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. 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

Classification:

Primary antibody

Alternative names:

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

Species reactivity:

Human, Mouse, Rat, Monkey

Host:

Rabbit

Isotype:

IgG

Immunogen:

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

Concentration:

1 mg/ml

Molecular weight:

46346

Applications:

WB, IHC-p, IF, ELISA

Storage:

-20°C for 1 year

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