Location, location, location

Why would you engage us to find the locations of glycosylation in your protein? Because our specialized bioinformatic team offers an in-depth and complete understanding of where and what glycans are attached to your protein.

We often observe, in both N-linked glycosylation and O-linked glycosylation, that not all of the possible sites of glycan attachment are occupied. By applying High Performance Liquid Chromatography (HPLC) and mass spectrometry, we can determine the sites where glycans are present, what type of glycans they are, as well as any sites that are unoccupied.

Furthermore, we’ve developed strategies, optimized for N-linked glycosylation or O-linked glycosylation, which we use in complicated applications such as comparability studies of biosimilars.

Analyzing the glycosylation sites of a glycoprotein is a key requirement of ICH Q6B.

Technical information

N- and O-linked glycans are attached to proteins via specific amino acids. While N-linked glycans are only attached to asparagine residues incorporated in a consensus sequence, O-linked glycans can be attached to a number of different amino acids.

Analysis of the N- or O-linked glycans can be carried out by HPAEC-PAD, LC-ESI-MS or MALDI-MS. We can either carry out a summary analysis of all glycosylation sites, or we can be site-specific.

The structural heterogeneity of a glycoprotein can be visualized using 2D PAGE or intact mass.

Your contact for Site of Modification at Protagen Protein Services GmbH


Dr. Marcus Mreyen

Director Business Development
Our business development team will be happy to assist you with your project.

Phone: +49 (0) 231 9742-6100
Email: salesproteinservices@ProtagenProteinServices.com