PRMT1, Recombinant, Human, GST-Tag (Protein Arginine N-methyltransferase 1, HRMT1L2, IR1B4, HCP1)

PRMT1 is a protein arginine methyltransferase that functions as a histone methyltransferase specific for histone H4. PRMT1 specifically methylates arginine-3 of histone H4 in vitro and in vivo. Methylation of arg3 by PRMT1 facilitates subsequent acetylation of histone H4 tails by p300. PRMT1 performs methylation of arg31 of STAT1 and this is required for transcription induced by IFN-alpha/IFN-beta. Arginine methylation of STAT1 is an additional posttranslational modification regulating transcription factor function, and alteration of arginine methylation might be responsible for the lack of interferon responsiveness observed in many malignancies. Type I PRMTs ((CARM1, PRMT1, PRMT2, PRMT3, PRMT6, and PRMT8) catalyze asymmetric dimethylarginine (ADMA), while type II PRMTs (e.g. PRMTs 5 and 7) catalyze SDMA. PRMT1 is the primary methyltransferase that deposits the ADMA mark, and it accounts for over 90% of this type of methylation. Source: Recombinant protein corresponding to human PRMT1, aa2-end, fused to N-terminal GST-tag, expressed in a Baculovirus infected Sf9 cell expression system. Molecular Weight: ~68kD, Specific Activity: ~6.2pmol/min/ug, Assay Conditions: Enzyme was incubated with 0.25uM of biotinylated H4 1-21 peptide with 1uM AdoMet in HMT buffer 2A in a 10ul reaction. 5ul of Rabbit AlphaLISA acceptor beads (1:250) and 5ul of Primary Antibody 4 (1:20) were added and incubation continued for 30 min. Streptavidin Donor beads (1:125) were added (10ul) and mixture was further incubated for 15 min at RT before A-counts were measured. Storage and Stability: Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.