Background:

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. Protein kinase cAMP-dependent type II regulatory subunit beta encoded by PRKAR2B 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 activated T cells. Knockout studies in mice suggest that this subunit may play an important role in regulating energy balance and adiposity. The studies also suggest that this subunit may mediate the gene induction and cataleptic behavior induced by haloperidol.

Classification:

Primary antibody

Alternative names:

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

Species reactivity:

Human;Mouse;Rat

Host:

Rabbit

Isotype:

IgG

Immunogen:

The antiserum was produced against synthesized peptide derived from human PKA-R2 beta. AA range:79-128

Concentration:

1 mg/ml

Molecular weight:

46346

Applications:

WB, IHC-p, ELISA

Storage:

-20°C for one year

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