O-glycosylation Modification and Modification Site Analysis Service
O-glycosylation typically occurs in secreted proteins and membrane-bound proteins, taking place in the Golgi apparatus. O-glycosylation glycans are attached to proteins through serine and threonine and then connect with hydroxyproline and hydroxylysine. The main method of O-glycosylation for secreted and membrane proteins is through the reduction at the reducing end of N-acetylgalactosamine (GalNAc). O-glycans are considered 'mucin-type' glycans. In addition to mucin-type O-linked glycans, many mammalian proteins are also connected with mannose (Man), fucose (Fuc), glucose (Glc), Gal, or xylose (Xyl) at the reducing end. O-glycans influence protein localization and transport, solubility, antigenicity, and cell-to-cell interactions.
Core structure of mucin-type glycans
O-glycan modification analysis is an effective method for identifying glycan binding sites. The principle involves introducing stable substituents (ether-linked methyl groups) at each free hydroxyl group of native glycans, then using acid hydrolysis to cleave glycosidic bonds, which are much weaker in stability than ether-linked methyl groups. This generates individual methylated monosaccharides with free hydroxyl groups at the previously introduced linkage positions. Partially methylated monosaccharides are opened with a reducing agent (usually borodeuteride) to introduce new hydroxyl groups (possibly introducing deuterium atoms at C-1), aiding in identifying the reducing end of each monosaccharide. Subsequently, all free hydroxyl groups are acetylated to form partially methylated alditol acetates (PMAA) for further analysis.
Biotechnology company Biotai Parker offers O-glycan modification and modification site analysis services, capable of analyzing the composition of O-glycans. The typical workflow for O-glycosylation analysis includes O-glycoprotein/peptide enrichment, O-glycan release, and O-glycan structure identification and quantitative analysis.
General workflow for O-glycan analysis
Sample transportation
If you provide tissue samples, please transport them on dry ice.
If you provide protein samples, please use normal tissue or cell lysis buffer for protein extraction.
Ensure an adequate amount of dry ice during transportation and choose a faster shipping method to reduce the potential degradation of samples during transit. If you have any questions about sample transportation, please feel free to contact us.
Biotai Parker Biotechnology has many years of experience in glycomics analysis services and can tailor glycomics analysis services to meet your specific needs. Welcome to consult!
Project report in Chinese/English
In the technical report, Biotai Parker will provide you with a detailed bilingual technical report in Chinese and English, including:
1. Experimental steps (in Chinese and English)
2. Relevant mass spectrometry parameters (in Chinese and English)
3. Mass spectrometry images
4. Raw data
5. Results of O-glycan modification and modification site analysis
One-stop service for O-glycan modification and modification site analysis
You only need to place an order and send the samples
Biotai Parker provides a one-stop service: sample processing, machine analysis, data analysis, and project report
