The minimal sample prep, easy-to-use design and wide dynamic range means you will spend less time setting up, and more time generating the data you need.
Solution state measurement coupled with high sensitivity means you can study proteins that are problematic for other systems including membrane proteins, multi-protein complexes, and intrinsically disordered proteins.
Work in crude biological mixtures with minimal preparation, while controlling for off-target binding. Gain valuable insights at the earliest possible stage.
Study protein-protein, protein-DNA and protein-lipid interactions in biological mixtures such as crude lysates of blood plasma. No surface binding means no artefacts so you can study proteins in near native state with no risk of non-specific binding.
In the process of calculating the binding affinity of an interaction the Fluidity One-W provides the hydrodynamic radius (Rh) of both the unbound labelled species and the complex. The hydrodynamic radius can be used to infer the stoichiometry of the protein complex and the overall conformational arrangement in solution.
There is a number of other techniques that are currently used to determine protein binding affinity, all with their own strengths and weaknesses, the Fluidity One-W is no different. We believe it should be a tool in your arsenal to compliment other methods, but you need to know how it compares to the other techniques.
Get in touch with our scientists to discuss if our technology could work for you.
Fluidity One-W highlights
Range (hydrodynamic radius)
0.7 – 20 nm
Range (molecular weight)
0.5 kDa – 14 MDa
CV < 10%
1 nM Alexa Fluor™ 488
Volume per measurement
Small proteins and peptides — 8 minutes
Large proteins — 14 minutes
Compatible with pure buffer or crude lysates
Runs per reagent cartridge
Dimensions (D x W x H; cm)
40 x 40 x 43
GFP, FITC, Alexa Fluor™ 488 and equivalents