The Phospho-PKA alpha/beta/gamma (Thr197) antibody detects endogenous protein kinase A (PKA) catalytic subunits (α, β, or γ) when phosphorylated at threonine 197. a critical post-translational modification for PKA activation. PKA is a serine/threonine kinase central to cAMP-dependent signaling, regulating processes like metabolism, gene expression, and cell proliferation. It consists of two regulatory subunits that inhibit catalytic subunits under low cAMP levels. Upon cAMP elevation, regulatory subunits dissociate, releasing active catalytic subunits.
Thr197 phosphorylation occurs in the catalytic subunit's activation loop, stabilizing the active conformation by facilitating proper alignment of the kinase domain. This autophosphorylation (or mediated by upstream kinases) is essential for full enzymatic activity. The antibody specifically recognizes this phosphorylation event across PKA α (PRKACA), β (PRKACB), and γ (PRKACG) isoforms, enabling researchers to study PKA activation dynamics in diverse tissues.
Applications include Western blotting, immunohistochemistry, and immunofluorescence to assess PKA activity in physiological or pathological contexts, such as metabolic disorders, cardiovascular diseases, or cancer. Its specificity makes it valuable for investigating cAMP-PKA signaling aberrations linked to endocrine tumors, neurodegenerative conditions, or drug responses. Proper controls (e.g., phosphatase-treated samples) are recommended to confirm phosphorylation-dependent signals.