Protein quality control is the most crucial checkpoint of any protein production and characterization process. All too many experiments end up unsuccessfully due to poor quality protein. Not only do you risk that useful data is not generated, but significant amounts of time can be lost on troubleshooting assay design without reliable insight to the protein itself. It is therefore highly valuable to have in-depth confirmation that the protein you work with behaves as in its native state. Typically, a set of different techniques needs to be employed prior to running an assay to gain insights into the state and condition of a given protein sample. Flow induced dispersion analysis (FIDA) is an immobilization-free ligand binding methodology employing Taylor dispersion analysis for measuring the hydrodynamic radius (size) of biomolecular complexes. The Fida 1 instrument offers great advantage for deciphering a wide array of quality control (QC) parameters. With Fida 1, these parameters do not have to be measured in a separate assay in advance of your experiments but are integrated in every measurement you perform. Combining these QC parameters with Fida 1 assays being tolerant to any type of buffer composition and consuming only nanoliter (nL) sample volume, is resulting in an assay robustness that cannot be achieved with any other technology. Flow induced dispersion analysis can measure the absolute in-solution size of your molecule in nanometers, quantifying sample aggregation and viscosity, identifying sample stickiness, defining the heterogeneity of a sample via the polydispersity index, and identifying free versus conjugated fluorophores in labelled samples.