyltransferases (PRMT) have been identified. PRMT1 is the predominant member of the methyl transferases, which catalyzes the protein arginine N-methylation reactions. PRMT1 is implicated in various cellular processes including: transcription, RNA processing, and signal transduction.

PRMT1 is the predominant member of the methyl transferases, which catalyzes the protein arginine N-methylation reactions. PRMT1 is implicated in various cellular processes including: transcription, RNA processing, and signal transduction.

Solution of 50 mM Tris, pH 7.6, 5 mM DTT, 0.2% IGEPAL^® CA-630, 150 mM NaCl, and 30% glycerol (w/v).

The N-methyltransferase activity is determined by detecting the level of radiolabel transfer from ³H-AdoMet (Methyl donor) to histone (Cat. No. H4380), which is arginine rich (methyl acceptor).

The specific activity is ≥ 0.1 nmol/mgP/min. measured by ³H-AdoMet incorporation into histone for 30 minues at 30 °C.

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