|Calculated MW||65.0 kDa|
|Other Names||PKA, cAMP-dependent protein kinase catalytic subunit alpha|
|Source||Baculovirus (Sf9 insect cells)|
|Storage||-80°C; Recombinant proteins in storage buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 0.25 mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, 25% glycerol).|
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Provided below are standard protocols that you may find useful for product applications.
Most of the effects of cAMP are mediated through the phosphorylation of target proteins on serine or threonine residues by the cAMP-dependent protein kinase (PKA). The inactive holoenzyme of AMPK is a tetramer composed of two regulatory and two catalytic subunits. The mammalian catalytic subunit has been shown to consist of three PKA gene products: C-α, C-β, and C-γ. Two PKA isoforms exist, designated types I and II, which differ in their dimeric regulatory subunits, designated RI and RII, respectively. Furthermore, there are at least four different regulatory subunits: RI-α, RI-β, RII-α, and RII-β. The cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. The catalytic subunit C-β of PKA (PKAcb) is a member of the Ser/Thr protein kinase family and is a catalytic subunit C-β of AMPK. Berube et al. assigned the PKAcb to human chromosome 1 by Southern blot analysis of somatic cell hybrids (1) and Simard et al located it to 1p36.1 by in situ hybridization (2).
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