• STJ73757 Immunofluorescence analysis of paraformaldehyde fixe HEK293 cells, permeabilized with 0. 15% Triton. Primary incubation 1hr (10ug/ml) followed by Alexa Fluor 488 secondary antibody (2ug/ml) , showing endoplasmic reticulum and cytoplasmic staining. The nuclear stain is DAPI (blue). Negative control: Unimmunized goat IgG (10ug/ml) followed by Alexa Fluor 488 secondary antibody (2ug/ml).

Anti-MTOR/FRAP2 antibody (1137-1150) (STJ73757)

SKU:
STJ73757-100

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Host: Goat
Applications: Pep-ELISA/IF
Reactivity: Human/Mouse/Rat/Dog/Pig/Cow
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Goat polyclonal antibody anti-MTOR/FRAP2 (1137-1150) is suitable for use in ELISA and Immunofluorescence research applications.
Clonality: Polyclonal
Conjugation: Unconjugated
Isotype: IgG
Formulation: 0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin. NA
Purification: Purified from goat serum by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide.
Concentration: 0.5 mg/mL
Dilution Range: IF-Strong expression of the protein seen in the ER and vesicles/cytoplasm of HEK293 cells. 10µg/ml
ELISA-antibody detection limit dilution 1:64000.
Storage Instruction: Store at-20°C on receipt and minimise freeze-thaw cycles.
Gene Symbol: MTOR
Gene ID: 2475
Uniprot ID: MTOR_HUMAN
Immunogen Region: 1137-1150
Accession Number: NP_004949.1
Immunogen Sequence: ETVDRLTESLDFTD
Post Translational Modifications Autophosphorylates when part of mTORC1 or mTORC2. Phosphorylation at Ser-1261, Ser-2159 and Thr-2164 promotes autophosphorylation. Phosphorylation in the kinase domain modulates the interactions of MTOR with RPTOR and AKT1S1/PRAS40 and leads to increased intrinsic mTORC1 kinase activity. Phosphorylation at Ser-2159 by TBK1 in response to growth factors and pathogen recognition receptors promotes mTORC1 activity. Phosphorylation at Thr-2173 in the ATP-binding region by AKT1 strongly reduces kinase activity.
Function Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals. MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2). In response to nutrients, growth factors or amino acids, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4. Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex. Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor. Activates dormant ribosomes by mediating phosphorylation of SERBP1, leading to SERBP1 inactivation and reactivation of translation. In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1. To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A. In the same time, mTORC1 inhibits catabolic pathways: negatively regulates autophagy through phosphorylation of ULK1. Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1. Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP. Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions. Prevents autophagy by mediating phosphorylation of AMBRA1, thereby inhibiting AMBRA1 ability to mediate ubiquitination of ULK1 and interaction between AMBRA1 and PPP2CA. mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor. Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules. The mTORC1 complex is inhibited in response to starvation and amino acid depletion. The non-canonical mTORC1 complex, which acts independently of RHEB, specifically mediates phosphorylation of MiT/TFE factors MITF, TFEB and TFE3 in the presence of nutrients, promoting their cytosolic retention and inactivation. Upon starvation or lysosomal stress, inhibition of mTORC1 induces dephosphorylation and nuclear translocation of TFEB and TFE3, promoting their transcription factor activity. The mTORC1 complex regulates pyroptosis in macrophages by promoting GSDMD oligomerization. MTOR phosphorylates RPTOR which in turn inhibits mTORC1. As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton. mTORC2 plays a critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of phosphoinositide 3-kinase, facilitating its activation by PDK1. mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B. mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422'. Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms. Plays an important regulatory role in the circadian clock function.regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks. Phosphorylates SQSTM1, promoting interaction between SQSTM1 and KEAP1 and subsequent inactivation of the BCR(KEAP1) complex.
Protein Name Serine/Threonine-Protein Kinase Mtor
Fk506-Binding Protein 12-Rapamycin Complex-Associated Protein 1
Fkbp12-Rapamycin Complex-Associated Protein
Mammalian Target Of Rapamycin
Mtor
Mechanistic Target Of Rapamycin
Rapamycin And Fkbp12 Target 1
Rapamycin Target Protein 1
Database Links Reactome: R-HSA-1257604
Reactome: R-HSA-1632852
Reactome: R-HSA-165159
Reactome: R-HSA-166208
Reactome: R-HSA-3371571
Reactome: R-HSA-380972
Reactome: R-HSA-389357
Reactome: R-HSA-5218920
Reactome: R-HSA-5628897
Reactome: R-HSA-5674400
Reactome: R-HSA-6804757
Reactome: R-HSA-8943724
Reactome: R-HSA-9639288
Cellular Localisation Lysosome Membrane
Peripheral Membrane Protein
Cytoplasmic Side
Endoplasmic Reticulum Membrane
Golgi Apparatus Membrane
Mitochondrion Outer Membrane
Cytoplasm
Nucleus
Pml Body
Microsome Membrane
Cytoplasmic Vesicle
Phagosome
Shuttles Between Cytoplasm And Nucleus
Accumulates In The Nucleus In Response To Hypoxia
Targeting To Lysosomes Depends On Amino Acid Availability And Rraga And Rragb
Lysosome Targeting Also Depends On Interaction With Meak7
Translocates To The Lysosome Membrane In The Presence Of Tm4sf5
Alternative Antibody Names Anti-Serine/Threonine-Protein Kinase Mtor antibody
Anti-Fk506-Binding Protein 12-Rapamycin Complex-Associated Protein 1 antibody
Anti-Fkbp12-Rapamycin Complex-Associated Protein antibody
Anti-Mammalian Target Of Rapamycin antibody
Anti-Mtor antibody
Anti-Mechanistic Target Of Rapamycin antibody
Anti-Rapamycin And Fkbp12 Target 1 antibody
Anti-Rapamycin Target Protein 1 antibody
Anti-MTOR antibody
Anti-FRAP antibody
Anti-FRAP1 antibody
Anti-FRAP2 antibody
Anti-RAFT1 antibody
Anti-RAPT1 antibody

Information sourced from Uniprot.org

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