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.