Anti-mTOR antibody (ab59350)
- Product nameAnti-mTOR antibodySee all mTOR primary antibodies ...
- DescriptionRabbit polyclonal to mTOR
- Specificityab59350 detects endogenous levels of total mTOR protein
- Tested applicationsIHC-P, ELISA more details
- Species reactivityReacts with: Human
Predicted to work with: Mouse, Rat
Synthesized phosphopeptide derived from human mTOR around the phosphorylation site of serine 2481 (I-H-SP-F-I).
- Positive controlHuman brain tissue
- Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
- Storage bufferPreservative: 0.02% Sodium Azide
Constituents: 50% Glycerol, PBS (without Mg2+ and Ca2+),, 150mM Sodium chloride, pH 7.4
- Concentration information loading...
- PurityImmunogen affinity purified
- Purification notesThe antibody was affinity-purified from The antibody was affinity-purified fromr abbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
- Clonality Polyclonal
- Epigenetics and Nuclear Signaling
- DNA / RNA
- DNA Damage & Repair
- DNA Damage Response
- DNA Damage Recognition
Our Abpromise guarantee covers the use of ab59350 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IHC-P||IHC-P: Use at an assay dependent dilution.|
- 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.
modificationsAutophosphorylated; 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.
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Anti-mTOR antibody images
ab59350, at a 1/50-1/100 dilution, staining human mTOR in brain with (+) or without (-) immunising peptide, using Immunohistochemistry, Paraffin embedded tissue
References for Anti-mTOR antibody (ab59350)
ab59350 has not yet been referenced specifically in any publications.