Recombinant PRMT7 (accession number NP_061896.1) was expressed in Sf9 cells and contains an N-terminal FLAG tag with an observed molecular weight of 80.1 kDa.
PRMT7
Origine: Rat
Hôte: Levure
Recombinant
> 90 %
ELISA
Indications d'application
Recombinant PRMT7 is suitable for use in the study of enzyme kinetics, inhibitor screening, and selectivity profiling. Specific Activity: Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3). Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s.
Restrictions
For Research Use only
Conseil sur la manipulation
Avoid repeated freeze/thaw cycles and keep on ice when not in storage.
Stock
-80 °C
Stockage commentaire
Recombinant proteins in solution are temperature sensitive and must be stored at -80°C to prevent degradation.
ARABIDOPSIS THALIANA PROTEIN ARGININE METHYLTRANSFERASE 7 Protein, ATPRMT7 Protein, DL4310W Protein, FCAALL.195 Protein, protein arginine methyltransferase 7 Protein, RGD1304869 Protein, 4933402B05Rik Protein, BC006705 Protein, zgc:66172 Protein, protein arginine methyltransferase 7 Protein, protein arginine methyltransferase 7 L homeolog Protein, protein arginine N-methyltransferase 7 Protein, Protein arginine N-methyltransferase 7 Protein, PRMT7 Protein, Prmt7 Protein, prmt7.L Protein, prmt7 Protein, prmt-7 Protein
Sujet
PRMT7 (Protein Arginine Methyltransferase 7) is a type I arginine methyltransferase. Arginine methylation is a common post-translational modification of histones and other cellular proteins. PRMT7 specifically mediates the symmetrical dimethylation of histone H4 at Arg3 to form H4R3me2s. PRMT7 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 recruitment of DNA methyltransferases at these sites. PRMT7 may also play a role in embryonic stem cell (ESC) pluripotency. PRMT7 is also able to mediate arginine methylation of histone H2A and myelin basic protein (MBP) in vitro. However, the biological relevance of such results is unclear.