Product Pathways - Screening Technologies
Mono-Methyl Arginine (Me-R4-100) Rabbit mAb #8015
|8015S||100 µl (10 western blots)||---||In Stock||---|
|8015||carrier free and custom formulation / quantity||email request|
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|W||1:1000||All Species Expected||Endogenous||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation, E-P=ELISA (Peptide)
Specificity / Sensitivity
Mono-Methyl Arginine (Me-R4-100) Rabbit mAb recognizes endogenous levels of mono-methyl arginine protein. This is a general mono-methyl arginine motif antibody without sequence preferences. It does not cross-react with di-methyl arginine or unmethylated arginine.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide library containing mono-methyl arginine surrounded by degenerate amino acids. The antibody is formulated from four rabbit monoclones in order to cover a broad range of reactivity.
Western blot analysis of extracts from various mouse tissues using Mono-Methyl Arginine (Me-R4-100) Rabbit mAb.
Western blot analysis of extracts from HCT 116 cells using Mono-Methyl Arginine (Me-R4-100) Rabbit mAb. Specific signals are blocked by mono-methyl arginine antigen peptide, but not by non-methyl arginine control peptide.
Immunoprecipitation of HCT 116 cell lysate using Mono-Methyl Arginine (Me-R4-100) Rabbit mAb or Rabbit (DA1E) mAb IgG XP® Isotype Control #3900. Western blot detection was performed with Mono-Methyl Arginine (Me-R4-100) Rabbit mAb. 10% input is shown in lane 1.
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,N’G-dimethylarginine), where one methyl group is placed on each of the two terminal guanidine nitrogens of arginine; and monomethylarginine (MMA, omega-NG-dimethylarginine), 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, and 6) 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).
- 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.
- Dhar, S. et al. (2013) Sci Rep 3, 1311.
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