![]() Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to NC sheets: procedure and applications. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis.The scientific community is now confronted with a variety of ways and means to carry out this transfer. Since the inception of this protocol in 1979, protein blotting has evolved greatly. This allowed analysis of specific proteins on the membrane using antibodies in a procedure called immunoblotting. The transfer produced a replica of the protein pattern in the gel to membrane support. This is where the procedure of western protein became a powerful and important procedure for studying proteins following electrophoresis, particularly proteins that are of low abundance. Therefore, there was a need to transfer the gel’s proteins to more stable support that could be accessed easily with antibodies. Also, the gel is fragile and can be easily broken when handled. The usefulness of the high separating power of sodium dodecyl sulfate-polyacrylamide gel electrophoresis was limited because the gel matrix’s separated proteins were difficult to access with antibodies or other probes. The cell contents, which include a mixture of proteins, are first separated from each other according to the protein’s size on a gel using a procedure called gel electrophoresis. Cells obtained from tissues or cells grown outside the human body in a plastic flask are first busted to release its contents. How do we identify every protein in the cell? This question vexed many scientists until the introduction of the procedure known as protein blotting or Western blotting.
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