T-cells are critical cells in the immune system, responsible for the coordination, development, and eventual suppression of an immune response in the presence of potentially harmful pathogens. T-cells detect antigens using T-cell receptors (TCRs), resulting in initiation of appropriate immune responses. Upon activation of mature T-cells, a protein called Nur77 is upregulated alongside other cellular functions including proliferation and acquisition of effector functions. During development of immature T-cells, Nur77 assists in apoptosis. Thus, the exact functions of Nur77 in different types of T-cells is unclear. In order to elucidate the role of Nur77 in T-cells, it is important to learn with which other proteins Nur77 interacts. Previously, our group used a yeast-two-hybrid (Y2H) screen to identify novel proteins that may interact with Nur77 in different types of T-cells. This study began to develop the appropriate protocols to confirm the Y2H findings: 1) bimolecular fluorescence complementation (BiFC) and 2) purifying His-tagged proteins. BiFC involves a circular DNA called a plasmid containing two portions that specify the instructions for making half of the Green Fluorescence Protein (GFP). DNA coding for Nur77 was added to one half of GFP and DNA coding for Notch1, a known binding partner for Nur77, was added to the other half of GFP. Once DNA coding for both proteins is added to the BiFC plasmid, we can use this system as a positive control for protein binding with unknown interactors. For the second goal, we used multiple protocols to determine which was most effective for purifying His-tagged proteins in the future by first purifying the His-tag on it’s own. These experiments pave the way for future confirmation of novel protein:protein interactions with Nur77.