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

Abstract 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 extract...
Ausführliche Beschreibung

Abstract 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. Ausführliche Beschreibung