PTMScan® Control Peptides Asymmetric Di-Methyl Arginine #51396
Product Information
Product Usage Information
1. Aliquot PTMScan® Control Peptides Asymmetric Di-Methyl Arginine for storage as single-use units at -20°C or proceed to immediate usage.
2. Resuspend sample peptides in the appropriate buffer and volume, e.g., 1.4 mL of PTMScan® IAP Buffer (1X).
3. Clear sample peptides by centrifugation.
4. Transfer clarified sample peptides to tubes containing IAP beads.
5. Add 10 µL of PTMScan® Control Peptides Asymmetric Di-Methyl Arginine to IAP beads and sample peptides and mix well.
6. Continue with PTMScan® or PTMScan® HS workflows at the 2-hour incubation step.
7. Detect PTMScan® Control Peptides Asymmetric Di-Methyl Arginine in the LCMS data file.
Storage
Product Description
Background
Arginine methylation is a prevalent PTM found on both nuclear and cytoplasmic proteins. Arginine methylated proteins are involved in many different cellular processes, including transcriptional regulation, signal transduction, RNA metabolism, and DNA damage repair (1-3). Arginine methylation is carried out by the arginine N-methyltransferase (PRMT) family of enzymes that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (4). There are three different types of arginine methylation: asymmetric dimethylarginine (aDMA, omega-NG,NG-dimethylarginine), where two methyl groups are placed on one of the terminal nitrogen atoms of the guanidine group of arginine; symmetric dimethylarginine (sDMA, omega-NG,NG-dimethylarginine), where one methyl group is placed on each of the two terminal guanidine nitrogens of arginine; and monomethylarginine (MMA, omega-NG-methylarginine), where a single methyl group is placed on one of the terminal nitrogen atoms of arginine. Each of these modifications has potentially different functional consequences. Though all PRMT proteins catalyze the formation of MMA, Type I PRMTs (PRMT1, 3, 4, 6, and 8) add an additional methyl group to produce aDMA, while Type II PRMTs (PRMT5 and 7) produce sDMA. Methylated arginine residues often reside in glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (5). However, PRMT4/CARM1 and PRMT5 methylate arginine residues within proline-glycine-methionine rich (PGM) motifs (6).
In undifferentiated mouse embryonic neural precursors, sDMA histone H4R3 is prevalent, but in later stages of development, both sDMA and aDMA di-methyl H4R3 modifications are detected in post-mitotic neurons and developing oligodendrocytes. This implies that sDMA modifications may be negative epigenetic regulatory events while aDMA modifications may signal epigenetic activation sites (7).
- Bedford, M.T. and Richard, S. (2005) Mol Cell 18, 263-72.
- Pahlich, S. et al. (2006) Biochim Biophys Acta 1764, 1890-903.
- Bedford, M.T. and Clarke, S.G. (2009) Mol Cell 33, 1-13.
- McBride, A.E. and Silver, P.A. (2001) Cell 106, 5-8.
- Gary, J.D. and Clarke, S. (1998) Prog Nucleic Acid Res Mol Biol 61, 65-131.
- Cheng, D. et al. (2007) Mol Cell 25, 71-83.
- Chittka, A. (2010) PLoS One 5, e13807.
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