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 PRKAR2A（protein kinase cAMP-dependent type II regulatory subunit alpha) 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).
PKA IIα reg Polyclonal Antibody detects endogenous levels of PKA IIα reg protein.
Optimal working dilutions should be determined experimentally by the investigator. Suggested starting dilutions are as follows: WB: 1:500-1:2000, IHC-p: 1:100-1:300, IF: 1:200-1:1000, ELISA: 1:10000. Not yet tested in other applications.
PKA IIα reg Polyclonal Antibody product listed herein is for research use only and is not intended for use in human or clinical diagnosis. Suggested applications of our products are not recommendations to use our products in violation of any patent or as a license. We cannot be responsible for patent infringements or other violations that may occur with the use of this product.
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