Bio-Techne Corporation announced the launch of its ProteinSimple-branded MauriceFlex™ during the WCBP conference in Washington D.C. MauriceFlex™ enables protein charge variant fractionation plus routine cIEF & CE-SDS assays, making it a unique multi-functional system that further streamlines protein characterization workflows. In-depth characterization of protein charge variants is critical to identify post-translational modifications (PTMs), as some PTMs impact a molecule's therapeutic functionality. These variants need to be separated and collected for further analysis by biochemical and biophysical techniques.

Capillary isoelectric focusing (cIEF) is the gold-standard for charge variant analysis, and MauriceFlex™ enables cIEF-based fractionation in the same day, precluding the need for method development, fractionation, and data bridging with ion-exchange chromatography (IEX) or other methods. MauriceFlex™ can run samples with urea, a feature that is missing in current capillary electrophoresis-mass spectrometry coupled methods. The MauriceFlex™ fractionation enables direct analysis of collected fractions without any mass spectrometry sample preparation for extended characterization.

In addition, MauriceFlex™ provides great freedom and flexibility to a scientist by enabling routine cIEF and CE-SDS assays on the same system that can further characterize the charge variant peaks with fractionation and mass spectrometry. At the WCBP conference, a major international biotech company presented their MauriceFlex™ data to evaluate the thermal degradation pathway of a therapeutic dual variable domain antibody called DVD-Ig™. They used MauriceFlex™ fractionation followed by MS characterization of the charge variant fractions to identify the modification(s) responsible for the thermal degradation.