Human PTEN Alexa Fluor™ Plus 405‑conjugated Antibody

The tumor suppressor gene PTEN (phosphatase and tensin homolog deleted on chromosome 10), also known as MMAC1 (mutated in multiple advanced cancers 1), encodes a phosphatase that contains the catalytic signature motif (HCXXGXXRS/T) found in all members of the protein tyrosine phosphatase family. In vitro, the recombinant PTEN has both lipid phosphatase and protein phosphatase activities (1, 2). Interestingly, accumulating evidence has shown that the tumor suppressor activity of PTEN relies on its ability to dephosphorylate phosphatidylinositol (3, 4, 5)-triphosphate specifically at position 3 of the inositol ring (3). This activity reduces the levels of phosphatidylinositol (3, 4, 5)-triphosphate which is specifically produced from phosphatidylinositol (4, 5)-diphosphate by PI 3-kinase upon activation by a variety of stimuli. Therefore, PTEN antagonizes PI 3-kinase-induced downstream signaling events and cellular processes including cell growth, apoptosis and cell motility. In vivo, the importance of PTEN catalytic activity in its tumor suppressor functions is underscored by the fact that the majority of PTEN missense mutations detected in tumor specimens target the phosphatase domain and cause a loss in PTEN phosphatase activity (4).