In the early 1980s, cell biologists kept slamming into the same obstacle when they tried deploying antibodies to elucidate the working of the Golgi complex. True, use of antibodies to identify proteins (Bader et al., 1982; de Camilli et al., 1983a,b; Huttner et al., 1983; Weiss et al., 1984; Woodcock-Mitchell et al., 1982; Yen and Fields, 1981), localize cellular structures (Levine and Willard, 1981), and differentiate cell types (Schnitzer et al., 1981; Skene and Willard, 1981) was booming. The difficulty was crafting antibodies to target exclusively proteins from the Golgi complex, recalls Graham Warren (now at Yale University, New Haven, CT). Even the purest mixtures of Golgi membranes contained contaminants, such as shards of cell membrane, and stimulated production of antibodies that labeled non-Golgi structures. Warren and his colleagues Daniel Louvard and Hubert Reggio, all then at the European Molecular Biology Laboratory in Heidelberg, Germany,...

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