Go Back cAMP-dependent protein kinase, holo enzyme complex, type II alpha (PKA C2RIIA2)

Product Detail

cAMP-dependent protein kinase (PKA) is an ubiquitous serine/theonine protein kinase present in a variety of tissues (e.g. brain, skeletal muscle, heart). The intracellular cAMP level regulates cellular responses by altering the interaction between the catatytic C and regulatory R subunits of PKA. The inactive tetrameric PKA holoenzyme R2C2 is activated when cAMP binds to R2, which dissociates the tetramer to R2*cAMP4 and two active catalytic subunits. Free catalytic subunits of PKA can phosphorylate a wide variety of intracellular target proteins. In response to hormone-induced high cAMP levels, PKA phosphorylates glycogen synthetase (inhibition of the enzyme activity) and phosphorylase kinase to block glycogen synthesis. Inactive holoenzyme consisting of one dimeric regulatory subunit type IIalpha (monomer 45 kD) and two monomeric catalytic subunits(cAMP-free, monomer of 41 kD). Holo enzymecan be activated by adding the second messenger cAMP (activation constant about 100 nM) releasing two monomeric catalytic subunits. The product is suitable for analysing PKA type II agonists (cAMP analogs) or antagonists.