Fig. 4.
Fig. 4. Expression of exogenous FasLs in transfected 3DO cells. The FasLs transfection was controlled by RT-PCR using as primer forward the T7 eukaryotic and as primer reverse the n. 3 shown in Fig 2A or using as primer forward the T7 eukaryotic and as primer reverse the SP6 eukaryotic. Each RT-PCR reaction (+) was controlled by using the respective RNA without the addition of reverse transcriptase (−) (B). The FasLs transfection was also controlled by immunoprecipitation with anti-FasL–COOH Ab of cell lysates (C) and supernatants (D). Western blotting of the GST-FasLs fusion protein. Ten micrograms of GST-FasLs (lines 1 and 3) or GST (lines 2 and 4) was resolved by electrophoresis in a 12% gradient polyacrylamide gel (E). Proteins were analyzed by Western blotting using the anti-FasL–COOH Ab (lines 1 and 2) or the anti-FasL MoAb (clone MTL4, lines 3 and 4) as described in Materials and Methods.

Expression of exogenous FasLs in transfected 3DO cells. The FasLs transfection was controlled by RT-PCR using as primer forward the T7 eukaryotic and as primer reverse the n. 3 shown in Fig 2A or using as primer forward the T7 eukaryotic and as primer reverse the SP6 eukaryotic. Each RT-PCR reaction (+) was controlled by using the respective RNA without the addition of reverse transcriptase (−) (B). The FasLs transfection was also controlled by immunoprecipitation with anti-FasL–COOH Ab of cell lysates (C) and supernatants (D). Western blotting of the GST-FasLs fusion protein. Ten micrograms of GST-FasLs (lines 1 and 3) or GST (lines 2 and 4) was resolved by electrophoresis in a 12% gradient polyacrylamide gel (E). Proteins were analyzed by Western blotting using the anti-FasL–COOH Ab (lines 1 and 2) or the anti-FasL MoAb (clone MTL4, lines 3 and 4) as described in Materials and Methods.

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