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Designed to address characterization challenges during biopharmaceutical drug development and quality monitoring.
July 21, 2021
By: Kristin Brooks
Managing Editor, Contract Pharma
MOBILion Systems Inc. has launched its first commercial High-Resolution Ion Mobility (HRIM) product, MOBIE, designed to address characterization challenges during biopharmaceutical drug development and quality monitoring. MOBIE is designed to provide fast, efficient separations with superior resolution and reproducibility, faster, simpler method development, and greater instrument uptime, according to the company. This new technology aims to help accelerate and simplify the workflows of challenging analyte classes including peptides, proteins, lipids and glycans, with analysis times 5-60 times faster than conventional separation methods. The technology behind MOBIE is the SLIM (Structures for Lossless Ion Manipulation) technology that provides the capability to separate and identify molecular structures that can either be too time-consuming or even impossible to detect with established methods such as liquid chromatography (LC). “MOBIE can not only separate and identify molecules other instruments fail to detect, but it achieves superior performance with rapid analysis times, more efficient analyte-agnostic workflows, and more reproducible results, making it ideal for routine analysis,” says Dr. Melissa Sherman, CEO of MOBILion Systems Inc., “We are excited to be bringing this best-in-class product to biopharma and biomarker researchers.” In 2018, MOBILion partnered with Agilent Technologies to integrate its first HRIM system with Agilent’s 6500 line of Q-TOF Mass Spectrometers to provide a tool for pharmaceutical companies to develop safer and more effective biologic therapeutics, and aid in biomarker research. Earlier this year, MOBILion partnered with Protein Metrics to integrate with the BYOS biopharma software suite, delivering a full workflow solution with fast, easy data processing. The combination of these platforms helps eliminate impediments to identifying and characterizing CQAs with the reliability, repeatability and speed required in modern biopharmaceutical organizations developing increasingly complex protein therapeutics.
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