Go Back cAMP-dependent protein kinase regulatory subunit II beta (PKA, RII beta), human

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cAMP-dependent protein kinase (PKA) is an ubiquitous serine/theonine protein kinase present in a variety of tissues. The intracellular cAMP level regulates cellular responses by altering the interaction between the catatytic C and regulatory R subunits of PKA. The inactive PKA holoenzyme is activated when cAMP binds to the regulatory subunits which induces the release of two active catalytic subunits. Cyclic AMP-dependent protein kinase type II beta is the predominant PKA isoform and principal mediator of cAMP action in the central nervous system. The majority of PKA type II is targeted to specific sites in the cytoskeleton or organelles of neurons via high-affinity binding to so called A Kinase Anchoring Proteins (AKAPs). AKAPs place PKA type II in proximity with neurotransmitter-activated adenylate cyclase, neurotransmitter receptors for desensitization, ion channels and substrates in the cytoskeleton such as microtubule-associated proteins. The recombinant RII beta regulatory subunit supplied by Biaffin is a 90 kDa dimeric protein (monomer 45 kD) suitable for inhibition studies and analysis of AKAP interactions.