The utilization of sodium oleate in membrane protein research is noteworthy for its unique surfactant properties. As an anionic surfactant derived from oleic acid, sodium oleate possesses an amphiphilic structure, consisting of a hydrophobic tail and a hydrophilic head. This characteristic enables it to interact with both hydrophobic regions of membrane proteins and the surrounding aqueous environment. Sodium oleate's surfactant nature, reducing surface tension and forming micelles, makes it particularly effective in solubilizing membrane proteins, including those embedded within lipid bilayers. Its applications extend to biochemistry, where it aids in the extraction and stabilization of membrane proteins, as well as colloid chemistry, where it contributes to the stabilization of colloidal dispersions. Additionally, sodium oleate finds industrial uses, playing a role in soap manufacturing and acting as a flotation agent in mineral processing. Researchers leverage sodium oleate's amphiphilic and surfactant characteristics to facilitate the study of membrane proteins, enabling their extraction, solubilization, and subsequent analysis for a comprehensive understanding of their structure and function in biological systems.