N-glycan modification and modification site analysis service
Glycosylation modification increases the complexity and functional diversity of protein molecular structures. It not only affects protein folding, structure, transport, localization, and bioactivity, but also regulates various physiological processes such as cell growth, division, differentiation, recognition, and adhesion through specific recognition between sugars and proteins. Among these, N-glycosylated proteins are commonly found on cell surfaces and in various body fluids. Cell surface glycoproteins are considered key drug targets, and glycoproteins in body fluids are major sources of disease-related biomarkers. Quantitative studies of N-glycosylated proteomics under various physiological and pathological conditions can elucidate the functions of protein glycosylation, which is of great significance for identifying new biomarkers for cancer prevention and diagnosis.
Based on the substitution of mannose residues, N-glycans can be roughly divided into three categories: complex, high-mannose structures, and hybrid structures. Complex types contain fucose, sialic acid, and α-linked galactose. High-mannose type core structures have multiple mannose residues on one branch. Hybrid types have mannose in the core structure of one branch and lactosamine sequences on another. General N-glycan site analysis strategy: isolate and enrich glycoproteins/glycopeptides, then use enzymatic or chemical methods to separate glycans from glycosylated peptides, and perform mass spectrometry analysis on the released glycans or deglycosylated peptides to analyze the overall expression and changes in glycans and/or glycoproteins in the sample.
Types of N-glycans (Varki A.et al; 2017)
BTP Bio N-glycosylation and site analysis service
BTP Bio provides N-glycosylation and site analysis services, capable of identifying modification sites and specific glycan types, analyzing N-glycosylation types and locations, and elucidating the structure and position of N-glycans, enabling quantitative analysis of glycan modifications. The general steps for N-glycan chain analysis are: 1) Enzymatic release of attached glycans; 2) Derivatization of released glycans through reductive amination reactions with aromatic hydrocarbons or fatty amines or permethylation reaction; 3) Glycan analysis.
Advantages of BTP Bio's mass spectrometry-based N-glycosylation analysis service
1. Lectin affinity method for enriching N-glycosylated peptides, with high specificity and enrichment efficiency
2. High-throughput identification, capable of detecting up to 10,000 N-glycosylation sites in one go
3. High detection sensitivity and good reproducibility
4. Relatively short project cycle
Sample transportation
If you are providing tissue samples, please transport them with dry ice.
If you are providing protein samples, please use normal tissue or cell lysis buffer for protein extraction.
Ensure adequate dry ice and choose a fast shipping method to minimize the possibility of sample degradation during transportation. If you have any questions about sample transportation, please feel free to contact us.
BTP Bio has many years of analytical service experience in the field of glycomics and can tailor glycomic analysis services to your specific needs. Welcome to inquire!
Bilingual project report in Chinese/English
In the technical report, BTP Bio will provide you with a detailed bilingual technical report in Chinese and English, which includes:
1. Experimental steps (in Chinese and English)
2. Relevant mass spectrometry parameters (in Chinese and English)
3. Mass spectrometry images
4. Raw data
5. N-glycosylation and site analysis results
One-stop service for N-glycosylation and site analysis
You only need to place an order and send the sample
BTP Bio's one-stop service completes: sample processing - on-machine analysis - data analysis - project report
