Extracts of His-tagged S139A/T421A double mutant (1) and wild-type PAK3 (2-5) were resolved by SDS-PAGE on a 10% Tris-glycine gel and transferred to PVDF. The membrane was blocked with a 5% milk- TBST buffer for one hour at RT, then incubated with MBS620041 for two hours at RT in a 1% BSA-TBST buffer, following prior incubation with: no peptide (1, 2), the non-phosphopeptide corresponding to the phosphopeptide
immunogen (3), a generic phosphoserine-containing peptide (4), or the phosphopeptide immunogen (5). After washing, the membrane was incubated with Pab IgG F(ab’)2 (HRP) goat x rabbit and detected using SuperSignal ECL method. Only the phosphopeptide corresponding to MBS620041 blocks the antibody signal. Phosphorylation of the wild-type but not the mutant protein is detected by MBS620041
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