PKA RIIα (pS99) Mouse anti-Human, Alexa Fluor 647, Clone: I65-856.286, 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, 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 II holoenzymes have three potential C subunits (Cα, Cβ, or Cγ)
• 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 RIIα subunit occurs at Serine 99 (S99) (Entrez Protein Accession No.CAA33094)
• Most cells express both type I and type II PKAs
• Although the Rα isoforms are ubiquitously expressed, the Rβ isoforms are predominantly found in nervous and adipose tissues
• 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 I65-856.286 antibody recognizes human PKA RIIα phosphorylated at S99
• Host Species: Mouse Clone: I65-856.286 Isotype: IgG1 κ Species Reactivity: Human Immunogen: Phosphorylated Human PKA RIIα Peptide Intracellular Staining