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
Store at -80ºC. Product is stable for at least 6-12 months.
0.1mg/ml(Please refer to the vial label for the specific concentration.)
Baculovirus (Sf9 insect cells)
Purity was assessed by SDS-PAGE (≥90%) and by HPLC.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
PKA, cAMPdependent protein kinase catalytic subunit alpha, cAMP-dependent protein kinase catalytic subunit alpha, PRKACB
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-alpha , C-beta, 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. 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).