Are you seeing the changes you want to see?

Almost all proteins, whether produced and purified as recombinant proteins or isolated from natural sources, will to some degree carry modified amino acids.

Characterizing product-related impurities is a major task. You’ll need us to analyze them with as much sensitivity and accuracy as possible. Such modifications may of course be part of the physiological function that you are developing.

But we understand that you’re keen to observe the lowest possible number of process-related modifications. The latter may occur during the sample handling process, for example in proteins that have been stored for a period of time during a stability study. They are unintentional and a source of structural heterogeneity in a protein. And that’s not what you want when you’re trying to develop a consistent, trustworthy drug substance or product.

All such changes are known as post-translational modifications and whilst some of them are desired, others are unwanted.

At Protagen, we use our mass spectrometers to detect even the smallest and peskiest modifications, which we usually analyze using a combination of electrophoretic, HPLC and peptide mapping methods.

Normally, mass spectrometry data is qualitative rather than quantitative. However we’ll provide you with data evaluations – that is, real numbers about the degree of modification taking place in your protein – so that you get a clear picture of how your protein is doing.

You can choose from the following types of analysis:

•    Deamidation
•    Oxidation
•    Glycosylation
•    Phosphorylation
•    N- and C- terminal truncation (see N/C- Terminal Sequencing)
•    Acetylation
•    Pyroglutamate formation

Characterizing post-translational protein modifications is a key requirement of ICH Q6B.

Your contact for Protein 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