Lactylation Modification Proteomics Service
Lactylation is an emerging post-translational modification (PTM) of proteins, wherein lactic acid molecules are covalently attached to lysine residues of proteins under enzymatic catalysis, using lactyl-coenzyme A (Lactyl-CoA) as the donor. This modification regulates protein charge states, three-dimensional structures, and functional properties, thereby participating in the modulation of gene expression, cellular signal transduction, metabolic reprogramming, and epigenetic regulation across multiple biological processes.
Figure 1. Different epigenetic mechanisms of protein lactylation. (Source: Lu Z, et al. 2024)
Our lactylation proteomics platform integrates advanced high-resolution mass spectrometry technology with in-depth bioinformatics analysis, providing comprehensive and highly sensitive lactylation identification and quantification services. We help research teams explore the mechanisms underlying lactylation in disease development and progression.
Our Services
The formation of lactylation modification involves the following steps:
- Substrate Preparation: Lactic acid is converted to lactyl-coenzyme A (Lactyl-CoA) under enzymatic catalysis with CoA
- Modification Transfer: Lactyl-CoA transferase catalyzes the transfer of the lactyl group to the ε-amino group of lysine residues on proteins
- Mass Shift: The modification causes a mass shift of 72.021 Da, which can be precisely detected via mass spectrometry
Service Content
| Service Item | Service Description |
| Modification Site Identification | Simultaneous detection of lactylated peptide segments on histones and non-histone proteins; precise localization of lysine residues undergoing lactylation; comprehensive coverage of modification sites |
| Quantitative Analysis | Label-free quantification based on peptide ion intensity; accurate capture of lactylation modification dynamics under different biological conditions; support for time-series analysis |
| Bioinformatics Analysis | Functional pathway annotation and enrichment analysis of lactylated proteins; construction of protein-protein interaction networks for modified proteins; identification of conserved amino acid motifs at modification sites |
| Multi-level Integrated Analysis | Integrated analysis of lactylated proteins with transcriptomics and metabolomics data; mining of associations between modifications and cellular phenotypes or disease states; prioritization of candidate disease biomarker proteins |
Service Advantages
We have established a comprehensive lactylation modification detection and analysis system that employs high-resolution mass spectrometry platforms to ensure detection accuracy, leverages specific antibody enrichment technology to enhance the detection efficiency of modified peptide segments, and implements rigorous quality control throughout the experimental workflow. Based on your specific research objectives, we flexibly design experimental schemes and analytical strategies, providing detailed technical reports, raw data, and downstream analysis support to ensure you can fully understand and maximize the value of your research outcomes. Our project timelines are transparent and controllable, with professional project management teams tracking progress at every stage to ensure high-quality, on-time completion.
Workflow
We thoroughly understand your research objectives, sample types, and sample quantities, assess whether sample quality meets detection requirements, and develop a personalized detection and analysis plan based on your specific needs.
We receive and assess sample quality, perform protein extraction, quantification, and enzymatic digestion, conduct specific enrichment of lactylated peptide segments, perform high-resolution detection using LC-MS/MS, and conduct quality assessment and quality control monitoring of raw data.
We perform database searching and peptide matching of raw spectra, execute modification site identification and confidence evaluation, complete quantitative analysis and statistical processing, conduct in-depth bioinformatics analysis, and generate comprehensive reports with visualization graphics.
We provide detailed methodology documentation and raw data, offer technical explanations regarding analysis results, assist with publication support and academic writing suggestions, and support any follow-up analysis requirements.
Considerations
- Modification Specificity: Lactylation occurs exclusively on lysine residues of proteins; modifications at other sites cannot be detected through this service.
- Enzyme Information: The mass spectrometry platform only provides identification of modification events and does not directly measure lactyl-CoA transferase activity.
- Protein Degradation: Severely degraded samples will significantly compromise detection efficiency; please ensure sample freshness and integrity.
- Tissue Specificity: Lactylation modification profiles differ significantly across different tissues/cells; inferences across different sample types should be made cautiously
- Statistical Interpretation: Changes in modification abundance do not necessarily correspond to equivalent changes in biological function; conclusions should be supported by subsequent validation
Reference
- Lu Z, et al. Lactylation: The emerging frontier in post-translational modification. Front Genet. 2024 Jun 27;15:1423213.
