Protein glycosylation is one of the most common and complex post-translational modifications and is critical in many biological processes, including cell adhesion to the extracellular matrix and intracellular protein ligand interactions. Creative BioMart's extensive experience in post-translational modification of proteins based on computational and experimental methods enables us to provide protein glycosylation service to accelerate your project.

Protein glycosylation, the covalent selection of individual sugars or glycans to target protein residues, provides greater proteomic diversity than other PTMs. The different types and structures of glycoproteins allow them to accommodate these different functions. There are two types of protein glycosylation, O-linked and N-linked, both involved in maintaining protein conformation and activity, protecting proteins from proteolytic degradation, and protein intracellular transport and secretion. In addition, N-glycan moieties also play key roles in the folding, processing and secretion of proteins in the endoplasmic reticulum (ER) and Golgi apparatus. Studies have found that abnormal glycosylation is associated with a variety of congenital, metabolic, neurodegenerative and immune diseases, as well as cancer. Therefore, scientists are increasingly focusing on protein glycosylation in the biomedical field. Protein glycosylation not only greatly facilitates the expansion of the proteome, but also has a profound impact on the function, stability, subcellular localization and other properties of proteins.

Fig 1. Protein glycosylation across evolution. ( Eichler J, 2019)

Services

Analysis of proteoglycans is complicated by the wide variety and large number of potential glycosylation combinations: even a single protein can undergo many N- and O-glycosylations. Furthermore, the same glycosylation site can be occupied by different glycans in different copies of the protein. To address these challenges, Creative BioMart has successfully employed a variety of techniques to reliably study protein glycosylation to fully understand the glycosylation status of proteins. In addition, we used a range of analytical and bioinformatic tools to assess the site-specific heterogeneity of heavily glycosylated proteins. We provide one-stop service for N- and O-glycosylation, glycomic analysis:

• Glycoprotein detection: we detect glycosylated proteins using staining and affinity-based methods.
• Glycan structure analysis: after confirming protein glycosylation, we elucidate the glycan moiety structure by chromatography and mass spectrometry. Glycans can be analyzed as they are attached to proteins or after they are released.
• Identification of glycosylation sites: identification of glycosylation sites provides an indication of the function of the glycan.
• Glycoprotein quantification: by lectin purification followed by a labeling procedure for relative quantification of specific glycoproteins.

Approaches for Analyzing Protein Glycosylation

The identification and quantification of proteoglycans is becoming increasingly important in biomedicine and biotechnology. We employ the following state-of-the-art methods for the identification and quantification of oligosaccharides, particularly N- and O-glycosylated proteins.

• Radiolabeling.
• Molecular Fluorescence Labeling.
• Electrophoresis.
• Lectin labeling.
• Antibody labeling.
• Chemical enzyme method.
• Chromatography.
• Mass spectrometry.

Our mission is to provide global customers with the most comprehensive and professional customized protein glycosylation service. If you have any special requirements about our services, please feel free to contact us. We are looking forward to working together with your attractive projects.

References

1. Eichler J. (2019) Protein glycosylation[J]. Current Biology. 29(7): R229-R231.
2. Roth Z, Yehezkel G, Khalaila I. (2012) Identification and quantification of protein glycosylation[J]. International journal of carbohydrate chemistry. 2012.

• Protein Acetylation Service
• Protein Carbonylation Service
• Protein Hydroxylation Service
• Protein Methylation Service
• Protein Nitrosylation Service
• Protein Phosphorylation Service
• Protein Proteolytic Service
• Protein Sulfation Service
• Protein Ubiquitination Service