**Background of Phospho-PKAC(Thr197) Antibody**
The Phospho-PKAC(Thr197) antibody is a specialized tool used to detect the activated form of the catalytic subunit of protein kinase A (PKA), a critical enzyme in cAMP-mediated signaling. PKA consists of two regulatory (R) and two catalytic (C) subunits. Upon cAMP binding, the R subunits dissociate, releasing active C subunits (PKAC) to phosphorylate downstream targets.
Threonine 197 (Thr197) in PKAC is located within the activation loop, a region essential for enzymatic activity. Autophosphorylation at Thr197 is required for full PKA activation, stabilizing the active conformation and enhancing substrate binding. This post-translational modification serves as a biomarker for PKA activation in cellular responses to hormones, neurotransmitters, and stress signals.
The Phospho-PKAC(Thr197) antibody specifically recognizes PKAC when phosphorylated at Thr197. enabling researchers to study PKA activation dynamics in various contexts, including metabolic regulation, cell proliferation, and apoptosis. It is widely used in techniques like Western blotting, immunofluorescence, and immunohistochemistry to assess PKA activity in diseases such as cancer, cardiovascular disorders, and neurodegenerative conditions.
By targeting this phosphorylation event, the antibody provides insights into cAMP/PKA pathway dysregulation and aids in evaluating therapeutic interventions targeting PKA signaling. Its specificity and reliability make it a valuable tool in both basic research and clinical studies.