Render Target: SSR
Render Timestamp:
10/15/2026, 9:05:53 PM EDT
10/16/2026, 1:05:53 AM UTC
Commit: 6bb8e03c04ff513ea8e7325ce35abd2ab0759b0e
XML generation date: 2026-10-13 20:21:23.321
Product last modified at: 2026-10-14T07:00:56.973Z
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PDP - Template Name: PTMScan (with Pricing)
PDP - Template ID: *******57cbce3
  1. Products /
  2. Proteomic Analysis Products /
  3. PTMScan® HS Pilot Acetyl-Lysine Motif (Ac-K) Kit

PTMScan® HS Pilot Acetyl-Lysine Motif (Ac-K) Kit #50071

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

    Acetylation of lysine, like phosphorylation of serine, threonine or tyrosine, is an important reversible modification controlling protein activity. The conserved amino-terminal domains of the four core histones (H2A, H2B, H3, and H4) contain lysines that are acetylated by histone acetyltransferases (HATs) and deacetylated by histone deacetylases (HDACs) (1). Signaling resulting in acetylation/deacetylation of histones, transcription factors, and other proteins affects a diverse array of cellular processes including chromatin structure and gene activity, cell growth, differentiation, and apoptosis (2-6). Recent proteomic surveys suggest that acetylation of lysine residues may be a widespread and important form of post-translational protein modification that affects thousands of proteins involved in control of cell cycle and metabolism, longevity, actin polymerization, and nuclear transport (7,8). The regulation of protein acetylation status is impaired in cancer and polyglutamine diseases (9), and HDACs have become promising targets for anti-cancer drugs currently in development (10).

    Limited Uses

    Except as otherwise expressly agreed in a writing signed by a legally authorized representative of CST, the following terms apply to Products provided by CST, its affiliates or its distributors. Any Customer's terms and conditions that are in addition to, or different from, those contained herein, unless separately accepted in writing by a legally authorized representative of CST, are rejected and are of no force or effect.

    Products are labeled with For Research Use Only or a similar labeling statement and have not been approved, cleared, or licensed by the FDA or other regulatory foreign or domestic entity, for any purpose. Customer shall not use any Product for any diagnostic or therapeutic purpose, or otherwise in any manner that conflicts with its labeling statement. Products sold or licensed by CST are provided for Customer as the end-user and solely for research and development uses. Any use of Product for diagnostic, prophylactic or therapeutic purposes, or any purchase of Product for resale (alone or as a component) or other commercial purpose, requires a separate license from CST. Customer shall (a) not sell, license, loan, donate or otherwise transfer or make available any Product to any third party, whether alone or in combination with other materials, or use the Products to manufacture any commercial products, (b) not copy, modify, reverse engineer, decompile, disassemble or otherwise attempt to discover the underlying structure or technology of the Products, or use the Products for the purpose of developing any products or services that would compete with CST products or services, (c) not alter or remove from the Products any trademarks, trade names, logos, patent or copyright notices or markings, (d) use the Products solely in accordance with CST Product Terms of Sale and any applicable documentation, and (e) comply with any license, terms of service or similar agreement with respect to any third party products or services used by Customer in connection with the Products.

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