Render Target: SSR
Render Timestamp:
10/15/2026, 9:06:03 PM EDT
10/16/2026, 1:06:03 AM UTC
Commit: 6bb8e03c04ff513ea8e7325ce35abd2ab0759b0e
XML generation date: 2026-10-13 20:21:23.077
Product last modified at: 2026-10-14T07:00:59.488Z
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PDP - Template Name: PTMScan (with Pricing)
PDP - Template ID: *******57cbce3

PTMScan® HS Pilot Mono-Methyl Arginine Motif (mme-RG) Kit #87654

Additional Information

This product is intended for peptide enrichment and mass spectrometry analysis. To learn more about our Proteomics Kits and Services please answer a few questions for our Proteomics group.

Contact the CST Proteomics Group

    Product Information

    Storage

    Please store the components at the temperatures indicated on the individual tube labels. Do not aliquot the antibody.

    Protocol

    Product Description

    PTMScan® HS (High Sensitivity) is an enhanced PTMScan methodology with improved identification of post-translationally modified (PTM) peptides. PTMScan technology employs a proprietary methodology from Cell Signaling Technology (CST) for peptide enrichment by immunoprecipitation using a specific magnetic bead-conjugated antibody in conjunction with liquid chromatography-tandem mass spectrometry (LC-MS/MS) for quantitative profiling of PTM sites in cellular proteins. PTMs analyzed using this technology include phosphorylation, ubiquitination, acetylation, and methylation, among others. The methodology enables researchers to isolate, identify, and quantify large numbers of PTM cellular peptides with high specificity and sensitivity. The workflow provides a global, unbiased overview of PTMs across cell and tissue samples of any species, regardless of modification site location. For more information on PTMScan products and services, please visit the Proteomics Resource Center.

    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).
    For Research Use Only. Not for Use in Diagnostic Procedures.
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