antibody

PRMT1 (Protein arginine N Methyltransferase 1, ANM1, HCP1, HRMT1L2, IR1B4)

P9004-02B

100 ul

polyclonal

domestic rabbit

nonconjugated

PRMT1 (Protein arginine N Methyltransferase 1, ANM1, HCP1, HRMT1L2, IR1B4)

rabbit

Pab

Antibodies

100 ul

IgG

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 beta receptors (10). These interactions suggest additional functions in transcriptional regulation, mRNA processing and signal transduction. Alternative mRNA splicing produces three enzymatically active PRMT1 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). Applications: Suitable for use in Immunofluorescence (IF-IC), Western Blot, Immunoprecipitation. Other applications not tested. Recommended Dilution: Western Blot: 1:1000 Immunoprecipitation: 1:50 Immunofluorescence (IF-IC): 1:100 Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. For long-term storage, store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Hu Mk Mo Rt

Synthetic peptide corresponding to the N-terminus of human PRMT1 (KLH). Species Sequence Homology: bovine

Detects endogenous levels of total human PRMT1(~41kD) protein (all three isoforms). Does not crossreact with other PRMT proteins. Species Crossreactivity: mouse, monkey and rat.

Purified by Protein A and peptide affinity chromatography.

Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol.

Not determined

Product Type: Pab Isotype: IgG Host: rabbit Source: human Concentration: Not determined Form: Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol. Purity: Purified by Protein A and peptide affinity chromatography. Immunogen: Synthetic peptide corresponding to the N-terminus of human PRMT1 (KLH). Species Sequence Homology: bovine Specificity: Detects endogenous levels of total human PRMT1(~41kD) protein (all three isoforms). Does not crossreact with other PRMT proteins. Species Crossreactivity: mouse, monkey and rat. Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

IF IP WB

-20°C

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. Cote, 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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