Phospho-PKA R2 Antibody / PRKAR2A (pS99)

Western blot: 1:500-1:2000

Optimal dilution of the phospho-PKA R2 antibody (pS99) should be determined by the researcher.

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 the PRKAR2A 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). [RefSeq]

Purified

Antibody in PBS with 0.02% sodium azide and 50% glycerol

A synthetic peptide specific to human PKA R2 / PRKAR2A (surrounding pS99) was used as the immunogen for the phospho-PKA R2 antibody.

This phospho-PKA R2 antibody (pS99) is available for research use only.

Affinity purified

Human

P13861