Protein Kinase Akt1, also known as Protein Kinase B alpha (PKBα), is a serine/threonine kinase that plays a crucial role in various cellular processes. This enzyme is encoded by the AKT1 gene in humans and is part of the Akt family of kinases, which are involved in cell signaling pathways that regulate cell survival, growth, proliferation, and metabolism .
Akt1 is a 59.9 kDa protein that contains an N-terminal pleckstrin homology (PH) domain, a central kinase domain, and a C-terminal regulatory domain . The PH domain allows Akt1 to bind to phosphatidylinositol (3,4,5)-trisphosphate (PIP3) at the plasma membrane, which is crucial for its activation. Upon binding to PIP3, Akt1 undergoes a conformational change that allows it to be phosphorylated at two key residues: threonine 308 (Thr308) in the kinase domain and serine 473 (Ser473) in the regulatory domain .
Akt1 is activated in response to various extracellular signals, including growth factors, hormones, and cytokines. Once activated, Akt1 phosphorylates a wide range of substrates involved in diverse cellular processes:
Recombinant human Akt1 is produced using baculovirus expression systems in insect cells (Sf21). The recombinant protein is typically tagged with a His6 tag at the N-terminus to facilitate purification and detection . This active form of Akt1 is used in various biochemical assays, including kinase assays and immunoprecipitation-kinase (IP-kinase) assays, to study its activity and interactions with other proteins .
Recombinant Akt1 is widely used in research to investigate its role in cellular signaling pathways and its implications in diseases such as cancer, diabetes, and cardiovascular diseases. By studying the activity and regulation of Akt1, researchers aim to develop targeted therapies that can modulate its function for therapeutic benefit .