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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.
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.