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AQS3™pro is the most recent protein characterization platform with integrated bioanalytics software that provides automated, sensitive spectroscopic analysis for characterization of secondary structure of proteins. The AQS3pro uses the patented technique of microfluidic modulation spectroscopy (MMS) which combines mid-infrared laser spectroscopy with microfluidics and advanced signal processing providing direct, label-free measurements over the concentration range 0.01 - 200 mg/mL. Designed for five key measurements - aggregation, quantitation, stability, similarity, structure, the AQS3 directly supports protein characterization throughout the biopharmaceutical development workflows.

Advantages of Microfludic Modulation Spectroscopy(MMS)

MMS is a novel and efficient technique for label-free protein analysis that directly addresses the limitations of current technologies. MMS provides drift-free, background subtracted, high sensitivity measurements of the protein secondary structure across four decades of concentration—from 0.1 to over 200 mg/mL.

  • Automated multi-sample analysis for walk away operation
  • High sensitivity to see change reproducibly at high precision
  • The widest concentration range to characterize biotherapeutics
  • Analytical software that easily transitions data into insight

See Change In Your Protein Characterization Workflow.

Quantitation: Proteins can be quantified over a linear concentration range that extends from 0.01 to > 200 mg/mL

Differential Absorbance Spectra: Continuous, rapid modulation between the sample solution and buffer reference streams produces a differential absorbance signal.

Absolute Absorbance Spectra: Buffer subtraction and concentration normalization enable direct protein-protein structural comparisons

Second Derivative Spectra: Second derivative spectra accentuate the specific structural differences between protein samples

Delta of Second Derivative: Delta of second derivative plots highlight structural differences and change in protein samples

Stability: Protein stability can be assessed by tracking changes in secondary structure motifs

Similarity: Protein similarity can be compared using area of overlap plots

Higher Order Structure: Higher order structure analysis quantifies the fractional content of different secondary structure motifs.

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