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Analysis of Monoclonal Antibodies by Ion Mobility-Mass Spectrometry (CAT#: STEM-ST-0152-LJX)

Introduction

Analytical techniques capable of detecting changes in structure are necessary to monitor the quality of monoclonal antibody drug products. Ion mobility mass spectrometry offers an advanced mode of characterization of protein higher order structure. In this service, we evaluated the reproducibility of ion mobility mass spectrometry measurements and mobiligrams, as well as the suitability of this approach to differentiate between and/or characterize different monoclonal antibody drug products.




Principle

Ion mobility spectrometry–mass spectrometry (IMS-MS) is an analytical chemistry method that separates gas phase ions based on their interaction with a collision gas and their masses. In the first step, the ions are separated according to their mobility through a buffer gas on a millisecond timescale using an ion mobility spectrometer. The separated ions are then introduced into a mass analyzer in a second step where their mass-to-charge ratios can be determined on a microsecond timescale.

Applications

For studying the gas phase ion structure
For detecting the chemical warfare agents and explosives
For the analysis of proteins, peptides, drug-like molecules and nano particles
For monitoring isomeric reaction intermediates and probe their kinetics
For proteomics and pharmaceutical analysis

Procedure

1. Add sample
2. The ions in the sample are separated in the ion mobility spectrometer
3. The separated ions are introduced into the mass analyzer for detection
4. Store the detection results

Materials

• Sample Type:
Monoclonal antibodies

Notes

1. Ion mobility spectrometry is also a very fast technique, making it suitable for high-throughput applications. The entire analysis can be completed in just a few minutes.
2. The method is extremely sensitive and able to detect trace amounts of contaminants that other spectrometry methods would miss.
3. The effective separation of analytes achieved with this method makes it widely applicable in the analysis of complex samples such as in proteomics and metabolomics.
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