Prkar2a (human) recombinant (partia l protein gst tag) 25 µg

cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunitéss. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunitéss bound to four cAMP and two free monomeric catalytic subunitéss. Four different regulatory subunitéss and three catalytic subunitéss have been identified in humans. The protein encoded by this gene is one of the regulatory subunitéss. This subunités can be phosphorylated by the activated catalytic subunités. It may interact with various A-kinase anchoring proteins and determine the subcellular localization of cAMP-dependent protein kinase. This subunités has been shown to regulate protein transport from endosomes to the Golgi apparatus and further to the endoplasmic reticulum (ER). [provided by RefSeq]