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. Different isoforms of catalytic and regulatory subunits suggest specific functions.
The recombinant RIIa dimeric protein (about 90 kDa) specifically inhibits PKA catalytic subunit (Ki about 0.7nM) and is suitable for the analysis of interactions with so-called A-kinase anchoring proteins (AKAPs). Subcellular localisation is regulated via interaction of PKA RII with AKAPs. Protein is available in a cAMP-free form, will be supplied in 50% glycerol and shipped on dry ice.
cAMP-free regulatory subunit, inhibits catalytic subunit PKA C-alpha
purity >95% (SDS-PAGE)
Size: 25 µg
Ordering information: shipped on dry ice
Product specific literature references:
Otten AD, Parenteau LA, Doskeland S, McKnight GS (1991) "Hormonal activation of gene transcription in ras-transformed NIH3T3 cells overexpressing RII alpha and RII beta subunits of the cAMP-dependent protein kinase" J. Biol. Chem. 266(34):23074-82
Carr DW, Stofko-Hahn RE, Scott JD et al. (1991) "Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif" J. Biol. Chem. 266 (22): 14188-92
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