PKAca, Active recombinant protein

Provided below are standard protocols that you may find useful for product applications.

Background

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 (AMPK). 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. 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-α of PKA (PKAca) is a member of the Ser/Thr protein kinase family and is a catalytic subunit C-β of AMPK. Tasken et al. assigned the PKAca gene to 19p13.1 (1). Yasuda et al found that protein kinase A is required for long-term potentiation in neonatal tissue and suggested that developmental changes in synapse morphology may underlie the changes in the kinase activity (2). Skalhegg et al generated a null mutation in the major catalytic subunit of PKAca, and observed early postnatal lethality in the majority of C-α knockout mice. Surprisingly, a small percentage of C-α knockout mice, although runted, survived to adulthood. In these animals, compensatory increases in C-β levels occurred in brain whereas many tissues, including skeletal muscle, heart, and sperm, contained less than 10% of the normal PKA activity (3).