RedShiftBio Aurora TX is a one drop, thermal ramping solution for protein and RNA characterisation of structure and stability.


RedShiftBio Aurora TX is a one drop, thermal ramping solution for protein and RNA characterisation of structure and stability.

Manufacturer RedShiftBio
Product Series Aurora
Measurement principle Microfluidic Modulation Spectroscopy (MMS)
Application Protein Conformation
Sample type Proteins, Peptides, mAbs, ADCs, AAVs, and mRNA
Low sample consumption 50 µl sample volume
Concentration range0.1 mg/mL to >100 mg/mL

Product Overview

The RedShiftBio Aurora TX, powered by Microfluidic Modulation Spectroscopy (MMS), fully characterises the structure and stability of RNA, proteins, peptides, and other biomolecules at the touch of a button, including thermal ramping to unlock a greater wealth of insights than ever before.

RNA and LNP analysis with MMS
Building on the existing capabilities of the Aurora, the Aurora TX makes analysing RNA structure effortless, using nearly drift-free, background compensated scans of the Amide I band (1700-1600 cm-1), typically used on proteins, but also ideal for nucleic acids. Aurora TX overcomes challenges of traditional spectroscopic techniques, such as manual workflows, buffer interference and background subtraction to enable easy detection and comparison of RNA changes that are vital for therapeutic development.

MMS technology delivers multiple measurements in a single analysis, unveiling a wealth of insights including structural changes, stability, concentration variations, and RNA-to-LNP ratio, all with walk-away automation.

Furthermore, robust delta software offers users an uncomplicated approach to RNA structural data collection and interpretation of results – no spectroscopy expertise needed. Aurora TX is easy to use, and automation makes it easy to generate a lot of data quickly for any application. Users can just pipette samples and matched buffer into a standard 96-well plate and the Aurora TX wizard walks you through getting your run started. Additionally the optional buffer station can enhance the ease of use and sample throughput.

  • Demonstration video
  • Benefits
  • Applications

Demonstration video


Key features of Aurora TX include:

  • Ultra-sensitive and highly reproducible structural measurements
  • Wide applicability across many therapeutic modalities
  • 50uL of sample at 0.1mg/mL is all you need for highly reproducible data
  • Thermal ramping capability for controlled temperature stress/stability assessments
  • Walk-away automation with multiple measurements in a single analysis
  • Robust delta software for simplified data collection and interpretation
  • New, streamlined optional buffer station that enhances throughput by integrating up to 8 buffers directly into the system during analysis


Secondary structure and thermal ramping capability
Characterise the structure of a wide range of biomolecules including RNA, LNPs, proteins, peptides, antibodies, ADCs, and AAVs by measuring change in stability due to buffer/pH/formulation, stress, point mutations, binding, and storage time/conditions.Thermal ramping applies stress in a repeatable and automated fashion to induce structural change and guide decision-making and candidate ranking, saving valuable R&D time.

Aggregation – This is a common indicator of protein instability, which can result in a therapeutic product being unfit for launch. MMS is one of the only techniques which can directly monitor the formation of aggregates due to its ability to measure intermolecular beta-sheet structures.

Quantitation of protein concentration – The structure and behavior of proteins in solution can be a function of their concentration, therefore the ability to accurately quantify protein concentration allows better comparison between different proteins and formulations. MMS’s high resolution (<0.001 cm-1) and low stray light susceptibility increases the linear concentration range for the measurement by more than 2 orders of magnitude. With a minimum measurable concentration of less than 10 μg/mL and an upper limit of greater than 200 mg/mL, this technique offers a significant improvement over conventional absorbance-based assays.

Protein Higher Order Structure (HOS) – During manufacturing, biopharmaceutical proteins may undergo conformational changes which can alter their secondary structure and therefore their function. MMS has the ability to detect these changes with great sensitivity, in the formulation buffer and at the concentration of interest, without the need for dilution or deuteration. MMS offers detailed information on which structural motifs in the protein molecule are changing, to help guide the development of more stable protein molecules and formulations.

Protein Stability – Measuring how stable a protein is to thermal or chemical exposure during manufacturing and storage is critical. Structural changes can lead to decreases in potency, degradation of the product, and increases in impurities and aggregates which can be extremely harmful. MMS technology enables the accurate assessment of the stability of the protein throughout the entire formulation, development, and manufacturing process, reducing risks and enabling control strategies for each critical quality attribute (CQA).

Biosimilarity – Along with functional comparisons, measurement and analysis of the structural similarity between proteins is an effective method of demonstrating bioequivalence. MMS measures protein secondary structure, reveals very small conformation differences between different proteins, and provides information as to where those differences occur. These capabilities make MMS a powerful tool in the analysis and development of biosimilars.


Product Enquiry


If you would like to enquire about this product, fill out this form and one of our product specialists will contact you shortly.
If you need help in the operation or repair of an instrument then please contact the Customer Help Centre directly.

Please note, product enquiries are only applicable to Australia, New Zealand, Papua New Guinea and Fiji

    Or call us instead at (02) 9541 3500