Electrochemical impedance spectroscopy (EIS) is a valuable research tool that provides accurate kinetic and mechanistic information from repeatable adsorption and desorption measurements on the surface of a sensor. The surface is represented as an electrode that exhibits both resistive and capacitive properties when a small amplitude sinusoidal excitation is used to perturb the system at equilibrium. Traditional theory from electrochemistry that describes the rates of reactions and other processes occurring at the electrode surface can be applied to biological systems. Consequently, the use of affinity-based biosensors in EIS is attracting interest. This allows for direct and label-free electrochemical immunosensing, potentially speeding up detection and analysis of biomarkers. In this study, EIS was used to develop protocols for sensing antibody-antigen interactions in protein-doped saline solutions. Specifically, EIS allowed identification of the appropriate conditions (AC frequency, DC potential) that would allow the most direct assessment of binding to the sensor. The impedances of gold electrodes in aqueous electrolyte were measured over time at the desired potential and AC frequency. The gold electrodes were modified by attachment of a self-assembled monolayer of 16-mercaptohexadecanoic acid (MHA) that was used to immobilize the antibody on the electrode. Initial experiments tracked antibody-antigen binding and/or fouling of the immobilized antibody sensor surface by bovine serum albumin (BSA) in phosphate buffered saline (PBS). Binding kinetics was modeled for both antibody-antigen interactions and non-specific protein adsorption.