cAMP-dependent protein kinase type II-beta regulatory subunit

BT-AP13077

Rabbit

IgG

20ul,50ul,100ul

Polyclonal

The antiserum was produced against synthesized peptide derived from human PKA-R2 beta around the phosphorylation site of Ser113. AA range:79-128

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

1 mg/ml

Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

-20°C for 1 year

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 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 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. This subunit has been shown to interact with and suppress the transcriptional activity of the cAMP responsive element binding protein 1 (CREB1) in activ

Human: P31323; Mouse: P31324; Rat: P12369;

46346

Human: 5577; Mouse: 19088; Rat: 24679

cAMP-dependent protein kinase type II-beta regulatory subunit; PRKAR2B; cAMP-dependent protein kinase type II-beta regulatory subunit

Signal transduction

PRKAR2B