Lysine succinylation is a post-translational modification (PTM) where a succinyl group, derived from succinyl-CoA, is covalently attached to the lysine residue of a protein. This modification can affect protein function by altering enzyme activity, protein stability, subcellular localization, and protein-protein interactions. It plays a crucial role in regulating cellular metabolism, mitochondrial function, and stress responses, and has been implicated in various diseases such as cancer, neurodegenerative disorders, and metabolic diseases.

Succinylation is typically detected using high-specificity antibody-based enrichment methods that capture succinylated peptides from complex biological samples. These peptides are then analyzed using LC-MS/MS (liquid chromatography-tandem mass spectrometry) to identify and quantify succinylation sites with high sensitivity. The data is further processed through bioinformatics pipelines, which include site-specific quantification, functional annotation, and pathway enrichment analysis to gain deeper insights into succinylation-mediated regulatory mechanisms.

Our succinylation proteomics service can analyze a wide range of biological samples, including animal tissues, plant tissues, cell lines, microorganisms, and biofluids. Whether you are studying metabolic pathways, disease models, or stress responses, our platform is capable of handling diverse sample types to detect succinylation modifications in various biological contexts.

Succinylation, like acetylation and lactylation, is a type of acylation modification, but it involves the transfer of a succinyl group from succinyl-CoA to lysine residues on proteins. While acetylation typically regulates gene expression and chromatin structure, succinylation is more closely associated with metabolic regulation, mitochondrial function, and energy production. Each acylation modification has its unique biological function and regulatory role in different cellular processes, making them key targets for understanding cellular homeostasis and disease mechanisms.

In cancer cells, metabolic reprogramming is a hallmark of tumor growth and survival. Succinylation modifies key metabolic enzymes that control pathways like glycolysis, oxidative phosphorylation, and lipid metabolism, thereby influencing cancer cell proliferation and energy metabolism. By regulating proteins involved in cell cycle progression and apoptosis, succinylation plays a crucial role in tumor progression and the development of chemoresistance, making it an important area of research for cancer therapy.

Integrating succinylation data with global proteomics is crucial for a comprehensive understanding of how succinylation affects cellular processes. By combining succinylation profiling with global protein expression data, researchers can distinguish whether phenotypic changes are driven by altered modification levels (succinylation) or changes in protein expression. This integration enables a deeper analysis of how post-translational modifications (PTMs) like succinylation influence protein function, metabolic reprogramming, and disease progression, providing more accurate and biologically relevant insights into complex cellular phenotypes.