O-Glycan Modification and Site Analysis Service

O-glycosylation typically presents in secreted proteins and membrane-bound proteins, taking place within the Golgi apparatus. O-glycans are linked to proteins through serine and threonine, and then to hydroxyproline and hydroxylysine. The primary method of O-glycosylation for secreted and membrane proteins involves reducing N-acetylgalactosamine (GalNAc) at the reducing end. O-glycans are considered "mucin-type" glycans. In addition to mucin-type O-linked glycans, many mammalian proteins also connect through mannose (Man), fucose (Fuc), glucose (Glc), galactose (Gal), or xylose (Xyl) at the reducing end. O-glycans affect the localization and transportation of proteins, the solubility of proteins, antigenicity, and intercellular interactions.

 

O-glycan modification analysis is an effective method for identifying glycan binding sites. Its principle involves introducing a stable substituent (ether-linked methyl) on each free hydroxyl group of the natural glycan, then cleaving the glycosidic bonds, which are much less stable than the ether-linked methyl, by acid hydrolysis, thereby generating single methylated monosaccharides with a free hydroxyl group at the previously introduced linking position. Partially methylated monosaccharides undergo ring opening with a reducing agent (usually deuterated borohydride) to introduce a new hydroxyl group (possibly a ²H at C-1), which helps identify the reducing end of each monosaccharide. Then, all free hydroxyl groups are acetylated to produce partially methylated alditol acetates (PMAAs) for subsequent analysis.

 

MtoZ Biolabs offers O-glycan modification and modification site analysis servicte, capable of decoding the composition of O-glycans. The general workflow for O-glycosylation analysis includes enrichment of O-glycoproteins/peptides, dissociation of O-glycans, structural identification, and quantitative analysis of O-glycans.

 

Sample Submission Requirements

1. If you are providing tissue samples, please transport them on dry ice.

2. If you are providing protein samples, please transport protein extracted normal tissue or cell lysates.

Ensure sufficient dry ice for transportation and choose the fastest mailing method to minimize the sample degradation during transport. If you have any questions about sample transportatiion, please contact us at any time.

 

MtoZ Biolabs has much analytical service experience in glycomics and can customize glycomics analysis services according to your specific needs. Free project evaluation!

 

Deliverables

1. Experimental Procedures

2. Mass Spectrometric Parameters

3. Mass Spectrometric Images

4. Raw Data

5. Results of O-Glycan Modification and Modification Site Analysis