| CatalogCode: | | NB120-12190 |
| ProductName: | | PRMT3 Antibody |
| Product Description: | | Mouse Monoclonal anti-PRMT3 (PRMT3-367) |
| Clone: | | PRMT3-367 |
| Clonality: | | Monoclonal |
| Immunogen: | | Synthetic peptide: TVHKNKKDPRSLIV conjugated to KLH, corresponding to amino acids 501-514 of Rat PRMT3. |
| Epitope: | | The antibody epitope resides within amino acids 501-514 of rat PRMT3. |
| Specificity: | | Ab12190 does not cross react with PRMT1, 2, 4, 5, or 6. |
| CrossReactivity: | | Expected to cross-react with Mouse (100% identity with immunogen), Rat (100% identity with immunogen) and Human (92% identity with immunogen) due to sequence homology.Not yet tested in other species. |
| Packaging: | | 0.05 ml purified Mouse IgG. |
| Uses: | | ELISA: Use at an assay dependent dilution. ICC: Use at an assay dependent dilution. WB: Use at a concentration of 1 - 2 ug/ml. This concentration is recommended using a whole cell extract of the 293T cell line transfected with human PRMT3.Predicted molecular weight: 58 kDa. Not tested in other applications.Optimal dilutions/concentrations should be determined by the end user. |
| Localization: | | Cytoplasmic |
| Control: | | 293T cell line transfected with human PRMT3. |
| 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 (Histone-2A, 3, 4), IL enhancer binding factor, nuclear factors (NF-45, -90, ILF3, Nucleolin, STAT1, Poly(A)-binding protein II), cell cycle proteins (phosphoprotein phosphatase 2A), signal transduction proteins (FGF2, Fibrillarin, FN, INFAR1, Jak, MBP, Src-adaptor Sam68), apoptosis proteins (FADD, ICE-like protease), and viral proteins (Hepatitis C NS3 RNA Helicase, HIV TAR). The mammalian PRMT family currently consists of 5 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all five PRMT members have been developed. These antibodies can be utilized to explore arginine methylation and its regulatory functions. |
| Storage: | | Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. |
| Purity: | | IgG purified |
| Isotype: | | IgG3 |
| Host_Name: | | Mouse |
| Buffer: | | Preservative: 15mM Sodium Azide Constituents: 0.01M PBS. pH 7.4 |
| ListPrice: | | 285 |
| AppSummary: | | ELISA, ICC, WB |
| SpeciesSummary: | | Hu, Mu, Rt |
| ALTnames: | | anti-PRMT1 antibody, anti-PRMT-1 antibody, anti-Protein Arginine N-Methyltransferase 1 antibody, anti-HRMT1L2 antibody, anti-HMT1 hnRNP Methyltransferase-like 2 antibody, anti-ANM1 antibody, anti-Arginine N-Methyltransferase 1 antibody, anti-IR1B4 antibody, anti-Interferon Receptor 1-Bound Protein 4 antibody, anti-H |
| ProteinTarget: | | PRMT3 |
| PackageSize: | | 0.05 ml |
| GeneralRef: | | General / background references:Frankel A et al. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J Biol Chem 277:3537-43 (2002). Rho J et al. Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family. J Biol Chem 276:11393-401 (2001). Frankel A & Clarke S PRMT3 is a distinct member of the protein arginine N-methyltransferase family. Conferral of substrate specificity by a zinc-finger domain. J Biol Chem 275:32974-82 (2000). Tang J et al. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J Biol Chem 273:16935-45 (1998). |
| NotesMain: | | Storage in frost-free freezers is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. |
| more information: | | company product webpage |
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