Dynamic isoelectric/anisotropy binding ligand assay (DIABLA) is a new method to identify proteins in a complex sample that bind to a molecule of interest. This is accomplished by first using dynamic isoelectric focusing (dynamic IEF), which is a new technique that is related to capillary isoelectric focusing but uses additional high-voltage power supplies. The additional supplies provide control over the shape of the electric field within the capillary. Manipulation of the electric field changes the pH gradient, enabling both the location and width of the focused protein bands to be controlled. When the proteins are focused the entire capillary is scanned to identify regions of non-zero anisotropy, which are locations where the molecule of interest is binding to a focused protein band. The binding proteins can then be isolated using the fractionation capabilities of dynamic IEF and identified using various analytical methods. This poster will present the theory behind DIABLA and will show proof of concept data demonstrating the binding of fluorescently-tagged progesterone to human progesterone receptor (HPR) and myoglobin. The proteins were tagged with a different fluorophore and then focused in the presence of progesterone. Fluorescence measurements show the uniform presence of progesterone and the two focused protein bands. Anisotropy measurements shows that progesterone binds to HPR and not myoglobin.