A novel use for coomassie brilliant blue (R-250) in protein gel-drying procedure and assessing the electro-transferring efficiency

The present study provides an alternative method for protein-gel drying. Rat brain protein extracts were separated using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by staining with coomassie brilliant blue (R-250). The stained gel was then subjected to electroblotting on nitrocellulose membranes. This method exhibited four advantages: 1) it eliminated problems associated with gel-drying (e.g., shrinkage of gel), 2) it allowed assessment of the efficiency of electro-transfer, 3) it significantly reduced the time of gel-drying procedure by an average of 40 minutes and 4) it facilitated visualizing electro-transferred proteins with the same efficiency as the common amidoblack staining technique. In conclusion, the described method is simple, economical and introduces several applications.