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Description
| Specificity | PRMT5 Rabbit Recombinant mAb detects endogenous level of total PRMT5. |
|---|---|
| Background | The protein arginine methyltransferase 5 (PRMT5, also known as Hsl7, Jbp1, Skb1, Capsuleen, or Dart5) is the major enzyme responsible for mono- and symmetric dimethylation of arginine. It is the primary Type II arginine methyltransferase and found in all eukaryotic species. Histone and other protein methylation by PRMT5 regulate genome organization, transcription, stem cells, primordial germ cells, differentiation, the cell cycle, and spliceosome assembly. PRMT5 also directly associates with a range of other protein factors, including pICln, Menin, CoPR5 and RioK1 that may alter its subcellular localization and protein substrate selection. In a variety of somatic cells, PRMT5 predominantly localizes to the cytoplasm and the translocation of PRMT5 appears to play a role in controlling pluripotency in early development of mouse embryos. |
Usage Information
| Application | WB,ELISA | ||
|---|---|---|---|
| Dilution |
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| Reactivity | Human Mouse Rat | ||
| MW (kDa) | 73kDa | ||
| Source | Rabbit | ||
| Concentration | 1mg/ml | ||
| Storage buffer | 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. | ||
| Storage (From the date of receipt) |
Store at –20°C. |
Application Data
WB