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PRMT3 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O60678 |
|---|---|
| Clone Names | 4051907 |
| Gene ID | 10196 |
|---|---|
| Other Names | Protein arginine N-methyltransferase 3, 211-, Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3, PRMT3, HRMT1L3 |
| Target/Specificity | The synthetic peptide sequence is selected from aa 456~472 of human PRMT3. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | PRMT3 (HGNC:30163) |
|---|---|
| Function | Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases (PubMed:22795084, PubMed:23445220, PubMed:25728001, PubMed:31378783, PubMed:33495566, PubMed:39513743). Catalyzes the asymmetric arginine dimethylation at multiple sites in the Arg/Gly-rich region of small ribosomal subunit protein uS5/RPS2 (PubMed:22795084). Also appears to methylate other ribosomal proteins (By similarity). May regulate retinoic acid synthesis and signaling by inhibiting ALDH1A1 retinal dehydrogenase activity (PubMed:33495566). Contributes to methylation of histone H4 'Arg-3', a specific tag for epigenetic transcriptional activation (PubMed:25728001, PubMed:31378783, PubMed:39513743). Mediates asymmetric arginine dimethylation of histone H4 'Arg-3' (H4R3me2a) in the promoter region of miRNA miR-3648, to promote its transcription and osteogenesis (PubMed:31378783). |
| Cellular Location | Cytoplasm, cytosol. Nucleus Note=Localized to the nucleus by ZNF200. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Arginine methylation is an irreversible post translational modification which has only recently been linked to protein activity. At least three types of PRMT enzymes have been identified in mammalian cells. These enzymes have been shown to have essential regulatory functions by methylation of key proteins in several fundamental areas. These protein include nuclear proteins, IL enhancer binding factor, nuclear factors, cell cycle proteins, signal transduction proteins, apoptosis proteins, and viral proteins. The mammalian PRMT family currently consists of 7 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all 7 PRMT members have been developed.
References
Wada K, et al. Biochim Biophys Acta. 2002. 1591:1.Cimato TR, et al. J Neurosci Res. 2002. 67:435.Frankel A, et al. J Biol Chem. 2002. 277:3537.Brahms H, et al. RNA. 2001. 7:1531.Pelletier M, et al. Mol Biochem Parasitol. 2001. 118:49.Belyanskaya LL, et al. J Biol Chem. 2001. 276:18681.Rho J, et al. J Biol Chem. 2001. 276:11393.Scorilas A, et al. Biochem Biophys Res Commun. 2000. 278:349.Frankel A, et al. J Biol Chem. 2000. 275:32974.Zhang X, et al. EMBO J. 19:3509.Tang J, et al. J Biol Chem. 1998. 273:16935.
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