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Succinylation Analysis Service

Protein succinylation is the process by which a succinyl group donor (e.g., succinyl coenzyme A) covalently binds a succinyl group to a lysine residue, either enzymatically or non-enzymatically. Lysine succinylation is widespread in eukaryotic and prokaryotic cells, and many succinylation sites have been identified in many species such as bacteria, fungi, parasites, and mammalian cells, and these modified proteins are found in various parts of cells, including cell membrane, cytoplasmic matrix, various organelles, and nucleus. Lysine succinylations are involved in different metabolic reactions in cells, including glucose metabolism, tricarboxylic acid cycle, and fatty acid metabolism, which are closely related to the activities of living organisms.

Our Succinylation Analysis Service

As an industry leader in PTMs, Creative Proteomics offers a large-scale protein succinylation analytical service package through mass spectrometry and enrichment processing. By using this service, customers will only need to send in the sample of investigation and leave the rest to our team, including but not limited to protein extraction, proteolysis, peptide separation, mass spectrometry analysis, mass spectrometry raw data analysis, and bioinformatics analysis.


During our service cycle, your provided protein samples will be digested into a mixture of peptide fragments and then separated by liquid chromatography according to their different components, hence reducing the overall complexity of your protein sample. Subsequently, succinylated peptides are annotated, identified, and specifically enriched using the high-quality succinylated modified antibodies or biological materials for final bioinformatic analysis. As a result, the succinylated protein modification is revealed, analyzed, and quantified by liquid chromatography-tandem mass spectrometry.


Technical Advantages

  • Adopt mainstream antibody affinity enrichment method to achieve high specificity and enrichment efficiency
  • Large-scale identification of enriched succinylated peptides with mass spectrometry of high resolution and high throughput
  • Combining commercially available quantitative techniques to analyze, compare, and correlate succinylation levels between different quantitatively
  • A research team with extensive experience in PTMs

Customized Bioinformatics Services

Standard AnalysisCustomized Analysis

a)  Collection of output statistics
b) Establishment of database and search for modified proteins
c) Identification of modified proteins and modification sites
d) Annotation of modified proteins
e) Quantitative analysis of modified proteins
f) Analysis of differential expression of modified proteins
g) Functional enrichment analysis of differentially modified proteins GO/KEGG

Modified peptide motif analysis
Protein network interaction prediction
Protein domain prediction (Advanced Analysis)
Protein subcellular localization analysis (Advanced Analysis)

Sample requirements

  • Fresh animal tissue: ≥600 mg
  • Fresh plant tissue: ≥6 g
  • Cell culture: ≥1×107 cells/tube x 3 tubes
  • Fungi and bacteria: ≥600 mg
  • Serum, plasma: 450 μL × 4 tubes
  • Protein solution: total protein of 5-10 mg
  • Body fluid samples: urine of 15 mL × 4 tubes (centrifuge at 1000 x g for 5 minutes and discard sediment); or other body fluids (saliva, amniotic fluid, cell culture supernatant, etc.) > 15 mL


  • Drug target research
  • Disease biomarker screening
  • Plant stress/resistance research
  • mechanism of action research

Technology platforms

Ion Chromatography
High-Performance Liquid Chromatography (HPLC)
Matrix-Assisted Laser Desorption Ionization Mass Spectrometry (MALDI-MS)

* For Research Use Only. Not for use in diagnostic procedures.
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