PRMT1 (A33) Antibody

2449:

Immunofluorescence , Immunoprecipitation , Western Blotting

PRMT1 (A33) Antibody detects endogenous levels of total PRMT1 protein (all three isoforms). The antibody does not cross-react with other PRMT proteins.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the N-terminus of human PRMT1. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of cell lysates from A549, NIH/3T3, H-4-II-E and COS cells using PRMT1 Antibody.

IF-IC

Confocal immunofluorescent analysis of either untreated HeLa (left), HCT-116 (middle) or SK-OV-3 (right) cells using PRMT1 (A33) Antibody (green). Actin filaments have been labeled with Alexa Fluor^® 555 phalloidin (red).

Protein arginine N-methyltransferase 1 (PRMT1) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). Though all PRMT proteins catalyze the formation of mono-methyl arginine, Type I PRMTs (PRMT1, 3, 4, and 6) add an additional methyl group to produce an asymmetric di-methyl arginine while Type II PRMTs (PRMT 5 and 7) produce symmetric di-methyl arginine (1). Mono-methyl arginine, but not di-methyl arginine, can be converted to citrulline through deimination catalyzed by enzymes such as PADI4 (2). Most PRMTs, including PRMT1, methylate arginine residues found within glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (1). However, PRMT4/CARM1 and PRMT5 methylate arginine residues within PGM (proline-, glycine-, methionine-rich) motifs (3). PRMT1 methylates Arg3 of histone H4 and cooperates synergistically with p300/CBP to enhance transcriptional activation by nuclear receptor proteins (4-6). In addition, PRMT1 methylates many non-histone proteins, including the orphan nuclear receptor HNF4 (6), components of the heterogeneous nuclear ribonucleoprotein (hnRNP) particle (7), the RNA binding protein Sam68 (8), interleukin enhancer-binding factor 3 (ILF3) (9) and interferon-α and β receptors (10). These interactions suggest additional functions in transcriptional regulation, mRNA processing and signal transduction. Alternative mRNA splicing produces three enzymatically active PMRT1 isoforms that differ in their amino-terminal regions (11). PRMT1 is localized to the nucleus or cytoplasm, depending on cell type (12,13) and appears in many distinct protein complexes. ILF3, TIS21 and the leukemia-associated BTG1 proteins bind PRMT1 to regulate its methyltransferase activity (9,14).

1. Bedford, M.T. and Richard, S. (2005) Mol. Cell 18, 263-272.
2. Wang, Y. et al. (2004) Science 306, 279-283.
3. Cheng, D. et al. (2007) Mol. Cell 25, 71-83.
4. Wang, H. et al. (2001) Science 293, 853-857.
5. Strahl, B.D. et al. (2001) Curr. Biol. 11, 996-1000.
6. Barrero, M.J. and Malik, S. (2006) Mol. Cell 24, 233-243.
7. Nichols, R.C. et al. (2000) Exp. Cell Res. 256, 522-532.
8. Côté, J. et al. (2003) Mol. Biol. Cell 14, 274-287.
9. Tang, J. et al. (2000) J. Biol. Chem. 275, 19866-19876.
10. Abramovich, C. et al. (1997) EMBO J. 16, 260-266.
11. Scorilas, A. et al. (2000) Biochem. Biophys. Res. Commun. 278, 349-359.
12. Frankel, A. et al. (2002) J. Biol. Chem. 277, 3537-3543.
13. Herrmann, F. et al. (2005) J. Biol. Chem. 280, 38005-38010.
14. Lin, W.J. et al. (1996) J. Biol. Chem. 271, 15034-15044.

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For Research Use Only. Not For Use In Diagnostic Procedures.