Peptide characterization

Detailed protein characterization by peptide map

Getting a peptide map is a critical part of any protein characterization project. It is used to confirm the amino acid sequence of your protein, and obtain detailed information about post translational modifications (PTMs), as well as locate truncations and cleavage sites.

It is...

Getting a peptide map is a critical part of any protein characterization project. It is used to confirm the amino acid sequence of your protein, and obtain detailed information about post translational modifications (PTMs), as well as locate truncations and cleavage sites.

It is often applied as a vital part of comparability studies, especially in quality assurance/quality control (QA/QC) of protein-based biologics, such as mAbs, ADCs and recombinant proteins.

High sequence coverage by specific proteases

The principle is to use a specific protease for digestion turning the protein into peptides. We perform peptide characterization by LC-MS/MS using the peptide mass (MS) and the fragmentation pattern (MS/MS) for each peptide.

To get as high sequence coverage as possible it is important to select the right proteases. Therefore, we prefer to perform bioinformatics analysis of your specific protein to be able to advise you about the type and number of proteases to apply for your project. In this way, full sequence coverage is achieved, and you receive a detailed protein sequencing report.

The analysis is regularly combined with other services, such as N-terminal Edman sequencing, de-novo sequencing and intact mass analysis, to extend the protein characterization.

You can choose your preferred peptide characterization analysis from below services:

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Is it possible to 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 could be the cause of 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 my 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 and characterization projects.

Analytical experts

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

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