This antibody is specific to PRKACB.
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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