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Glycoproteomics Service

Glycosylation refers to the process by which proteins or lipids are linked to glycan chains by the action of enzymes. As an important post-translational modification, glycosylation is involved in and regulates many life activities of living organisms. With the continuous development of proteomic technology, studies for protein glycosylation have received extensive attention. Glycobiology is the study of glycan formations, structures, and functions and has become an area of interest for life sciences that cannot be ignored at present.

Principle

Hydrophilic interaction liquid chromatography (HILIC) is a glycopeptide enrichment technology based on the strong hydrophilic properties of polyhydroxy-rich glycan chains, meanwhile utilizing chromatography to separate glycopeptides from non-glycosylated peptides. HILIC remains unbias for different types of glycopeptides and can maintain the integrity of the sugar chain structure, which is suitable for studying the complete glycopeptide structures.

The identification of a single N-glycoprotein: After protein cleavage into peptides by trypsin, glycopeptides are enriched using the HILIC assay. N-glycosaminidase (PNGase) cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and complex oligosaccharides. Then, PNGase F was removed, and mass spectrometry was performed. The identification of glycosylated proteins and modification sites in complex samples is performed using the Byonic method. The Byonic search engine provides a sensitive and comprehensive identification of peptides and proteins, which is accompanied by the Preview^TM software allows rapid assessment of peptide quality errors, digestion specificity, and modifications.

Our Glycoproteomics (Glycopeptides Analysis) Services

Creative Proteomics combines reductase digestion, N-glycosylated peptide enrichment, deglycosylation in H₂O¹⁸, and highly sensitive LC-MS detection techniques to analyze and clarify N-glycosylation modification sites of samples. The deglycosylated N-glycan chains can also be interpreted by the MALDI-TOF, which can provide relevant experimental evidence, including XICs mass spectra, MS2 spectra, and MALDI-TOF glycan spectra to support data analysis.

Workflow of Glycoproteomics

LC-MS/MS approaches of Proteomics and Glycoproteomics

LC-MS/MS approaches of Proteomics and Glycoproteomics (Rui Zhu et al. 2018)

Service Contents

Analysis of N-Glycan modification sites (optional O¹⁸ labeling)
MALDI-TOF Glycopeptide Mapping (including N-Glycan and O-Glycan)
Glycoprotein Profiling of Intact Proteins
Glycoform Ratio Analysis
Analysis of glycosylation sites and glycoforms

Advantages

Professional technical support
Experienced operators
Independently developed and advanced experimental SOPs
Rich experience in animal & plant analysis
Strong bioinformatics team

Applications

- Identification of post-translational modifications of proteins from animal tissues, cells, organelles, blood, plasma, urine, cerebrospinal fluid, saliva, and other body fluids
- Post-translational modification identification of extracted proteins from plants (rice, Arabidopsis, wheat, etc.)
- Identification of protein post-translational modifications from yeast, E. coli
- Other common biological protein samples

Platforms

MALDI-TOF, Q-Exactive Plus, Q-Exactive HF, Orbitrap Fusion, Orbitrap Fusion Lumos

Sample requirements

Tissue samples: animal, microbial tissue wet weight > 30 mg; plant fresh tissue > 300 mg
Cell samples: cell volume > 10⁷
Body fluid samples: serum volume > 1500 μL
Protein extracts: total protein > 200 μg and concentration > 1 μg/μL
SDS-PAGE gel samples: total target protein > 50 μg

Delivery

Experimental report
Raw data
Experimental results

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

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From Our Clients

"I recently used their proteomics service for a project analyzing protein interactions in yeast models. The team was very responsive and helped clarify the methodology they employed, which made me feel confident in the results. The data quality was solid, with clear identification of several key proteins involved in our study. Their thorough analysis enabled me to pinpoint specific interactions that I hadn't considered before, which significantly improved the direction of my research. I appreciate their professionalism and support throughout the process."

Sarah Thompson, University of California, Berkeley

"Our lab collaborated with them on a project studying cancer biomarkers. The proteomics analysis provided was detailed and focused, specifically highlighting the differential expression of proteins between healthy and tumor samples. Their clear explanations of the data helped my team understand the biological implications. I also appreciated their willingness to revise the reports based on our feedback, ensuring that we had everything we needed for our publication. This collaborative spirit was invaluable."

Emily Rodriguez, Stanford University

"Our lab worked with them on a project studying the effects of diet on gut microbiota using proteomics. They used a label-free quantification method to analyze proteins in fecal samples before and after dietary intervention. The results showed significant changes in protein expression linked to microbial activity. This was pivotal for our hypothesis about diet-microbiota interactions. The clarity of their data presentation made it easy for our team to integrate these findings into our ongoing research."

Dr. Lisa Wong, University of Toronto

"My experience with Creative Proteomics during the mass spectrometry analysis was excellent. We sent in human saliva and mouse brain tissue samples, which they expertly analyzed using both LC-MS and GC-MS techniques. The results were invaluable, revealing key metabolites in the saliva and identifying biomarkers linked to brain function in the brain tissue."

Dr. Emily Carter, Senior Research Scientist

"The overall service from Creative Proteomics was outstanding. They made the entire process seamless and efficient, allowing us to focus on our research. We worked with leaf and root samples from various Arabidopsis genotypes for targeted metabolomics analysis. Their thorough profiling of primary and secondary metabolites gave us important insights into how the plants respond metabolically to environmental stress."

Dr. Laura Henderson, Plant Physiologist

"We had a pleasant collaboration with Creative Proteomics on mass spectrometry analysis of lipids. They conducted a detailed analysis of lipid species, providing us with important insights into lipid metabolism and its relationship with metabolic syndrome disease states."

Dr. Sarah Mitchell, Research Scientist

Online Inquiry

Please submit a detailed description of your project. We will provide you with a customized project plan to meet your research requests. You can also send emails directly to for inquiries.

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