N-glycosylation is the covalent attachment of an oligosaccharide (also referred to as glycan) to protein at asparagine residues by an N-glycosidic bond. This type of linkage is essential for multiple biological processes, including cell development and differentiation, cell-cell or cell-matrix communication, and pathogen-host interaction. Furthermore, the N-glycan components of biotherapeutics may primarily determine biological activity and therapeutic efficacy. Therefore, N-glycan patterns must be addressed for continued safety, purity, and potency of drug product and proteomics studies.
Figure 1. N-glycans are attached to asparagine residues of proteins.
At Creative Proteomics, we provide comprehensive, reproducible, and high-throughput analysis of N-linked glycans present on monoclonal antibodies and other related glycoproteins. This service is dedicated to accelerating your biotherapeutics development projects by enabling rapid and reliable characterization, and routine analysis of N-glycan patterns in your samples for the assessment of product quality and consistency of manufacture in the development and production of protein pharmaceuticals.
Creative Proteomics provides the N-glycan profiling analysis for protein, antibody drug, peptides, etc., by utilizing MALDI-TOF-MS or HILIC-UHPLC MS. Hydrophilic interaction chromatography (HILIC) has been a powerful technology for N-glycan profiling.
Figure 2. Workflow for N-glycan profiling service.
We work with a range of sample sources as follows.
Creative Proteomics offers several service options according to your specific needs. Please do not hesitate to contact us if you have any further questions or concerns.
1. Duke C H T R. N-Glycan composition profiling for quality testing of biotherapeutics. BioPharm International, 2015, 28(12).