Using direct CIEF-MS and prep-CIEF for MS-characterization of protein isoforms, LC-MS analysis, peptide mapping and other techniques
Usually, capillary isoelectric focusing (CIEF) methods rely only on optical detection due to the incompatibility of common CIEF reagents with ESI-MS detection (e.g. methylcellulose, ampholytes). Recent developments show promising results of the CIEF separation of intact mAb charge variants and coupling CIEF directly to mass spectrometry (MS).
In this webinar, Prof. Dr. Christian Neusüß (Aalen University) and Dr. Carsten Sonksen (Novo Nordisk) discuss the results of their work on online iCIEF-MS of intact monoclonal antibody samples and analysis of fractions collected from iCIEF separated protein. This is the first online coupling of iCIEF to MS providing direct identification of each intact mAb charge variant. This method even provides unattended repeated fractionation of such variants for further offline characterizations like peptide mapping.
- Prof. Dr. Christian Neusüß (Aalen University) will share insights into the application of iCIEF-MS for protein isoform characterization.
- Dr. Carsten Sönksen (Novo Nordisk) will present data using prep-iCIEF with subsequent peptide mapping and LC-MS analysis.
- Dr. Tiemin Huang (President & CEO, Advanced Electrophoresis Solutions) will precede the presentations explaining the experimental setup needed to run such experiments.
You will learn about:
- Routine protein isoform characterization by MS and peptide mapping, using either direct MS coupling or fractionation
- Making routine unattended CIEF fractionation possible
- Whole solution charge-based protein separation and characterization using CIEF
Who should attend
- Scientists working in assay development or biopharmaceutical QC labs, including CROs and CMOs
- Anyone who works with CIEF, IEX, Gel-IEF, or anything with iso electrical focusing
Certificate of Attendance
All webinar participants can request a certificate of attendance, and a learning outcomes summary document for continuing education purposes.