PP2A catalytic subunit pTyr307, Santa Cruz Biotechnology, sc-12615

Our team performed a comprehensive review of the scientific literature to identify studies using antibodies against human Protein Phosphatase 2A (PP2A), followed by extraction and evaluation of available data according to the pAbmAbs rating criteria. In this study, Frohner et al. conducted a head-to-head comparison of eight commercially available antibodies against PP2A catalytic subunit phosphorylated at Tyr307 (PP2AC pTyr307). Antibody performance was evaluated by WB and ELISA, with particular emphasis on specificity for Tyr307 phosphorylation versus other post-translational modifications, including Leu309 methylation. For WB experiments, antibodies were tested using lysates from stably HA-PP2AC-expressing NIH 3T3 cells, transiently transfected HEK293T cells, HAP1 cells, and primary mouse CD4+ T cells under multiple experimental conditions, including phosphatase treatment, modulation of PP2A methylation, kinase activation, and site-directed mutagenesis. Peptide ELISA was performed using synthetic PP2A C-terminal peptides carrying defined combinations of post-translational modifications. Detailed experimental procedures are provided in the original publication (see reference). This antibody, sc-12615 from Santa Cruz Biotechnology, detects phosphorylated PP2AC over unmodified PP2AC in peptide ELISA. However, the signal is not specific for pTyr307, as an equally strong signal is observed for an HA-derived pTyr9 control peptide. Recognition of pTyr307 is unaffected by the methylation state of neighboring Leu309. The antibody showed no or poor detection of PP2AC in WB, regardless of Tyr307 phosphorylation. This antibody has been discontinued by the manufacturer.