Recombinant Human PRKACB/PKC beta GST Active

Biomolecules

Recombinant full-length human PKA cb containing N-terminal GST tag was expressed by baculovirus in Sf 9 insect cells. 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-alpha, Cbeta, and C-gamma. 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-alpha, RI-beta, RII-alpha, and RII-beta. 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-beta of PKA (PKAcb) is a member of the Ser/Thr protein kinase family and is a catalytic subunit C-beta of AMPK. PKAcb was assigned, to human chromosome 1 by Southern blot analysis of somatic cell hybrids and located it to 1p36.1 by in situ hybridization.

342 nmol/min/mg: 342 umol phosphate incorporated into CREBtide substrate per minute per mg protein at 30C for 15 minutes using a final concentration of 50 uM ATP (0.83 uCi/assay). See QA/QC section for details.