Glycomic Profiling Service

Glycomics refers to the collection, analysis, and utilization of glycosidic biological data at the omics level. The profound biological effects of lipid and protein glycosylation make glycomics an important field in life sciences. N-glycome analysis (a comprehensive study of all glycans) is a complement to genomics and proteomics. Glycomics studies at the cellular or organismal level can provide a general overview of the overall glycosylation patterns of glycome, glycoprotein, lipid, or other type of biomolecules. Glycomics analysis can be used to compare differences between two glyco-engineered host strains in the production of therapeutic glycoproteins or to compare cancer data at different stages to discover new biomarkers.

 



Figure 1. Glycomics Analysis Service

 

Services at MtoZ Biolabs

We can identify all N-glycans expressed by plasma/serum, cells, tissues, or organisms. All glycans linked to proteins will be digested and hydrolyzed by enzyme and separated by hydrophilic chromatography, followed by quantitative analysis by MALDI-TOF-MS.

 

Analysis Workflow



Services at MtoZ Biolabs

1. Glycoprotein Analysis

2. Quantitative Glycoproteomics

3. N-glycan Analysis Service

4. O-glycan Analysis Service

5. N-glycosylation Site Analysis

6. O-glycosylation Site Analysis

7. N-glycan Modification and Modification Site Analysis Service

8. O-glycan Modification and Modification Site Analysis Service

9. HILIC-UHPLC Analysis of N-glycan Bonds

• • Glycosylation Sites and Glycoform Analysis Services

  Protein glycosylation not only influences the protein's spatial configuration, biological activity, transportation, and localization, but also plays a crucial role in specific biological processes such as molecular recognition, cell communication, and signal transduction. Therefore, the analysis of glycosylation sites and their glycoforms is of great significance.

• • N-Glycosylation Site Analysis Service | Biological Products

  N-glycosylation is a post-translational modification involved in various physiological and pathological processes. The variability of glycosylation modification site is a key indicator of cellular activity, as evidenced by the correlation between the reduction of glycosylation attachment site on serum protein and the severity of congenital disorders of glycosylation (CDGs). Therefore, accurately determining site occupancy rate is crucial for understanding the impact of protein glycosylation on human health.

• • O-Glycosylation Site Analysis Service | Biological Products

  Unlike N-glycans, O-glycans are smaller, highly diversified branched carbohydrate molecules that can attach to various protein structures. This characteristic leads to the complexity of the analysis, making it difficult to analyze O-glycosylation sites. The variability of glycosylation sites is a key indicator of cellular activity, as evidenced by the correlation between the reduction in serum protein glycosylation sites and the severity of congenital disorders of glycosylation (CDGs).

• • O-Glycan Profiling Service

  Glycosylation analysis is one of the most challenging types of post-translational modification (PTM) analysis. Glycosylation modifications typically occur at the group level rather than as individual modifications. Even a single glycosylation site on a protein may exhibit various chain lengths and multiple polysaccharide isomers with different branching.

• • O-Glycan Modification and Site Analysis Service

  O-glycosylation typically occurs 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

• • N-Glycan Profiling Service | HILIC-UHPLC MS

  Glycosylation primarily refers to the enzymatic process of linking polysaccharides to proteins, lipids, or other organic molecules, and is the most common type of post-translational modification (PTM). Due to the complexity and isoform nature of the linked polysaccharides, glycan analysis presents significant challenges. As protein therapeutics such as monoclonal antibodies, glycoproteins, hormones, cytokines, and coagulation factors are increasingly used in clinical practice, the detection of protein N-gly

• • HILIC-UHPLC Based N-Glycosidic Bonds Analysis Service

  Glycosidic bonds rarely affect the function of glycoproteins, thus they are usually not necessary to determine. However, the glycan structure of glycoproteins is highly complex, and assessing the configuration and location of N-glycan glycosidic bonds is helpful for analyzing the structure of glycoproteins. There are five common types of N-glycosidic bonds, with the most common being the connection between N-acetylglucosamine (GlcNAcβ1-Asn) and asparagine (Asn). Other types connected to Asn include glucose

• • N-Glycan Modification and Site Analysis Service

  Glycosylation modifications increase the complexity of protein molecular structure and the diversity of functions, not only affecting protein folding, structure, transportation, localization, and biological activity but also regulating 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 ubiquitously present on cell surfaces and various body fluids.

• • Glycosylation Site Analysis Service

  The analysis of glycosylation sites in glycosylated proteins is of great importance for studying protein structure and function.

• • Glycan Profile Analysis Service

  For the relative quantification of glycan types in glycosylated proteins, MtoZ Biolabs provides glycan type relative quantification services based on MALDI-TOF/LC-MS. Due to the diversity of O-glycosylation modifications and the absence of universal enzymes that can cleave all O-glycans, our glycan type analysis currently focuses only on N-glycosylated proteins.