Fast expression screening that reveals expression levels of properly folded recombinant proteins

Protein expression and production teams in the pharmaceutical industry, CROs, and other protein service providers spend a lot of time and resources trying to identify the optimal conditions for high expression levels of recombinant protein. The process is generally tedious and inefficient, often driven by trial and error, especially for novel targets. It’s clear that knowing early on if a recombinant protein is not only highly expressed but also structurally stable would make protein production teams more efficient by lowering cost, providing actionable insights at the small-scale stage, and allowing faster hand-over of high-quality proteins to clients or teams downstream. This case study compares the evaluation of expression conditions of His-tagged HRV3C protease expressed in E.coli using data from traditional SDS-PAGE and the Andromeda system.

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Analyze self-interaction to predict viscosity and aggregation propensity at higher concentrations
Analyze self-interaction to predict viscosity and aggregation propensity at higher concentrations

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Measure binding affinities for any type of interaction — examine a label-free or labeled target molecule at anytime
Measure binding affinities for any type of interaction — examine a label-free or labeled target molecule at anytime

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