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Western blotting (also called immunoblotting, because an antibody is used to specifically detect its antigen) was introduced by Towbin, et al. in 1979 and is now a routine technique for protein analysis. The term “blotting” refers to the transfer of biological samples from a gel to a membrane and their subsequent detection on the surface of the membrane.
Western blotting can produce qualitative and semi-quantitative data about the protein of interest. It is an important technique used in cell and molecular biology. It enables the researchers to identify the specific protein from a mixture of proteins extracted from cells as well as evaluate their size and amount.
Western blotting (protein blotting or immunoblotting) is a rapid and sensitive assay for the detection and characterization of proteins. It is based on the principle of immunochromatography where proteins are separated into polyacrylamide gel according to their molecular weight.

Electrophoresis is a common lab technique used to identify, quantify, and purify nucleic acid fragments. Samples are loaded into wells of an agarose or acrylamide gel and subjected to an electric field, causing the negatively charged nucleic acids to move toward the positive electrode. Shorter DNA fragments will travel more rapidly, whereas the longest fragments will remain closest to the origin of the gel, resulting in separation based on size.