This antibody got two bands about 45 kDa and 50-55 kDa in western blotting, and the 50-55 kDa may be caused by phosphorylation.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. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. It may interact with various A-kinase anchoring proteins and determine the subcellular localization of AMPK.
|Immunocytochemistry, Immunofluorescence, Immunoprecipitation, Western Blot|
|PBS with 50% glycerol and 0.1% sodium azide; pH 7.3|
|Human, Mouse, Rat|
|Antigen Affinity Chromatography|
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