Celine Pompéia , Fernanda Ortis and Mari Cleide

نویسنده

  • Celine Pompéia
چکیده

whereas the recognition of c-Fos (a protein of the same family as Fra-1), MS2-polymerase (the protein in fusion) and β-galactosidase (a nonspecific protein that allows to control for nonspecific anti-Fra-1 reactivity as well as its reactivity to contaminating bacterial proteins) decreases. These results are confirmed by the Western blots shown in Figure 2, where anti-Fra-1 antiserum recognition of Fra-1 protein is significantly higher after immunopurification, with c-Fos recognition practically disappearing. Western blot assays also show that recognition of the MS2-polymerase protein levels decrease upon purification (data not shown). Figure 1B shows the results of purification of the anti-c-Fos antiserum by adsorption to extracts from bacteria producing MS2-polymerase-Fra-1. These results also show reproducible enrichment of the purified antibody response to c-Fos. Therefore, two specific antisera against two closely related proteins (cFos and Fra-1) were generated using this combined technique. These antisera are being used in our laboratory to investigate the role of c-Fos and Fos-related proteins in polyomavirus-induced malignant transformation (M.L.S. Oliveira and M.C.S. Armelin, unpublished).

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تاریخ انتشار 1999