Mammalian target of rapamycin (mTOR), a serine/threonine kinase involved in diverse cellular processes, including protein translation, mRNA turnover, and protein stability, mediates, at least in part, some of the biological actions of Akt. As a Kinase subunit of both mTORC1(complex1) and mTORC2(complex2), mTOR regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation.

Western Blot: 1:2,000;

Type: Primary
Antigen: MTOR (mechanistic target of rapamycin (serine/threonine kinase))
Clonality: Monoclonal
Clone: 5300000000000
Conjugation: Unconjugated
Epitope:
Host: Mouse
Isotype: IgG1 Kappa
Reactivity: Human