Anti-PRKAR2A antibody produced in rabbit

rabbit

100

affinity isolated antibody

primary antibodies

polyclonal

buffered aqueous solution

43
45

mouse, rat, human

3.29 mg/ml

western blot: 1:1000-1:2000

P13861

wet ice

−20℃

human ... PRKAR2A(5576)

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).

Recombinant fusion protein containing a sequence corresponding to amino acids 1-404 of human PRKAR2A (NP_004148.1).

PBS with 0.02% sodium azide,50% glycerol,pH7.3.

Store at -20℃. Avoid freeze / thaw cycles.

12 - Non Combustible Liquids

WGK 1