Identification of Lactylation Modification Sites in Proteins

Protein lysine lactylation is a novel post-translational modification (PTM) widely present in the cells of fungi and mammals (such as humans and mice), which directly stimulates gene transcription and significantly affects downstream gene expression and DNA replication. Understanding the roles and regulatory mechanisms of lysine lactylation in physiological and pathological processes highly dependent on glycolysis and lactic acid is crucial.

 

Services at Mtoz Biolabs

1. Mass Spectrometry (MS)

MS technology is one of the main methods for identifying protein lactylation modification sites. With a high-resolution mass spectrometer, such as the Orbitrap Fusion Lumos mass spectrometer, the mass of the modified protein or peptide can be accurately determined, thereby inferring the type and location of the modification. Combined with enzymatic digestion and nano-liquid chromatography (Nano-LC) technology, the separation efficiency and identification sensitivity of the sample can be improved.

 

2. Nuclear Magnetic Resonance (NMR)

NMR technology can provide structural information of proteins or peptides, including the exact location of the modification site and the structural details of the surrounding environment. For lactylation modification, NMR can help determine the impact of the modification on the three-dimensional structure of the protein.

 

3. Tandem Mass Spectrometry (MS/MS)

Through MS/MS technology, selected peptide ions can be further decomposed during the mass spectrometry analysis process to obtain more detailed sequence information, including the exact location of the modification. Combined with specific data analysis software and databases, lactylation modification sites can be identified automatically.

 

4. Bioinformatics Tools

With the rapid development of mass spectrometry data and protein databases, many bioinformatics tools and algorithms have been developed for analyzing and predicting protein lactylation modification sites. These tools can predict potential lactylation sites based on known modification patterns, protein sequences, and structural information.

 

In addition to the above methods, there are other techniques and methods to identify the lactylation sites of proteins, such as immunofluorescence, immunoblotting, etc., but mass spectrometry technology is the most accurate and high-throughput method.

 

MtoZ Biolabs has developed an efficient proteomics technology based on Mass Spectrometry (MS) for the whole system identification and quantification of PTM substrates and mapping their sites. For lysine lactylation analysis, we will combine immunoprecipitation based on anti-lactic acid antibody with liquid chromatography-tandem mass spectrometry (LC-MS/MS) technology. We use a series of enzymatic and chemical cleavage methods and extensive fractionation to maximize proteome sequence coverage. In addition, our bioinformatics platform can help understand the functional relevance of protein lactylation in cellular physiology. Free project evaluation，Welcome to learn more details!