| Full Name | protein kinase, cAMP-dependent, regulatory, type II, alpha |
| 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). [provided by RefSeq, Jul 2008] |
| Synonyms | PKR2 Antibody , PRKAR2A Antibody , PRKAR2 Antibody , protein kinase, cAMP-dependent, regulatory, type II, alpha Antibody |
| Specificity | The antibody only detects PKA R2 phosphorylated on Serine 99. Phosphoserine 99 in Human corresponds to phosphoserine 96 in mouse. |
| Host | Rabbit |
| Clonality | Monoclonal |
| Clone Name | E151 |
| Isotype | IgG |
| Immunogen | A synthetic phospho-peptide corresponding to residues surrounding Ser99 of human PKA R2 |
| Antigen Species | Human |
| Species Reactivity | Human, Mouse, Pig, Rat |
| Conjugation | Unconjugated |