For a list of peer-reviewed articles our products have been cited in, check out the publications page.
This document details the benefits and advantages of the Maurice system compared to iCE3.
new general catalog in Japanese 2021
Simple Plex assay for the detection of mouse and rat Fibroblast
Growth Factor 21 (FGF-21) in cell culture supernatant (CCS)*,
serum, and plasma (EDTA/Heparin)
*CCS are validated for mouse samples only.
Simple Plex assay for the detection of mouse CXCL15/Lungkine in
cell culture supernatant (CCS), serum, plasma (EDTA/Heparin), and
bronchoalveolar lavage fluid (BALF)
See why leaders in regenerative medicine and cell therapy research use Simple Western™ and Single-Cell Western.
Simple Plex assay for the detection of human Tissue Inhibitor of
Metalloproteinases 2 (TIMP-2) in cell culture supernatant (CCS),
serum, plasma (EDTA/Heparin), saliva, and urine
Utilizing Waters’ Open Interface Portal (OIP) for multi-vendor hardware control, ProteinSimple’s Maurice Empower® Control Kit enables seamless control of the Maurice platform with all key functions preserved and with full regulatory compliance, including 21 CFR Part 11 controls for industry-leading security and data integrity.
Simple Western was used to separate proteins by charge and size to evaluate the pharmacokinetic properties of adalimumab and two adalimumab biosimilars in human serum.
Viral capsid content can impact gene therapy product efficacy and is therefore considered a Critical Quality Attribute (CQA) that must be properly evaluated during the development and manufacturing of AAVs. Traditional analytical tools such as transmission electron microscopy (TEM), analytical ultracentrifugation (AUC), and ion-exchange chromatography (IEX) can be used to characterize capsid content but are complex, labor-intensive, and pose challenges in data reproducibility, throughput, and scalability. In this application note, we show how imaged-capillary isoelectric focusing (icIEF) technology on Maurice can be used to characterize empty, intermediate and full AAV capsids at native and stability screening conditions, providing robust and reproducible data. With this, Maurice provides crucial data to aid in developing the right formulation for AAV therapeutics.
Therapeutic monoclonal antibodies (mAbs) make up a large portion of the rapidly growing drug market. Ensuring safety and efficacy through comprehensive understanding of these products’ critical quality attributes (CQAs), including charge heterogeneity, is a regulatory requirement. Various charge isoforms of mAbs can result from cell culture or production processes, potentially affecting the mAb structure and function. While imaged capillary isoelectric focusing (icIEF) is the preferred method for charge profiling, ion-exchange chromatography (IEC) has been the major tool for fractionation combined with characterization. However, IEC is not compatible with certain types of molecules, hydrophobic antibody drug conjugated (ADCs) for example, and icIEF typically provides higher separation resolution. Moreover, an individual charge variant obtained from IEC fractionation may not be comparable to the variant peak in the icIEF profile. Therefore, there is an unmet need for IEF-based fractionation of charge variants for characterization.
We have developed a novel icIEF fractionation solution, which involves icIEF separation and collection of charge variants. This solution enables Maurice icIEF-based peak identification followed by downstream analysis. Here we report icIEF fractionation followed by ZipChip-based mass spectrometry (MS) characterization of the NIST mAb and XMT-1535 mAb. ZipChip (CE-ESI) was utilized for mass spectrometry characterization of the fractions due to its broad sample matrix compatibility, easy sample prep, and fast mass spectrometry analysis time. Individual charge variants of each antibody were successfully collected in less than 2 hours with purity > 80% using icIEF separation conditions with or without urea. Rapid analysis using ZipChip chowed the mass spec identification of major and minor isoforms correlated well with reported mass spec data (literature and report). Urea in icIEF separation did not affect the quality of fractionation nor the mass spec result. Multiple fractionation runs of the NIST mAb suggested good reproducibility of the system. We believe this novel icIEF fractionation solution coupled with other analysis methods, such as mass spectrometer, will deliver a powerful charge variant characterization tool for biotherapeutic analytical tool kit.