PKA C-α Recombinant Rabbit mAb (S-2564-5)

PKA C-α protein, fully known as cAMP-dependent protein kinase A catalytic subunit alpha, is a crucial signal transduction molecule within cells, often regarded as one of the fundamental "molecular switches" of life. As the core catalytic component of the PKA holoenzyme, it exists in an inactive state bound to regulatory subunits. When the levels of the second messenger cAMP rise, cAMP binds to the regulatory subunits, causing their dissociation from the catalytic subunit and thereby activating PKA C-α. Once activated, PKA C-α exerts its function by transferring a phosphate group from ATP to specific serine or threonine residues on its target substrate proteins, a process known as reversible phosphorylation. This mechanism precisely regulates a vast array of core physiological functions, including glycogen metabolism, lipid synthesis, gene transcription, cell proliferation and differentiation, learning and memory, and heart rhythm. Dysregulation of its activity or expression is closely associated with various human diseases, such as cancer, heart disease, metabolic disorders, and brain dysfunction.