The microtubule-associated protein, tau, has previously been found to be one of the major components of neurofibrillary tangles, a hallmark of Alzheimer’s disease; however, the exact mechanism through which tau dissociates from microtubules (MTs) and forms these neurotoxic aggregates is not fully understood. Previous studies have shown that tau can undergo liquid-liquid phase separation (LLPS) in vitro in the presence of polyanionic biomolecules found in cells, such as RNA, suggesting a possible intermediate between MT-bound tau in health and aggregated tau in the disease state. Due to the complexity of interactions and forces driving coacervation, the Safinya group is interested in developing fundamental knowledge of this phenomena as it pertains to tau functionality. We have provided evidence that tau coacervation may also be induced under various other conditions, such as in the presence of GTP and even by itself in solution. This has been done by recombinantly expressing and purifying certain isoforms of tau protein and using it to perform microscopy experiments which have helped us learn about the physical properties of LLPS tau. Here we present results from purifying and labeling our protein as well as preliminary data from DIC and fluorescence microscopy. By building off of these results, we hope to use this experimental platform to bring us closer to understanding the exact mechanisms through which neurofibrillary tangles develop in individuals with Alzheimer’s disease.