PKA IIβ reg rabbit pAb

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

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

5577

P31323

Cytoplasm. Cell membrane. Colocalizes with PJA2 in the cytoplasm and at the cell membrane.

Rabbit

Human, Mouse, Rat

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

Polyclonal

WB, IHC, IF, ELISA

1 year

1 mg/mL

Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/100 - 1/300. ELISA: 1/10000. Not yet tested in other applications.

46kD

PBS with 0.02% sodium azide and 50% glycerol pH 7.4. Store at -20°C. Avoid repeated freeze-thaw cycles.