Malonylation Proteomics Service
Malonylation is a newly discovered and functionally significant post-translational modification that primarily occurs on lysine residues. With the rapid advancement of proteomics and mass spectrometry technologies, malonylation has emerged as an important member of the histone lysine acylation modification family, demonstrating increasing research value. Malonylation plays a central role in cellular metabolic regulation. This modification uses malonyl-CoA as a donor to covalently attach a malonyl group to lysine residues on target proteins, thereby participating in the regulation of multiple key biological processes including protein stability, subcellular localization, metabolic enzyme activity, transcriptional factor activity, protein-protein interactions, and protein-DNA interactions.
Figure 1. Illustration of malonyl-CoA metabolism. (Source: Colak G, et al. 2015)
Research indicates that malonylation modifications are primarily found in mitochondria and bacteria, where they are closely associated with metabolic processes. Abnormalities in this modification have been linked to various disease states, particularly demonstrating significant regulatory roles in metabolic disorders, cancer, and developmental abnormalities, offering new perspectives for related disease research.
Our Services
We provide comprehensive and professional malonylation proteomics analysis services, including:
- Malonylation Site Identification: Systematically identifies malonylated proteins and their precise modification sites using high-specificity antibody enrichment and high-resolution mass spectrometry.
- Quantitative Malonylation Proteomics Analysis: Employs advanced quantitative strategies to accurately measure malonylation levels under different physiological or pathological conditions, revealing dynamic changes in malonylation patterns.
- Pan-Cellular Protein Malonylation Profiling: Utilizes optimized proteomics technologies to comprehensively analyze all malonylated proteins within cells, constructing a complete malonylation landscape.
- Functional Studies of Malonylation: Integrates bioinformatics analysis to deeply elucidate the biological functions of malonylation, including its effects on metabolic pathways, enzyme activity regulation, and cellular stress responses.
Service Advantages
Our malonylation proteomics service platform offers the following core strengths:
- High-Specificity Enrichment: Employs optimized antibody affinity enrichment methods with high affinity and specificity for malonylated peptides, ensuring efficient recovery of low-abundance malonylated peptides from complex samples.
- Advanced Analytical Platform: Equipped with high-resolution, high-sensitivity mass spectrometry systems, guaranteeing accuracy and reliability in large-scale malonylated peptide identification.
- Comprehensive Coverage: Through optimized peptide separation and enrichment strategies, combined with necessary digestion and fractionation methods, significantly increases the number and coverage of identified malonylated proteins.
- Professional Bioinformatics Analysis: Provides a complete bioinformatics analysis pipeline, including modified protein and site identification, functional classification, metabolic pathway annotation, and protein-protein interaction network analysis.
Workflow
Protein extraction and quantification are performed using standardized protocols based on the sample type.
Protein samples are digested using specific proteases, with multi-enzyme strategies employed to increase coverage.
Malonylated peptides from the digest are enriched using malonylation-specific antibodies via immunoaffinity purification.
Enriched peptides are separated by high-performance liquid chromatography and analyzed by high-resolution mass spectrometry.
Raw MS data is acquired and processed using professional software for database searching and statistical analysis.
A comprehensive bioinformatics analysis is conducted on the identified malonylated proteins and sites to uncover their biological significance.
A detailed technical report is provided, including the experimental procedure, MS parameters, identification results, and bioinformatics analysis content.
Sample Submission Guidelines
To ensure accurate experimental results, please refer to the following sample requirements:
| Sample Type | Minimum Amount Required |
| Plant Leaves | Wet weight ≥ 0.8 g |
| Plant Roots, Stems, Xylem, Phloem, etc. | Wet weight ≥ 10 g |
| Cell Samples | Cell count equivalent to wet weight ≥ 8×10⁷ |
| Tissue Samples (Human, Animal, Microbial) | Wet weight ≥ 300 mg |
| Body Fluid Samples | Serum/Plasma volume ≥ 1 ml, CSF ≥ 1 ml, Urine ≥ 50 ml |
All samples must be stored in liquid nitrogen or at -80°C and shipped with sufficient dry ice to avoid repeated freeze-thaw cycles.
Malonylation proteomics provides a powerful tool for deciphering metabolic regulation in life processes. We look forward to supporting your research with professional and reliable technical services, helping you unravel the mysteries of protein modifications together.
Reference
- Colak G, et al. Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation. Mol Cell Proteomics. 2015 Nov;14(11):3056-71.
