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Equal amounts of total proteins were loaded, separated by SDS-PAGE, and processed for immunoblotting with custom-made AvrA antibody.

ARC-purified hmCD40 and hmCD40Δ67 samples were fractionated by SDS-PAGE and processed for liquid chromatography/tandem mass spectrometry (Fig. 1).

Cell pellets were lysed in a nuclear and cytoplasmic extraction reagent (Thermo scientific), proteins separated by SDS-PAGE and processed for western blotting.

For the proteomic profiling step, the purified platelet membrane fraction was pre-fractionated using 1D SDS-PAGE and processed according to the workflow shown in Figure 1A.

Protein extracts were prepared from cells, and 20 µg of each was used for separation by 4 12% SDS-PAGE and processed for Western blot analyses as described previously [39].

The samples were then loaded onto SDS-PAGE and processed as described above for western blotting.

Fractions were then resolved using SDS-PAGE and processed for quantitative immunoblot.

For palmitome analysis after 2-BMP or DMSO treatment, samples were separated by SDS-PAGE and processed as above.

Twenty to 40 μg of WCE or nuclear and cytoplasmic fractions were subjected to SDS-PAGE and processed by immuno-blot.

Protein extracts were separated by SDS-PAGE and processed for trypsin digestion and LC-MS/MS analyses as previously described (Adam et al., 2011).