Succinylation Analysis Service

Protein succinylation is a post-translational modification that introduces a succinyl group to lysine residues, dramatically altering the charge and structural properties of proteins. This modification has emerged as a critical regulator of metabolic processes, gene expression, and disease progression. MtoZ Biolabs delivers a Succinylation Analysis Service that moves from carefully matched sample preparation and selective enrichment through high resolution LC-MS/MS acquisition to rigorous data preprocessing, site localization, and systems level interpretation. 

1. Target Protein Succinylation Analysis

This service is designed for detailed investigation of succinylation on individual proteins of interest. MtoZ Biolabs identifies modification sites with high accuracy and quantifies site occupancy under varying biological conditions. This focused approach helps elucidate how succinylation modulates the function, localization, or stability of specific metabolic enzymes or regulatory proteins.

2. Succinylation Proteomics

For broader discovery-driven studies, MtoZ Biolabs offers succinylation proteomics, enabling comprehensive mapping of succinylated proteins across the entire proteome. This global strategy uncovers large-scale succinylation patterns, reveals cross-talk with other acyl modifications, and provides systems-level insight into the metabolic and signaling pathways governed by succinylation.

What Is Succinylation?

Lysine succinylation (Ksucc) is a reversible and evolutionarily conserved post-translational modification that introduces a succinyl group onto the amino group of lysine residues. This reaction alters the local charge from positive to negative, introducing significant structural and functional changes in proteins. Succinylation was first identified in histones but has since been found in a wide range of metabolic enzymes and regulatory proteins across prokaryotes and eukaryotes.

This process can occur through both non-enzymatic and enzymatic pathways. In the non-enzymatic mechanism, succinyl-CoA serves as the acyl donor and reacts directly with lysine residues. As a central metabolic intermediate, succinyl-CoA is primarily derived from the tricarboxylic acid (TCA) cycle, amino acid catabolism, fatty acid metabolism, and porphyrin biosynthesis. The dynamic balance of succinylation is maintained by desuccinylases such as SIRT5, which remove succinyl groups and restore protein activity. In the enzymatic mechanism, certain succinyltransferases, such as KAT2A, HAT1, and CPT1A, are able to catalyze the transfer of succinyl groups to lysine residues, enhancing the regulation of specific substrates. This enzyme-mediated process provides an additional layer of control, linking succinylation to precise cellular pathways.

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Adejor, J. et al. Curr Issues Mol Biol. 2024.

Figure 1. Process of Lysine Succinylation

Recent studies have shown that succinylation influences chromatin remodeling, mitochondrial energy metabolism, oxidative stress response, and cellular differentiation. Dysregulation of succinylation has been associated with cancer, cardiovascular disease, metabolic disorders, and neurodegeneration. With the advancement of high-resolution LC-MS/MS technologies and enrichment-based proteomics, large-scale succinylomes have been mapped, providing new insights into this important PTM.

Analysis Workflow

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Sample Submission Suggestions

1. Sample Types

We accept various biological sample types, including but not limited to:

  • Cultured cells

  • Microorganism samples

  • Animal or human tissue

  • Plant tissue

  • Biological fluids such as plasma or serum

  • Protein extracts

2. Storage and Transport

  • Samples should be snap-frozen in liquid nitrogen and stored at –80°C until shipment.

  • Ship samples on dry ice.

  • Avoid repeated freezethaw cycles.

*Note: If you have special sample types or require additional guidance, please contact us for personalized support before sample preparation.

Service Advantages

1. Advanced Analysis Platform: MtoZ Biolabs established an advanced Succinylation Analysis Service platform, guaranteeing reliable, fast, and highly accurate analysis service.

2. One-Time-Charge: Our pricing is transparent, no hidden fees or additional costs.

3. High-Data-Quality: Deep data coverage with strict data quality control. AI-powered bioinformatics platform integrates all succinylation analysis data, providing clients with a comprehensive data report.

Applications

The Succinylation Analysis Service at MtoZ Biolabs supports diverse areas of biological and biomedical research:

1. Metabolic Regulation

Linking succinylation events to mitochondrial function, the TCA cycle, and energy homeostasis, helping to reveal how metabolism shapes protein activity.

2. Epigenetic Research

Investigating histone succinylation and its role in chromatin remodeling, gene expression, and transcriptional regulation.

3. Signal Transduction

Profiling succinylated signaling proteins to uncover how this modification modulates pathways controlling cell growth, stress response, and communication.

4. Disease Mechanism Studies

Characterizing succinylation changes associated with cancer, neurodegeneration, and cardiovascular disorders.

5. Biomarker Discovery and Drug Development

Identifying succinylation-based biomarkers and potential therapeutic targets for translational medicine.

Deliverables

1. Comprehensive Experimental Details

2. Materials, Instruments, and Methods

3. The Detailed Information of Succinylation Analysis

4. Mass Spectrometry Image

5. Bioinformatics Analysis

6. Raw Data

Succinylation represents a key regulatory layer that links metabolism with gene regulation, protein function, and disease. With state-of-the-art mass spectrometry, robust enrichment methods, and expert interpretation, MtoZ Biolabs' Succinylation Analysis Service provides a comprehensive and reliable platform for researchers to study this important PTM, driving discoveries in basic biology, disease research, and translational medicine. Free project evaluation, welcome to learn more details!

    

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