PKA Catalytic β (human), (recombinant) (GST-tag)

PKA belongs to the cAMP-dependent protein kinase (PKA) family. PKA isoforms type I and II include respective dimeric R subunits RI and RII which each produce two subunits designated RI-α, RI-β, RII-α, and RII-β. The catalytic subunit also consists of more than one gene product. Researchers cloned mammalian catalytic subunit C-α, C-β, and C-γ cDNAs. The catalytic subunit C-β belongs to the Ser/Thr protein kinase family. Activated by cAMP, PKA C-β resides in the cytoplasm (inactive holoenzyme and monomeric catalytic subunit), and translocates into the nucleus (monomeric catalytic subunit). A number of inactive tetrameric holoenzymes result from the combination of homo- or heterodimers of the different regulatory subunits associated with the two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. PKA C-β acts as a p75 neurotrophin receptor (NTR)-interacting protein, which phosphorylates p75 (NTR) at Ser304.