Cell Signaling Technology

Product Pathways - Chromatin Regulation

PRMT1 (F339) Antibody #2453

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Mk (B) Endogenous 41 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  B=Bovine
Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

PRMT1 (F339) Antibody detects endogenous levels of total PRMT1 protein (all three isoforms). The antibody does not cross-react with other PRMT proteins.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to the carboxy terminus of human PRMT1. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

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

Background

Protein arginine N-methyltransferase 1 (PRMT1) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins, which catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). There are two types of PRMT proteins. While both types catalyze the formation of mono-methyl arginine, Type I PRMTs (PRMT1, 3, 4, and 6) add an additional methyl group to produce asymmetric di-methyl arginine and 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 performed by enzymes such as PADI4 (2). Most of the PRMTs, including PRMT1, methylate arginine residues found within glycine-arginine rich (GAR) domains of proteins, such as RGG, RG, and RXR repeats (1). However, PRMT4/CARM1 and PRMT5 instead 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 (4,5,6). 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), suggesting additional functions in transcriptional regulation, mRNA processing and signal transduction. Alternative mRNA splicing results in three enzymatically active isoforms of PMRT1 protein that differ in their amino terminal regions (11). PRMT1 is localized in 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 to PRMT1 and 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. 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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This product is for in vitro research use only and is not intended for use in humans or animals. This product is not intended for use as therapeutic or in diagnostic procedures.

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