PTMScan® Lactyl Lysine Motif (K-La) Kit #83284
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 post-translational 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 post-translationally 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
Lactyl lysine (lactylation) is a reversible post-translational modification (PTM) that occurs on the ε-amino group of the lysine side chain. Originally discovered on histone proteins, lactylation has been documented on non-histone proteins, including ATRX and PARP1 (1,2).
Lactyl lysine exists as two stereoisomers: KL-la and KD-la, though the chief form in mammalian cells is the L stereoisomer KL-la (S configuration). EP300 and KAT2A are among the known enzymes that utilize lactyl-coenzyme A (lactyl-CoA) to lactylate proteins, while SIRT3 and HDAC1 have been documented to remove lactylation (3,4). These enzymes regulate other lysine acyl PTMs, most notably lysine acetylation. However, the regulatory pathways of lactylation differ in several aspects from analogous pathways of acetylation. For example, ACSS2 converts lactate into lactyl-CoA through a cascade of ERK signaling and PIN2 isomerization. While ACSS2 can similarly process acetate into lactyl-CoA, the ACSS2 residues responsible for binding differ from the residues for binding lactate (5). In another example, AARS1 can directly conjugate lactate to proteins without generating a lactyl-CoA donor (6).
Lactate is involved in diverse biological contexts, such as accumulation in brain tissue during cerebral ischemia-reperfusion injury and aerobic glycolysis in cancer. Lactylation roles are likely equally diverse and potentially distinct from acetylation (7). Interestingly, few domains that otherwise bind acetylated lysines have been found to bind lactylated lysines. One known lactyl lysine binder is TRIM33, where a conserved glutamate within the TRIM33 bromodomain is necessary and sufficient for binding to lactylated histones, yet does not affect binding to acetylated histones (8). Differentiating the unique regulation and impact of lactylation from other acyl PTMs remains an active and important area of research.
Lactyl lysine exists as two stereoisomers: KL-la and KD-la, though the chief form in mammalian cells is the L stereoisomer KL-la (S configuration). EP300 and KAT2A are among the known enzymes that utilize lactyl-coenzyme A (lactyl-CoA) to lactylate proteins, while SIRT3 and HDAC1 have been documented to remove lactylation (3,4). These enzymes regulate other lysine acyl PTMs, most notably lysine acetylation. However, the regulatory pathways of lactylation differ in several aspects from analogous pathways of acetylation. For example, ACSS2 converts lactate into lactyl-CoA through a cascade of ERK signaling and PIN2 isomerization. While ACSS2 can similarly process acetate into lactyl-CoA, the ACSS2 residues responsible for binding differ from the residues for binding lactate (5). In another example, AARS1 can directly conjugate lactate to proteins without generating a lactyl-CoA donor (6).
Lactate is involved in diverse biological contexts, such as accumulation in brain tissue during cerebral ischemia-reperfusion injury and aerobic glycolysis in cancer. Lactylation roles are likely equally diverse and potentially distinct from acetylation (7). Interestingly, few domains that otherwise bind acetylated lysines have been found to bind lactylated lysines. One known lactyl lysine binder is TRIM33, where a conserved glutamate within the TRIM33 bromodomain is necessary and sufficient for binding to lactylated histones, yet does not affect binding to acetylated histones (8). Differentiating the unique regulation and impact of lactylation from other acyl PTMs remains an active and important area of research.
- Zhang, D. et al. (2019) Nature 574, 575-580.
- Bao, Q. et al. (2024) J Am Soc Mass Spectrom 35, 3221-3232.
- Moreno-Yruela, C. et al. (2022) Sci Adv 8, eabi6696.
- Fan, Z. et al. (2023) iScience 26, 107757.
- Zhu, R. et al. (2025) Cell Metab 37, 361-376.e7.
- Ju, J. et al. (2024) J Clin Invest 134, e174587. doi: 10.1172/JCI174587.
- Shi, P. et al. (2025) Front Cell Dev Biol 13, 1535611.
- Nuñez, R. et al. (2024) ACS Chem Biol 19, 2418-2428.
限制使用
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