• NatureSynthetic
  • Amino Acid Sequence
    • SpeciesHuman

Associated products


Our Abpromise guarantee covers the use of ab99155 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Blocking - Blocking peptide for Anti-mTOR antibody (ab25880)

  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.

    Preservative: 0.02% Sodium Azide
    Constituents: 0.1% BSA, PBS, pH 7.2

General Info

  • Alternative names
    • dJ576K7.1 (FK506 binding protein 12 rapamycin associated protein 1)
    • FK506 binding protein 12 rapamycin associated protein 1
    • FK506 binding protein 12 rapamycin associated protein 2
    • FK506 binding protein 12 rapamycin complex associated protein 1
    • FK506-binding protein 12-rapamycin complex-associated protein 1
    • FKBP rapamycin associated protein
    • FKBP12 rapamycin complex associated protein
    • FKBP12-rapamycin complex-associated protein
    • FKBP12-rapamycin complex-associated protein 1
    • FLJ44809
    • FRAP
    • FRAP1
    • FRAP2
    • Mammalian target of rapamycin
    • Mechanistic target of rapamycin
    • mTOR
    • OTTHUMP00000001983
    • RAFT1
    • Rapamycin and FKBP12 target 1
    • Rapamycin associated protein FRAP2
    • Rapamycin target protein
    • Rapamycin target protein 1
    • RAPT1
    • Serine/threonine-protein kinase mTOR
    see all
  • FunctionKinase subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Growth factor-stimulated mTORC1 activation involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino-acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. 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). mTORC1 phosphorylates and activates S6K1 at 'Thr-421', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Phosphorylates MAF1 leading to attenuation of its RNA polymerase III-repressive function. mTORC2 is also activated by growth. factors, but seems to be nutrient-insensitive. 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, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'.
  • Tissue specificityExpressed in numerous tissues, with highest levels in testis.
  • Sequence similaritiesBelongs to the PI3/PI4-kinase family.
    Contains 1 FAT domain.
    Contains 1 FATC domain.
    Contains 7 HEAT repeats.
    Contains 1 PI3K/PI4K domain.
  • Post-translational
    Autophosphorylated; when part of mTORC1 or mTORC2.
  • Cellular localizationEndoplasmic reticulum membrane. Golgi apparatus membrane. Mitochondrion outer membrane. Lysosome. Cytoplasm. Nucleus > PML body. Shuttles between cytoplasm and nucleus. Accumulates in the nucleus in response to hypoxia (By similarity). Targeting to lysosomes depends on amino acid availability and RRAGA and RRAGB.
  • Information by UniProt

References for Human mTOR peptide (ab99155)

ab99155 has not yet been referenced specifically in any publications.

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