, corresponding to internal sequence amino acids 346-360 of Human PRMT7. This amino acid sequence can be found in five different human PRMT7 isoforms: CRA_a (692 amino acids), CRA_b (613 amino acids), CRA_c (465 amino acids), CRA_d (655 amino acids) and CRA_e (567 amino acids)
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use a concentration of 2 µg/ml. Detects a band of approximately 68 kDa.
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.
Defects in PRMT7 are associated with mild intellectual disabilityy, obesity and symmetrical shortening of the digits and posterior metacarpals and metatarsals. The phenotype is a phenocopy of pseudohypoparathyroidism (PHP).
Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. Contains 2 SAM-dependent MTase PRMT-type domains.
Verbiest V et al. Protein arginine (N)-methyl transferase 7 (PRMT7) as a potential target for the sensitization of tumor cells to camptothecins. FEBS Lett582:1483-9 (2008).
Read more (PubMed: 18381071) »