Render Target: SSR
Render Timestamp:
10/15/2026, 9:05:38 PM EDT
10/16/2026, 1:05:38 AM UTC
Commit: 6bb8e03c04ff513ea8e7325ce35abd2ab0759b0e
XML generation date: 2026-10-13 20:21:23.221
Product last modified at: 2026-10-14T07:01:00.457Z
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PDP - Template Name: PTMScan (with Pricing)
PDP - Template ID: *******57cbce3

PTMScan® HS Succinyl-Lysine Motif (Succ-K) Kit #60724

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

    Lysine is subject to a wide array of regulatory post-translational modifications due to its positively charged ε-amino group side chain. The most prevalent of these are ubiquitination and acetylation, which are highly conserved among prokaryotes and eukaryotes (1,2). Acyl group transfer from the metabolic intermediates acetyl-, succinyl-, malonyl-, glutaryl-, butyryl-, propionyl-, and crotonyl-CoA all neutralize lysine’s positive charge and confer structural alterations affecting substrate protein function. Lysine acetylation is catalyzed by histone acetyltransferases, HATs, using acetyl-CoA as a cofactor (3,4). Deacylation is mediated by histone deacetylases, HDACs 1-11, and NAD-dependent Sirtuins 1-7. Some sirtuins have little to no deacetylase activity, suggesting that they are better suited for other acyl lysine substrates (5).

    SirT5 is a predominantly mitochondrial desuccinylase and demalonylase (5,6). In the absence of a known succinyltransferase, succinylation is likely driven by the concentration of succinyl-CoA and intracellular pH and is subject to metabolic fluctuations (7,8). Protein succinylation is especially prevalent among mitochondrial metabolic proteins and bacteria, further solidifying the evolutionary link between mitochondria and prokaryotes. It often occurs at lysine residues that are alternatively acetylated or ubiquitinated. More than a thousand lysine succinylation sites were identified on hundreds of proteins, including glutamate dehydrogenase (15 sites), malate dehydrogenase, citrate synthase, carbamoyl phosphate synthase 1, and histone proteins (9).
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