mTOR exists as two types of complexes called mTORC1 and mTORC2. mTORC1 is regulated in activity by amino acid and inhibited specifically by a immunosuppressant “rapamycin”. It is considered that PRAS40 is phosphorylated by mTORC1, for phosphorylation of PRAS40 (proline-rich Akt substrate of 40 kDa) which is a novel substrate of mTOR at Ser-183 (human) is induced by amino-acid stimulation and inhibited by rapamycin. It is known that mTORC1 is inhibited by AMP kinase system and then phosphorylation of PRAS40 at Ser-183 is inhibited by 2-Deoxyglucose (2DG) treatment inducing activation of AMP-kinase. It is shown that PRAS40 is dissociated from raptor which is a component of mTORC1 when it is phosphorylated by mTORC1, and it is assumed that phosphorylation of PRAS40 at Ser-183 is involved in controlling mTOR signal-transducing pathway. This antibody recognizes the phosphorylation of PRAS40 at Ser-183 (human). For research use only, not for use in diagnostic procedures.
