Anti-PTEN (human), Rabbit Monoclonal (RM511)

PTEN (phosphatase and tensin homologue deleted on chromosome ten) is a tumor suppressor implicated in a wide variety of human cancers. PTEN encodes a 403 amino acid polypeptide and contains a tensin like domain as well as a catalytic domain similar to that of the dual specificity protein tyrosine phosphatases. PTEN preferentially dephosphorylates phosphoinositide substrates. PTEN negatively regulates intracellular levels of phosphatidylinositol-3, 4, 5-trisphosphate in cells and functions as a tumor suppressor by negatively regulating PI3K/Akt signaling pathway. PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity. PTEN regulates p53 protein levels and activity and is involved in G protein-coupled signaling during chemotaxis. PTEN plays a role as a key modulator in neurogenesis, including correct neuron positioning, dendritic development and synapse formation and it may be also a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form of PTEN induces less tumor suppressive ability.