Western blotting, immunoprecipitation, & immunofluorescence microscopy all have what in common? involve the use of antibodies require the use of an SDS-PAGE gel before they are performed give information about protein secondary structure (alpha helices and beta strands) give information about protein molecular weight

Answer

involve the use of antibodies

Explanation

Western blotting detects proteins in a sample by denaturation and then running through gel electrophoresis. In western blotting, the unbound antibodies are washed away, leaving the tightly bound antibodies to the protein of interest. Immunoprecipitation isolates specific proteins from a sample containing thousands of different proteins, through the use of antibodies that can bind specifically to the target protein. Immunoprecipitation uses antibodies to remove specific protein antigen out of the solution. Immunofluorescence microscopy uses fluorophores like the soluble organic dyes and can use antibodies to detect the distribution of proteins, and other antigen targets.