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. It may interact with various A-kinase anchoring proteins and determine the subcellular localization of cAMP-dependent protein kinase. This subunit has been shown to regulate protein transport from endosomes to the Golgi apparatus and further to the endoplasmic reticulum (ER).

Specificity:

protein kinase cAMP-dependent type II regulatory subunit alpha

Alternative names:

PKR2; PRKAR2

Species reactivity:

Human, Mouse, Rat

Host:

Mouse

Ig type:

PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Immunogen:

Full length human recombinant protein of human PRKAR2A (NP_004148) produced in HEK293T cell.

Purification & Purity:

Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)

Molecular weight:

45.3 kDa(Predicted)

Applications:

IF, IHC, WB

Usage:

WB 1:2000, IHC 1:50, IF 1:100

Storage:

PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Precautions:

For research use only, not for use in diagnostic procedure.

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