Product characterization

Detailed sequence analysis by quantitative peptide mapping

Getting a peptide map is a critical part of any analysis project. You use it to confirm the amino acid sequence of your protein and quantify post-translational modifications (PTMs). Peptide analysis can locate truncations and cleavage sites and identify degradation products with stabilit...

Getting a peptide map is a critical part of any analysis project. You use it to confirm the amino acid sequence of your protein and quantify post-translational modifications (PTMs). Peptide analysis can locate truncations and cleavage sites and identify degradation products with stability studies.

The analysis is often vital in comparability studies, especially in quality assurance/quality control (QA/QC) of protein-based biologics. These include mAbs, ADCs, and also recombinant proteins.

How to get high sequence coverage with specific proteases

The principle uses a particular protease that digests the protein and turns it into peptides. We then perform peptide characterization by LC-MS/MS. More specifically, we use the peptide mass (MS) and the fragmentation pattern (MS/MS) for each peptide.

To get the highest sequence coverage possible, it is important to select the right proteases. Therefore, the first step is to perform bioinformatics analysis of your specific protein to advise on the type and number of proteases to apply to your project. This way, full sequence coverage is achieved, and you receive a detailed report.

Experience shows that many customers also combine peptide mapping with other services. Therefore, you may want to add intact mass analysis to extend the protein characterization.

You may select your preferred peptide analysis from the below services:

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Can I compare batch-to-batch variations in N-glycosylations?

The HILIC workflow provides a reproducible, accurate, sensitive and fast glycan assessment. Therefore, it is very useful for routinely monitoring of critical glycoforms.

What causes decreased protein stability?

Since disulfide bonds provide stability, problems with the protein’s stability and activity often correlate with an abnormal disulfide bridge pattern. For many proteins and peptides, disulfide bridges are even essential for optimal biologic function.

How do I characterize the N-glycosylation of an antibody?

For a comprehensive characterization of N-glycosylation of a monoclonal antibody (mAb) you would typically use four complementary HILIC MS-based analysis techniques for top-down analysis, middle-up approach, bottom-up characterization and free N-glycan analysis.

Who is this for?

We primarily help customers within the pharmaceutical industry and biotechs working on drug development, e.g.

Project managers

Working with process development projects.

Analytical experts

Protein scientists that work with ELISA, masss spectrometry, or CMC.

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