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  • What is polyacrylamide gel electrophoresis?
  • The most commonly used polyacrylamide gel electrophoresis for quantitative protein analysis is Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The polyacrylamide gel forms by polymerizing acrylamide and a crosslinking agent, i.e., N, N’-methylene-bis-acrylamide.
  • What is sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE)?
  • The method is called sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). SDS (also called lauryl sulfate) is an anionic detergent; the negative charges on SDS destroy most of the complex structure of proteins and are strongly attracted toward an anode (positively charged electrode) in an electric field.
  • How do proteins migrate in polyacrylamide gel electrophoresis?
  • In polyacrylamide gel electrophoresis, proteins migrate in response to an electrical field through pores in a polyacrylamide gel matrix; pore size decreases with increasing acrylamide concentration. The combination of pore size and protein charge, size, and shape determines the migration rate of the protein.
  • What is the difference between agarose gel and polyacrylamide gel electrophoresis?
  • In polyacrylamide gel electrophoresis, polyacrylamide gel separates macromolecules, i.e., proteins of size five kDa to 250 kDa. Similarly, it can also isolate DNA of 5- 500 bp size. In agarose gel electrophoresis, agarose gel separates DNA, RNA, and protein. It can isolate DNA about 50-20,000 bp in size.