Protein Phosphatase 2A (PP2A) is a ubiquitous and conserved Serine/Threonine phosphatase and accounts for a large fraction of phosphatase activity in eukaryotic cells. PP2A plays an important role in cell cycle regulation, cell growth control, development, regulation of various signal transduction pathways, and cell mobility.
PP2A comprises A and B subunits which are regulatory and a catalytic C subunit. When the PP2A catalytic C subunit (36 kDa) associates with the regulatory A (65 kDa, PR65) and B subunits (PR55, PR56, PR72, PR93 etc), wide variety of heterotrimeric holoenzymes are produced with distinct functions and characteristics. The different association of the subunits give PP2A large regulatory flexibility and differential substrate specificity. The A subunit exists as two isoforms ( α and β ) as does the C subunit, whereas the B subunits fall into three families designated B, B' (also called B56), and B''. The A subunit is the scaffold required for the formation of the heterotrimeric complex and the binding of A subunit alters the enzymatic activity of the catalytic subunit, even if the B subunit is absent.

Western Blot: 0.2 ?g/ml; Immunoprecipitation: 2.0 ?g;

Type: Primary
Antigen: PPP2R1A/B (protein phosphatase 2, regulatory subunit A, alpha/beta)
Clonality: Monoclonal
Clone: 20G6
Conjugation: Unconjugated
Epitope:
Host: Mouse
Isotype: IgG2b Kappa
Reactivity: Human, Mouse, Rat