All components in this kit are stable for at least 12 months when stored at the recommended temperature. Upon receipt, 26719S should be stored at 4°C. 9993S should be stored at -20°C. Do not aliquot the antibody.
HS is an enhanced PTMScan®
methodology with improved identification of post-translationally modified peptides. PTMScan®
technology employs a proprietary methodology from Cell Signaling Technology (CST) for peptide enrichment by immunoprecipitation using a specific bead-conjugated antibody in conjunction with liquid chromatography tandem mass spectrometry (LC-MS/MS) for quantitative profiling of post-translational modification (PTM) sites in cellular proteins. PTMs that can be analyzed by PTMScan®
technology include phosphorylation, ubiquitination, acetylation, and methylation, among others. The technology enables researchers to isolate, identify, and quantitate large numbers of post-translationally modified cellular peptides with a high degree of specificity and sensitivity (HS), providing a global overview of PTMs in cell and tissue samples without bias about where the modified sites occur. For more information on PTMScan®
products and services, please visit www.cellsignal.com/applications/proteomics.
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; 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).
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