Applications

A growing range of applications using Microfluidic Diffusional Sizing

The Fluidity One offers scientists a unique combination of capabilities not found in other protein characterisation approaches. The ability to study proteins in their native state, in solution, quickly and with very little sample is advantageous in a variety of research areas. Select from the application areas below to learn more.

Application Notes

  • Application note

    Oligomerization of Interleukin-2

    A commercially available human interleukin-2 is assessed by microfluidic diffusional sizing on the Fluidity One across a dilution series. The hydrodynamic radius is observed to increase with increasing concentration, in a way which suggests a monomer-trimer equilibrium with positive cooperativity is established.

  • Application note

    Interleukin-2 stability in changing buffer and temperature conditions

    The stability of interleukin-2 in different buffers and storage temperatures is evaluated using the Fluidity One. We find that IL-2 forms aggregates within 24 hours in some buffers, and that the Fluidity One provides a simple means to evaluate the stability of proteins across different conditions.

  • Application note

    A comparison of Microfluidic Diffusional Sizing with Dynamic Light Scattering and Taylor Dispersion Analysis

    The established technologies of Dynamic Light Scattering (DLS) and Taylor Dispersion Analysis (TDA) are compared to Microfluidic Diffusional Sizing (MDS) for sizing proteins of varying molecular weights and at varying concentrations. We show that MDS offers comparable sizing of proteins over a range of sizes, and can provide consistent sizing to lower concentrations than the other techniques.

  • Application note

    Detecting insulin oligomerisation using microfluidic diffusional sizing

    Insulin monomers self-assemble into hexamers, which is known to affect its level of uptake in the human body. Here we show that Microfluidic Diffusional Sizing (MDS) can be used to detect these changes.