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PTMScan® HS Succinyl-Lysine Motif (Succ-K) Kit
Proteomic Analysis Products

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

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PTMScan® HS Succinyl-Lysine Motif (Succ-K) Kit: Image 1
Motif analysis using all succinyl lysine peptides enriched and identified by PTMScan® HS Succinyl-Lysine Motif (Succ-K) Kit from three different samples. One milligram each of mouse embryo, mouse liver, and HCT 116 human colon cancer cells were independently digested with trypsin and immunoprecipitated with PTMScan® HS Succinyl-Lysine Magnetic Immunoaffinity Beads. Orbitrap Q Exactive mass spectrometer analysis identified a total of 4,440 non-redundant sites. The motif logo shows that the Succ-K antibody is a general motif antibody that recognizes the Succ-K motif independent of protein context, without other amino acid preferences.
Product Includes Volume (with Count)
PTMScan® HS Succinyl-Lysine (Succ-K) Magnetic Immunoaffinity Beads 1 x 200 µl
PTMScan® HS Immunoaffinity Purification (IAP) Bind Buffer #1 (1X) 1 x 25 ml
PTMScan® HS Immunoaffinity Purification (IAP) Wash Buffer (1X) 1 x 50 ml


All components in this kit are stable for at least 12 months when stored at the recommended temperature. Upon receipt, 37868S should be stored at 4°C. 25144S and 42424S should be stored at -20°C. Do not aliquot the antibody.

Product Description

PTMScan® 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 Proteomics Resource Center.


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).

Limited Uses

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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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