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cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase (AMPK), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of AMPK is a tetramer composed of two regulatory and 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. Four different regulatory subunits and three catalytic subunits of AMPK have been identified in humans. PRKACB is a member of the Ser/Thr protein kinase family and is a catalytic subunit of AMPK.
cAMP-dependent protein kinase C beta; cAMP-dependent protein kinase catalytic beta subunit isoform 4ab; cAMP-dependent protein kinase catalytic subunit alpha; cAMP-dependent protein kinase catalytic subunit alpha, isoform 1; cAMP-dependent protein kinase catalytic subunit beta; cAMP-dependent protein kinase catalytic subunit C alpha; Cs-PKA; PKA C-alpha; PKA C-beta; Pkaca; Pkacb; PKCA1; PKCD; PPNAD4; Prkaca; Prkacb; protein kinase A; protein kinase A catalytic subunit; protein kinase A catalytic subunit beta; protein kinase cAMP-activated catalytic subunit alpha; protein kinase cAMP-activated catalytic subunit beta; protein kinase, cAMP dependent, catalytic, alpha; protein kinase, cAMP dependent, catalytic, beta; protein kinase, cAMP-dependent, alpha catalytic subunit; protein kinase, cAMP-dependent, beta catalytic subunit; protein kinase, cAMP-dependent, catalytic, alpha; protein kinase, cAMP-dependent, catalytic, beta; sperm cAMP-dependent protein kinase catalytic subunit
100 µg
100 µL
100 µL
100 µL
100 µg
100 µL
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