Anti-PRMT9 Antibody, clone 128-29-1 clone 128-29-1, from mouse

Putative protein arginine N-methyltransferase 9 (UniProt Q6P2P2; also known as Putative protein arginine N-methyltransferase 10) is encoded by the PRMT9 (also known as PRMT10) gene (Gene ID 90826) in human. Mammalian protein arginine methyltransferases (PRMTs) catalyze the methylation of arginine residues on histone and non-histone proteins. PRMTs are divided into three types based on their mode of activity. Type I PRMTs (PRMT1-4, PRMT6, and PRMT8) transfer up to two methyl groups on the same terminal guanidino nitrogen of arginine to form omega-NG-monomethylarginine (MMA) and omega-NG,NG-asymmetric dimethylarginine (ADMA) residues. Type II PRMTs (PRMT5 and PRMT9) transfer methyl groups on different terminal guanidino nitrogens to form ΜΜAlpha and omega-NG,N'G-symmetric dimethylarginine (SDMA) residues, while type III PRMT7 transfers only one single methyl group to form MMA residues. PRMT9 is involved in alternative splicing regulation by modulating spliceosomal small nuclear ribonucleoprotein (snRNP) maturation in the cytoplasm. PRMT9 complexes with the splicing factors SF3B2 (SAP145) and SF3B4 (SAP49) and mediates SF3B2 Arg508 modification via MMA and SDMA. Similar to PRMT7, but unlike other PRMTs, PRMT9 contains a duplicated methyltransferase domain (a.a. 137-446 and 530-845), with the N-terminal MTase acting as a funtional AdoMet-binding domain and the C-terminal MTase domain serving a pseudodimer function, mimicking the homodimer formation of other PRMTs needed for subtrate processing. In addition, PRMT9 contains three tetratricopeptide repeats (TPR1-3; a.a. 25-58, 67-100, 101-134) known to mediate protein-protein interactions.