Immunodetection of Proteins by Western Blotting

Abstract

The technique of protein immunoblotting, more commonly known as "Western" blotting, was first described a decade ago by Towbin et al., (1), using electric current to transfer polypeptides from polyacrylamide gels to nitrocellulose, although several groups had previously reported the use of capillary forces to effect the transfer of DNA ("Southern" blotting [2]), RNA ("Northern" blotting [3-5]), and protein (6,7) from agarose and polyacrylamide gels.