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44-992G has been used successfully in the ChIP analysis of PKA beta pS338.
The catalytic subunit C-beta of PKA (PRKACB) is a member of the Ser/Thr protein kinase family (the PKA catalytic subunit consist of three gene products: C-alpha, C-beta, and C-gamma) and has been assigned to human chromosome region 1p36.1. PRKACB is derived from a gene distinct from C-alpha and shows tissue-specific expression. At the amino acid level C-alpha and C-beta showed 93% homology. 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.
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Protein Aliases: cAMP-dependent protein kinase C beta; cAMP-dependent protein kinase catalytic beta subunit isoform 4ab; cAMP-dependent protein kinase catalytic subunit beta; PKA C-beta; protein kinase A catalytic subunit beta; protein kinase, cAMP-dependent, beta catalytic subunit; protein kinase, cAMP-dependent, catalytic, beta
Gene Aliases: PKA C-beta; PKACB; PRKACB
Molecular Function: non-receptor serine/threonine protein kinase