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RedShiftBio Launches New Protein Characterization Instrument System - AQS3pro

publication date: May 24, 2018
 | 
author/source: RedShiftBio

RedShiftBio AQS3pro


See Change with the new AQS3pro System for protein characterization from RedShiftBio.

One highly automated system, five key measurements: Aggregation, Quantification, Stability, Structure and Similarity. RedShift™ BioAnalytics, Inc. (RedShiftBio™) launch the AQS3™pro, a new protein characterization platform with powerful, integrated bioanalytics software that delivers automated, high sensitivity spectroscopic analysis for the development, formulation and manufacture of biotherapeutics.

The AQS3pro allows users to ‘see change™’ in the secondary structure of proteins over the concentration range of 0.1 to 200 mg/mL, providing the Aggregation, Quantification, Stability, Structure and Similarity measurements that underpin drug safety and efficacy. Its ability to provide multiple attribute data reduces or eliminates the need for performing separate measurements across different tools. Combined with its advanced automated multi-sample capability, the AQS3pro substantially streamlines the analytical workflow associated with the commercialization of biotherapeutics.

‘The AQS3pro is an important advance in biophysical characterization technology that transforms the utility of IR spectroscopy for biotherapeutic analysis,’ said Dr. Eugene Ma, CTO, RedShiftBio. ‘Its introduction is the culmination of first rate R&D by our in-house team coupled with extensive input from a network of industrial and academic collaborators. The accuracy, repeatability and reproducibility of the new system has been verified across hundreds of samples, involving thousands of protein measurements.  These data and the enthusiasm of contributing partners underpin our confidence in its considerable value to the industry.’

The AQS3pro uses the patented technique of Microfluidic Modulation Spectroscopy (MMS) which combines mid-infrared laser spectroscopy with microfluidics and advanced signal processing to measure the secondary structure of proteins. It provides direct, label-free measurements over the concentration range 0.01 to 200 mg/mL, characterizing samples under all the conditions routinely encountered in biopharmaceutical development and manufacture, without sample dilution.

Measurement is highly automated, with workflow efficiency further boosted by multi-sample, walk-away operation and state-of-the-art bioanalytics software. The innovative and flexible analytics suite automates the routine analysis of spectroscopic data, at the same time providing improved tools for gaining insights into structural change and its implications.

‘We have been partnering in the testing of the AQS3pro’, said Professor Christopher Roberts of the University of Delaware. ‘The application of MMS and infrared spectroscopy for protein solutions offers the ability for simultaneous and in situ quantification of secondary structural changes and protein concentration across a broad range of protein concentrations, and a wide range of sample conditions.  This tool will be extremely useful for scientists and engineers spanning from basic protein science to biologic product development.'




 

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