Introduction
Small ubiquitin-like modifier (SUMO) is a post-translational modification of protein, which refers to the covalent
attachment of a small ubiquitin-related modifier (SUMO) to the protein. A protein with approximately 18% homology to
ubiquitin, the SUMO protein is approximately 100 amino acids in length and has considerable structural overlap with
ubiquitin. In mammals, the SUMO family includes four known SUMO isomers: SUMO 1-4.
The conjugation of SUMO, known as SUMOylation, is an essential PTM that is highly conserved in eukaryotes and is
involved in regulating the subcellular localization of many substrate proteins, such as gene transcription,
subnuclear structure formation, viral infection, and cell cycle progression. The imbalance of SUMOylation and
deSUMOylation is related to the occurrence and progression of various diseases, and the identification of protein
SUMO will help to elucidate disease pathogenesis and provide support to develop potential therapeutic strategies or
target drugs.
Fig. 1.
Biochemical process of SUMO modifications in mammal cells. (Yang Y, et al., 2017)
Our Services
The methods of SUMOylation identification mainly include bioinformatics combined with amino acid site-directed
mutagenesis and mass spectrometry (MS)-based proteomics analysis. With a powerful mass spectrometry sequencing
platform, Creative Proteomics has launched a high-sensitivity mass spectrometry analysis platform
for protein SUMOylation identification. Multiple samples and sumoylation in eukaryotes and prokaryotes can be
analyzed for robust identification and quantification of SUMO modifications.
At Creative Proteomics, our highly qualified scientists isolate target SUMOylated proteins by
affinity chromatography, and then identify them by MS. Throughout the service cycle, SUMO proteins were digested
with endoprotease Lys-C, enriched using specific antibodies or affinity-immobilized metal affinity chromatography,
and identified by MS.
With cutting-edge equipment and expertise in protein sequencing and mass spectrometry, we provide one-stop protein
sumoylation identification service. You only need to tell us the purpose of your experiment and send your samples to
us, we will take care of all the follow-up matters of the project.
The simple process of our service includes:
- Protein extraction.
- In-gel or in-solution enzymatic digestion.
- Sumoylation peptide enrichment (optional step).
- Peptide separation.
- Mass spectrometry analysis.
- Bioinformatics analysis.
What Can We Offer You?
- SUMOylated Peptide Enrichment
- Identification of Protein SUMO Modification Sites
- Structural Analysis of Protein SUMO Modifications
- Mapping SUMO-modified Lysines
- Protein SUMO Qualitative Analysis
- Stability Analysis of SUMO-Modified Proteins
Advantages of Our Services
- High site coverage: SUMOylated peptides can be enriched to improve the detection effect.
- High precision and accuracy: A high-resolution mass spectrometer is used, and specific modified peptides and
modification sites can be found, which can effectively improve the quantitative and qualitative analysis of
post-translational modifications of protein drugs.
- Experienced: Professional advices from our scientists with years of experience in protein sequencing.
- Fast turnaround: 5-7 days to provide comprehensive report.
- Customized service: Tailoring the best solution according to your project and sample type.
Sample Requirements
- Tissue samples: Plant tissue samples > 200 mg, blood samples > 1 mL (with EDTA for anticoagulation of
plasma), serum > 0.5 mL, urine> 2 mL, animal tissue samples > 1 g, cell samples > 5X107
cells, microorganisms > 200 mg (dry weigh).
- Protein samples > 1 mg.
Thanks to our powerful mass spectrometry sequencing platform, Creative Proteomics provides a
one-stop protein sumoylation identification service for customers worldwhile. Our experienced scientists work with
you to develop tailor-made analytical solutions. Please feel free to contact
us with any questions regarding protein sumoylation identification.
References
- Yang Y, He Y, Wang X, et al. (2017) Protein SUMOylation modification and its associations with disease.
Open Biol. 7(10):170167.
- Sheng Z, Wang X, Ma Y, et al. (2019) MS-based strategies for identification of protein SUMOylation
modification. Electrophoresis. 40(21):2877-2887.
