Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers

Proteome profiling is most commonly based on a two-dimensional gel electrophoresis to separate and visualize proteins for identification. The success of a proteomic experiment is critically dependent on the sample preparation. The two most effective and widely used lysis buffers for extracting proteins from cells and tissues are Radio-Immunoprecipitation Assay buffer (RIPA buffer) and Urea lysis buffer. These buffers are rapid and highly efficient for cell lysis and good solublization of a wide range of proteins. In this study, the proteome profile of Rabbit muscle and tendon was analysed by 2-D gel electrophoresis using RIPA buffer and Urea lysis buffers. The variations in lysis buffers for extracting proteins clearly improve the resolution of protein identification spots as compared to conventional methods.