| Product description |
Mouse monoclonal [PRMT3 - 367] to PRMT3Posttranslational modifications of proteins play an important role in the regulation of protein function, stability and localization. Such modifications occur on different amino acids and include phosphorylation, glycosylation, acetylation, or methylation. Arginine methylation is mediated by the Protein-Arginine Methyl Transferase (PRMT) family of enzymes, which are important in signal transduction, transcription, RNA transport, and splicing. PRMTs are divided into two types defined by their activity. Type I PRMTs (including PRMT 1, 3, 4, and 6) are characterized by the formation of asymmetric dimethylated arginine residues. In type I PRMTs, the methylate arginine is found in different motifs such as the Arg-Gly-Gly-rich region (RGG motif) in many RNA binding proteins or the Arg-Xaa-Arg motif in poly(A)- binding protein II. Type II PRMTs, which include only PRMT5, are defined by the formation of symmetric dimethylated arginine residues. Substrates for PRMT5 include myelin basic protein (MBP) and the spliceosomal D1 and D3 proteins. PRMT3 is expressed in several tissues such as heart, small intestine, kidney, ovary, testis, thyroid, and cortex with a cytoplasmic localization within the cells. PRMT3 consists of two important domains in its N-terminal region (a C2H2 zinc-finger motif and a tyrosine-phosphorylation consensus sequence), which are probably important for regulation and catalytic activity. |
