AbstractSodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting are complementary methods for separating and detecting the presence of a specific protein from a complex mixture. Proteins, from a cell extract, for example, are separated electrophoretically through a polyacrylamide gel. Next, these are transferred onto a nitrocellulose membrane by electrical current, preserving the original banding pattern from the gel. The membrane is probed with an antibody specific for the protein of interest, forming an antibody-antigen complex that can be visualized by a variety of techniques. This chapter outlines a procedure for the analysis of a specific protein(s) from cultured, asexual stage Plasmodium falciparum by SDS-PAGE and Western blotting, using a minigel system. The entire procedure can be completed in one day. Most of the methods outlined below are applicable to proteins from a wide variety of sources.KeywordsSodium Dodecyl SulfateInner CoreAmmonium PersulfateTransfer BufferPlastic WrapThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.