Akt (pS473) Mouse, V450, Clone: M89-61, BD

Description

• Akt [also known as PKB (Protein kinase B) or RAC-PK (Related to the A and C kinases)] is a family of serine/threonine kinases that contains a pleckstrin homology (PH) domain
• PH domains play important roles in signal transduction
• There are three known isoforms of Akt in mammalian cells [Akt1 (α), Akt2 (β) and Akt3 (γ)]; they are thought to be regulated similarly
• Akt is activated by insulin and growth factors by a mechanism involving phosphoinositide 3-OH kinase
• Phosphoinositide 3-OH kinases products bind to the PH domain, resulting in translocation of Akt to the plasma membrane and activation of Akt to phospho-Akt by upstream kinases
• Akt is phosphorylated within the activation loop at threonine 308 and the C-terminus at serine 473 (S473)
• Phospho-Akt promotes cell survival by inhibiting apoptosis
• Specifically, phospho-Akt1 has been shown to phosphorylate Bad, a member of the Bcl-2 family that promotes cell death
• This phosphorylation results in the inactivation of the proapoptotic function of Bad
• The Akt molecule is thus considered to link extracellular survival signals (growth factors) with the apoptotic machinery (BAD)
• Akt is also a key mediator of the metabolic effects of insulin
• Additionally, Akt has been referred to as an oncogene because it has increased activity in a number of tumors
• The M89-61 antibody recognizes Akt phosphorylated at S473
• This phosphorylation site is shared by all three isoforms of Akt
• The homologous phosphorylation sites in Akt2 and Akt3 are S474 and S472, respectively.