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Render Timestamp:
10/15/2026, 8:22:42 PM EDT
10/16/2026, 12:22:42 AM UTC
Commit: 6bb8e03c04ff513ea8e7325ce35abd2ab0759b0e
XML generation date: 2026-08-27 20:20:14.221
Product last modified at: 2026-08-28T07:00:55.661Z
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PDP - Template Name: PTMScan (with Pricing)
PDP - Template ID: *******57cbce3

PTMScan® Phospho-ATM/ATR Substrate Motif [pSQ] Kit #12267

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

    Product Usage Information

    Cells are lysed in a urea-containing buffer, cellular proteins are digested by proteases, and the resulting peptides are purified by reversed-phase solid-phase extraction. Peptides are then subjected to immunoaffinity purification using a PTMScan® Motif Antibody conjugated to protein A agarose beads. Unbound peptides are removed through washing, and the captured PTM-containing peptides are eluted with dilute acid. Reversed-phase purification is performed on microtips to desalt and separate peptides from antibody prior to concentrating the enriched peptides for LC-MS/MS analysis. CST recommends the use of PTMScan® IAP Buffer #9993 included in the kit.

    Storage

    Antibody beads supplied in IAP buffer containing 50% glycerol. Store at -20°C. Do not aliquot the antibody.

    Protocol

    Product Description

    PTMScan® technology employs a proprietary methodology from Cell Signaling Technology (CST) for post-translationally modified (PTM) peptide enrichment by immunoprecipitation using a specific agarose 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. 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

    PhosphoScan® Technology employs a phospho-residue (Tyr, Ser, Thr) motif antibody for phospho-peptide immunoaffinity purification from cell extracts combined with LC tandem MS/MS to identify and quantify changes in phosphorylation levels (1). Ataxia telangiectasia mutated kinase (ATM) and ataxia telangiectasia and Rad3-related kinase (ATR) are related kinases that regulate cell cycle checkpoints and DNA repair (2). The identified substrates for ATM are p53, p95/NBS1, MDM2, Chk2, BRCA1, CtIP, 4E-BP1, and Chk1 (2,3). The consensus sequence for ATM/ATR substrates is [pS/pTQ]. Hydrophobic amino acids at positions -3 and -1, and negatively charged amino acids at position +1 are positive determinants for substrate recognition by these kinases. Positively charged residues surrounding the [pS/pTQ] are negative determinants for substrate phosphorylation (4). The complex phenotype of AT cells suggests that it likely has additional substrates (4). To better understand the kinase and identify substrates for ATM and the related kinase ATR, we have developed antibodies that recognize phosphorylated serine or threonine in the [pS/pTQ] motif.
    For Research Use Only. Not for Use in Diagnostic Procedures.
    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    AcetylScan is a registered trademark of Cell Signaling Technology, Inc.
    MethylScan is a registered trademark of Cell Signaling Technology, Inc.
    NAThis product is supplied and sold under certain patents owned by Active Motif, US patents 9938524, 10689643, 11306307 and 12049622, and related patents in other countries, for purchaser’s internal research only, and may not be used for any commercial purpose, including the provision of services.
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