Protein-protein interaction

In-solution Biophysics - Fida neo

One technology to measure: affinity (from pM to mM), kinetics, quantity, 8 quality control parameters per data point (Absolute size measurement Rh, aggregation, viscosity, stickiness, PDI, labelling quality, PDB correlator & sample loss). With as little as 4 uL analyte with fixed 40 nL indicator, you can save material & effort, minimise assay development time and expands the range of possible biological systems to be characterised. You have an option of switching detectors while using a single base instrument (label-free or labelled, 280nm or 480nm respectively).

Key Features:

• Affinity assays, as well as stoichiometry validation and oligometric/structural state of proteins.
• Size changes of less than 5% in hydrodynamic radius are detectable, has a dynamic size ranging from 0.5 to 500nm Rh.
• No immobilization: in-solution nature of FIDA allows for access to all binding sites - no more non-specific binding issues.
• No constraints: crude or purified samples, any pH, ionic strength limits, detergents or buffers.
• No regeneration: eliminates risk of denaturing immobilised protein. Allows for fast determination of slow off rates for high affinity interactions.