This research focused on the analysis of proteins through a two-step process: the isolation of proteins from tissue samples using the RIPA (Radioimmunoprecipitation assay) buffer method, followed by the estimation of protein content utilizing the Bradford method. The RIPA buffer, known for its ability to solubilize various cellular components, was employed to break down cell membranes and liberate proteins from the tissue samples. This process was optimized to ensure maximum protein extraction efficiency. Subsequently, the concentration of the isolated proteins was determined using the Bradford method, a colorimetric technique that relies on the interaction between Coomassie Brilliant Blue dye and proteins. The intensity of the color change was measured at a specific wavelength and correlated with the protein concentration. This method allowed for quick and relatively simple quantification of the protein content. The outcomes of this study showcased the successful isolation of proteins from tissue samples and their subsequent quantification using the Bradford method. The results shed light on the protein composition of the samples, providing valuable information for further downstream applications. This comprehensive analysis contributes to the broader understanding of protein analysis techniques, enhancing their applicability in fields such as molecular biology, biotechnology, and medical research." Furthermore, to delve deeper into the protein composition, SDS-PAGE was conducted. This technique separates proteins based on their molecular weight in a polyacrylamide gel matrix. The addition of Sodium Dodecyl Sulfate (SDS) denatures the proteins and imparts a negative charge, allowing for uniform migration during electrophoresis. The resulting gel revealed distinct protein bands corresponding to different molecular weights, enabling the assessment of protein integrity and potential presence of multimeric complexes.