PTMScan® Formyl Lysine Motif (For-K) Kit #25217
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.
Product Information
Storage
Antibody beads supplied in IAP buffer containing 50% glycerol. Store at -20°C. Do not aliquot the antibody.
实验步骤
Product Description
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 (LC) tandem mass spectrometry (MS/MS) for quantitative profiling of posttranslational modification (PTM) sites in cellular proteins. These include phosphorylation, ubiquitination, acetylation, and methylation, among others. PTMScan® Technology enables researchers to isolate, identify, and quantitate large numbers of posttranslationally modified cellular peptides with a high degree of specificity and sensitivity, providing a global overview of PTMs in cell and tissue samples without preconceived biases about where these modified sites occur. For more information on PTMScan® products and services, please visit Proteomics Resource Center.
Background
Lysine formylation (For-K), also known as N6-formyl-lysine, is a posttranslational modification (PTM) that occurs on the nitrogen atom of the lysine side chain. This PTM differs from N-terminal formylation that occurs in the context of initiation of prokaryotic translation and gramicidin production (1,2).
Unlike other acyl-modifications on proteins, such as acetyl or succinyl lysine, formyl lysine is not primarily derived from an analogous coenzyme A metabolite. Instead, formyl lysine can be derived from diverse molecules, including peroxynitrite, 3'-formylphosphate, trichloroethylene oxide, and formaldehyde, and this PTM has been proposed as a biomarker for formaldehyde inhalation (3-7). Due to the various chemicals that can induce formylation, users should carefully consider their experimental workflows to avoid introducing spurious formyl lysines that can confound bona fide endogenous formyl lysine sites (8). Previous studies have identified formyl lysine sites on tau, histones, other non-histone chromatin factors, and milk proteins (3,9-11). In the context of tau, one proposed effect of this PTM is polymerization inhibition (3).
Unlike other acyl-modifications on proteins, such as acetyl or succinyl lysine, formyl lysine is not primarily derived from an analogous coenzyme A metabolite. Instead, formyl lysine can be derived from diverse molecules, including peroxynitrite, 3'-formylphosphate, trichloroethylene oxide, and formaldehyde, and this PTM has been proposed as a biomarker for formaldehyde inhalation (3-7). Due to the various chemicals that can induce formylation, users should carefully consider their experimental workflows to avoid introducing spurious formyl lysines that can confound bona fide endogenous formyl lysine sites (8). Previous studies have identified formyl lysine sites on tau, histones, other non-histone chromatin factors, and milk proteins (3,9-11). In the context of tau, one proposed effect of this PTM is polymerization inhibition (3).
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- Jiang, T. et al. (2007) Proc Natl Acad Sci USA 104, 60-5.
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- Osés-Prieto, J.A. et al. (2007) Mol Cell Proteomics 6, 181-92.
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- Milkovska-Stamenova, S. and Hoffmann, R. (2019) Amino Acids 51, 891-901.
限制使用
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For Research Use Only. Not for Use in Diagnostic Procedures.
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