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2. TRPC1, TRPC4 and TRPC5 co-immunoprecipitate from Sf9 cell lysates. Sf9 cells were co-infected with recombinant baculovirus for expression of individual TRPC channel pairs; (upper panels) TRPC1 and TRPC4; (middle panels) TRPC4 and TRPC5; (bottom panels) TRPC1 and TRPC5. Each panel shows a Western blot using the indicated anti-TRPC antibody; lane 1, proteins from total cell lysates; lane 2, proteins immunoprecipitated with the indicated antiTRPC channel antibody. ) TRPC SUBUNIT ASSEMBLY 23 FIG.

Proteins from synaptosomal preparations isolated from rat cortex were immunoprecipitated and subjected to Western blot analysis. Each panel shows a Western blot using the indicated anti-TRPC antibody; lane 1, proteins from total synaptosomal lysates; lane 2, proteins immunoprecipitated with the indicated anti-TRPC channel antibody. ) TRPC7 co-associate, but no cross-association between the two major TRPC channel subgroups is observed at least when heterologously expressed. To determine if the TRPC channel subunit speci¢city observed in heterologous expressing systems applies to channels in vivo, similar immunoprecipitation experiments were performed from rat brain lysates.

Schilling: I don’t know the answer to that, but it is possible that you can have FK506 binding to FKBP-52 without causing displacement from its target protein, because there are these multiple FK506 binding domains on FKBP-52. In fact, the ¢rst and second FK506 binding domains are highly conserved. It is possible that you could have three FK506 molecules bound to FKBP-52. These three FK506 binding domains on FKBP-52 may also independently interact with di¡erent proteins. Thus, one can envision FKBP-52 acting as a linker between the TRPC channel and a PDZ-containing protein.

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