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PRMT7 blocking peptide
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- BACKGROUND
| Primary Accession | Q9NVM4 |
|---|---|
| Gene ID | 54496 |
| Calculated MW | 78459 Da |
| Gene ID | 54496 |
|---|---|
| Application & Usage | The peptide is used for blocking the antibody activity of PRMT7. It usually blocks the antibody activity completely in Western blot analysis by incubating the peptide with equal volume of antibody for 30-60 minutes at 37°C. |
| Other Names | Protein arginine N-methyltransferase 7, 2.1.1.-, Histone-arginine N-methyltransferase PRMT7, 2.1.1.125, [Myelin basic protein]-arginine N-methyltransferase PRMT7, 2.1.1.126, PRMT7, KIAA1933 |
| Target/Specificity | PRMT7 |
| Formulation | 50 µg (0.5 mg/ml) in phosphate buffered saline (PBS), pH 7.2, containing 50% glycerol, 1% BSA and 0.02% thimerosal. |
| Reconstitution & Storage | -20 °C |
| Background Descriptions | |
| Precautions | PRMT7 blocking peptide is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | PRMT7 |
|---|---|
| Synonyms | KIAA1933 |
| Function | 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. |
| Cellular Location | Cytoplasm, cytosol. Nucleus |
Research Areas
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