Anti-phospho-PKA C (Thr197) / PRKACA/PRKACB/PRKACG, clone 32P41

Rabbit IgG in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol, 0.4-0.5mg/ml BSA. Phospho-PKA C (Thr197) antibody detects Protein kinase A catalytic subunit phosphorylated at threonine 197, encoded by PRKACA, PRKACB, and PRKACG. Protein kinase A catalytic subunit is the enzymatic component of the cAMP-dependent protein kinase holoenzyme, which regulates metabolism, growth, and gene expression. Phosphorylation at threonine 197 is required for full activation of the catalytic subunit. Phospho-PKA C (Thr197) antibody provides researchers with a highly specific reagent to study activation of PKA signaling in multiple biological systems.Protein kinase A catalytic subunit is activated when cAMP binds regulatory subunits, releasing the catalytic subunits into the cytoplasm. Research using Phospho-PKA C (Thr197) antibody has demonstrated that phosphorylation at threonine 197 occurs within the activation loop and is necessary for stabilizing the active conformation. This phosphorylation is typically mediated by phosphoinositide-dependent kinase 1 and ensures robust catalytic activity toward downstream substrates. Without this modification, kinase activity is impaired, highlighting its essential role in PKA signaling.Studies with Phospho-PKA C (Thr197) antibody have revealed that phosphorylation of the catalytic subunit regulates diverse cellular processes. These include glycogen metabolism, lipolysis, ion channel regulation, and transcriptional activation. PKA phosphorylates transcription factors such as CREB, influencing gene expression programs in response to hormonal and metabolic signals. By monitoring phosphorylation at Thr197, researchers gain insight into dynamic activation of cAMP-dependent signaling.Dysregulation of PKA phosphorylation has been linked to disease. Research using Phospho-PKA C (Thr197) antibody has shown that abnormal activity contributes to endocrine disorders, cardiovascular disease, and cancer. Mutations in PRKACA are associated with adrenal hyperplasia and Cushing's syndrome, conditions characterized by excessive PKA signaling. In oncology, altered phosphorylation of PKA subunits affects cell proliferation and survival, supporting tumor growth. These findings emphasize the importance of Thr197 phosphorylation in physiology and pathology.Phospho-PKA C (Thr197) antibody is widely applied in western blotting, immunohistochemistry, and immunofluorescence. Western blotting distinguishes active phosphorylated subunits, immunohistochemistry highlights activated kinase in tissues, and immunofluorescence demonstrates localization of phosphorylated subunits in response to stimuli. These applications make Phospho-PKA C (Thr197) antibody an indispensable tool in signaling research.By supplying validated Phospho-PKA C (Thr197) antibody reagents, NSJ Bioreagents supports studies into kinase signaling, endocrine biology, and cancer. Detection of phosphorylation at threonine 197 in PRKACA, PRKACB, and PRKACG provides a precise marker of Protein kinase A catalytic activity.