Go Back cAMP-dependent protein kinase, catalytic subunit (PKA, Calpha) mouse

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) regulating several 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 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. The ?-isoform is the predominant form with a broad tissue distribution and can be used for in vitro enzymological studies of neural and hormonal signal transduction or to phosphorylate target proteins in vivo (via microinjection) including ion channels, transcriptional activator proteins and regulatory enzymes of glycogen metabolism. Highly active PKA catalytic subunit recombinantly expressed in E. coli and purified using several chromatographic steps. Preferred peptide substrate is kemptide (LRRASLG).