Q: How to check if proteins were transferred efficiently from a gel to a membrane?

     The procedure is fast and simple. After completion of a transfer, the gel is placed in a protein stain, as Coomasie R250, for a quick confirmation if any bands are still left in a gel. 

    Presence of bands confirms non-complete transfer, which may impact detection of a target protein, especially if bands in the blot are in the MW range of a target protein. 

    The aim is, to adjust transfer conditions, in terms of time and voltage to allow complete transfer from a gel to a membrane in the MW range of a target protein, which is later to be visualized on the blot using specific antibody. 

    This simple and fast method, to check the gel for the remaining protein bands, will help to secure that applied transfer conditions allow proteins to efficiently leave the gel. 

    Note: keep in mind, that depending upon MW of a transfer protein which is aimed to be detected, specific transfer conditions need to be adjusted, which is described here:

    How to transfer low and high molecular weight proteins

      Which membrane to chose?



         Gel check for protein transfer efficiency

      In this example, proteins from two different gels were transferred to PVDF membrane in a double sandwich. Following the transfer, each gel was stained in Coomasie R250 to confirm if proteins were efficiently transferred from a membrane. 

      The second gel showed bands, which means, that the transfer was not complete. 
      Double sandwich is not recommended for quantitative Western blot, as transfer efficiency may not be complete. 

       Technical tips

      Technical tips


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