PKA (RIIβ) (pS114) Mouse anti-Human, Alexa Fluor 647, Clone: 47, BD

cAMP-dependent Protein Kinase (PKA) is composed of two distinct subunits: catalytic (C) and regulatory (R). Four regulatory subunits have been identified: RIα, RIβ, RIIα, and RIIβ. These subunits define type I and II PKAs. Following binding of cAMP, the regulatory subunits dissociate from the catalytic subunits, rendering the enzyme active. Type I and type II holoenzymes have three potential C subunits (Cα, Cβ, or Cγ). Most cells, including T lymphocytes, express both type I and type II PKAs. RIIa expression is associated with cellular transformation, while RIIβ expression correlates with mitotic arrest and cellular differentiation. Type II PKA can be distinguished by autophosphorylation of the R subunits, while type I PKA binds Mg/ATP with high affinity. The cAMP-dependent autophosphorylation of the human RIIβ subunits occurs at serine 114 (S114). In addition to their enzyme regulatory activity, the RIIα and RIIβ subunits determine the subcellular location of the holoenzymes via their interactions with specific intracellular anchoring proteins. The 47/PKA monoclonal antibody recognizes the phosphorylated S114 in the RIIβ subunit of PKA. The orthologous phosphorylation site in mouse and rat PKA(RIIβ) is S112.

Host Species: Mouse
Clone: 47
Isotype: IgG1 κ
Species Reactivity: Human
Immunogen: Phosphorylated Human PKA(RIIβ) Peptide

Intracellular Staining