Recombinant human mTOR + MLST8 + Raptor protein
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Recombinant human mTOR + MLST8 + Raptor protein is a Human Fragment protein, in the 1362 to 2549 aa range, expressed in Baculovirus infected Sf9 cells, with >50%, suitable for SDS-PAGE, FuncS.
View Alternative Names
FRAP, FRAP1, FRAP2, RAFT1, RAPT1, MTOR, Serine/threonine-protein kinase mTOR, FK506-binding protein 12-rapamycin complex-associated protein 1, FKBP12-rapamycin complex-associated protein, Mammalian target of rapamycin, Mechanistic target of rapamycin, Rapamycin and FKBP12 target 1, Rapamycin target protein 1, mTOR
- FuncS
Supplier Data
Functional Studies - Recombinant human mTOR + MLST8 + Raptor protein (AB196074)
Activity assay using ab196074.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human mTOR + MLST8 + Raptor protein (AB196074)
10% SDS-PAGE analysis of 3 μg ab196074 with Coomassie staining.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The mTORC1 complex regulates processes of cell growth proliferation and autophagy in response to nutrient signals. mTORC1 integrates inputs from upstream growth factors and amino acid levels to influence cell cycle progression and protein synthesis. The complex localizes to the lysosomal surface where it becomes activated. This activation allows mTORC1 to control anabolic pathways ensuring that cells can increase their mass and function optimally in response to environmental cues.
Pathways
MTORC1 interacts with the PI3K/AKT signaling pathway which is essential for controlling metabolism and cellular survival. This pathway involves proteins such as AKT and TSC2 which serve as regulators of mTORC1 activity. Additionally mTORC1 influences the AMPK pathway which balances energy expenditure with availability. Through these interactions mTORC1 serves as a pivotal node that integrates nutrient and energy signals to coordinate cell growth and division.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
The protein expressed by the MTOR gene is a serine/threonine protein kinase that serves as a central regulator of cellular metabolism, growth, and survival in response to various signals, such as hormones and nutrients. MTOR operates within two distinct signaling complexes, mTORC1 and mTORC2. mTORC1 is activated to upregulate protein synthesis by phosphorylating regulators of mRNA translation and ribosome synthesis, and phosphorylates and activates proteins like RPS6KB1 and RPS6KB2 to promote protein synthesis. It controls MiT/TFE factors TFEB and TFE3 by mediating their retention and inactivation under nutrient-rich conditions, and it inhibits autophagy by phosphorylating DAP and RUBCNL/Pacer. Additionally, mTORC1 engages in feedback control on growth factor signaling and may influence microtubules through CLIP1 phosphorylation. The mTORC2 complex may regulate cellular processes, including survival and cytoskeletal organization, by phosphorylating AKT1 and regulating the actin cytoskeleton via PRKCA, PXN, and Rho-type guanine nucleotide exchange factors. It also regulates the phosphorylation of SGK1. This supplementary information is collated from multiple sources and compiled automatically.
Sequence similarities
Belongs to the PI3/PI4-kinase family.
Post-translational modifications
Autophosphorylates when part of mTORC1 or mTORC2 (PubMed:15467718, PubMed:9434772). Phosphorylation at Ser-1261, Ser-2159 and Thr-2164 promotes autophosphorylation (PubMed:19487463). Phosphorylation in the kinase domain modulates the interactions of MTOR with RPTOR and AKT1S1/PRAS40 and leads to increased intrinsic mTORC1 kinase activity (PubMed:15905173, PubMed:19145465, PubMed:21576368). Phosphorylation at Ser-2159 by TBK1 in response to growth factors and pathogen recognition receptors promotes mTORC1 activity (PubMed:29150432). Phosphorylation at Thr-2173 in the ATP-binding region by AKT1 strongly reduces kinase activity (PubMed:24247430).
Subcellular localisation
Mitochondrion outer membrane
Target data
Additional targets
Product promise
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