PKARIIb (pS114) Mouse, Unlabeled, Clone: 47, BD

Description

• 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 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
• Flow Cytometry, Intracellular Staining, Western Blotting