Biotechnology and Bioinformatics (1+1)

Introduction

The transfer of protein bands from an acrylamide gel onto a more stable and immobilizing support is called as protein blottin or western blotting . The western blot was described by W. Neal Burnette, of Fred Hutchinson Cancer Research Center in Seattle, Washington(1981). Western blotting is commonly used to positively identify a specific protein in a complex mixture and to obtain qualitative and semi quantitative data about that protein. This method is, however, dependent on the use of a high-quality antibo dy directed against a desired protein. A variety of analysis involving immunoblotting, DNA binding proteins, and glycoproteins could then be performed on the proteins blotted onto the filters. This method is an extension of the “southern blot” used to transfer DNA from gels to nitrocellulose filter and is called as the “western blotting”. The benefits of a protein blot include rapid staining/destaining, detection of proteins at low concentrations and rapid localization of the proteins in preparative gels. The blot can be preserved as a replica of the original gel. The transfer of proteins is carried out either by electrophoresis (electroblotting) or by the capillary action of buffer (capillary blotting).