Recombinant Human Raptor protein is a Human Full Length protein, in the 1 to 379 aa range, expressed in Wheat germ and suitable for SDS-PAGE, ELISA, WB.
M E S E M L Q S P L L G L G E E D E A D L T D W N L P L A F M K K R H C E K I E G S K S L A Q S W R M K D R M K T V S V A L V L C L N V G V D P P D V V K T T P C A R L E C W I D P L S M G P Q K A L E T I G A N L Q K Q Y E N W Q P R A R Y K Q S L D P T V D E V K K L C T S L R R N A K E E R V L F H Y N G H G V P R P T V N G E V W V F N K N Y T Q Y I P L S I Y D L Q T W M G S P S I F V Y D C S N A G L I V K S F K Q F A L Q R E Q E L E V A A I N P N H P L A Q M P L P P S M K N C I Q L A A C E A T E L L P M I P D L P A D L F T S C L T T P I K I A L R W F C M Q K C V S L V P G V T L D L I E K I P G R L N D R R T P L G E L N W I F T A I T D T I A W N V L P R D L F Q K L F R Q D L L V A S L F R N F L L A E R I M R S Y N C T P V S S P R L P P T Y M H A M W
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Component of the mechanistic target of rapamycin complex 1 (mTORC1), an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:32561715, PubMed:37541260). 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 several substrates, such as ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:37541260). In the same time, it inhibits catabolic pathways by phosphorylating the autophagy initiation components ULK1 and ATG13, as well as transcription factor TFEB, a master regulators of lysosomal biogenesis and autophagy (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:32561715, PubMed:37541260). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:37541260). Within the mTORC1 complex, RPTOR acts both as a molecular adapter, which (1) mediates recruitment of mTORC1 to lysosomal membranes via interaction with small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD), and a (2) substrate-specific adapter, which promotes substrate specificity by binding to TOS motif-containing proteins and direct them towards the active site of the MTOR kinase domain for phosphorylation (PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:37541260). mTORC1 complex regulates many cellular processes, such as odontoblast and osteoclast differentiation or neuronal transmission (By similarity). mTORC1 complex in excitatory neuronal transmission is required for the prosocial behavior induced by the psychoactive substance lysergic acid diethylamide (LSD) (By similarity).
KIAA1303, RAPTOR, RPTOR, Regulatory-associated protein of mTOR, Raptor, p150 target of rapamycin (TOR)-scaffold protein
Recombinant Human Raptor protein is a Human Full Length protein, in the 1 to 379 aa range, expressed in Wheat germ and suitable for SDS-PAGE, ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.31% Glutathione
Component of the mechanistic target of rapamycin complex 1 (mTORC1), an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:32561715, PubMed:37541260). 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 several substrates, such as ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:37541260). In the same time, it inhibits catabolic pathways by phosphorylating the autophagy initiation components ULK1 and ATG13, as well as transcription factor TFEB, a master regulators of lysosomal biogenesis and autophagy (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:32561715, PubMed:37541260). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:37541260). Within the mTORC1 complex, RPTOR acts both as a molecular adapter, which (1) mediates recruitment of mTORC1 to lysosomal membranes via interaction with small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD), and a (2) substrate-specific adapter, which promotes substrate specificity by binding to TOS motif-containing proteins and direct them towards the active site of the MTOR kinase domain for phosphorylation (PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:37541260). mTORC1 complex regulates many cellular processes, such as odontoblast and osteoclast differentiation or neuronal transmission (By similarity). mTORC1 complex in excitatory neuronal transmission is required for the prosocial behavior induced by the psychoactive substance lysergic acid diethylamide (LSD) (By similarity).
Belongs to the WD repeat RAPTOR family.
Insulin-stimulated phosphorylation at Ser-863 by MTOR and MAPK8 regulates mTORC1 activity (PubMed:19864431). Phosphorylated at Ser-863 by NLK in response to stress, disrupting the interaction with small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD), thereby preventing lysosome recruitment and activation of the mTORC1 complex (PubMed:26588989). Osmotic stress also induces phosphorylation at Ser-696, Thr-706 and Ser-863 by MAPK8 (PubMed:19864431, PubMed:22493283). Ser-863 phosphorylation is required for phosphorylation at Ser-855 and Ser-859 (PubMed:19864431). In response to nutrient limitation, phosphorylated at Ser-722 and Ser-792 by AMPK; phosphorylation promotes interaction with 14-3-3 proteins, leading to negative regulation of the mTORC1 complex (PubMed:18439900). Phosphorylation at Ser-722 and Ser-792 by AMPK in response to glucose starvation inhibits O-GlcNAcylation by OGT and subsequent activation of mTORC1 (PubMed:37541260). In response to growth factors, phosphorylated at Ser-719, Ser-721 and Ser-722 by RPS6KA1, which stimulates mTORC1 activity (PubMed:18439900, PubMed:18722121). Phosphorylation at Ser-791 by PKA downstream of cAMP inhibits the mTORC1 complex (PubMed:31112131). Phosphorylated at Ser-877 by TBK1, leading to negative regulation of the mTORC1 complex (PubMed:31530866).
Raptor short for Regulatory-associated protein of mTOR functions as an important component of the mechanistic target of rapamycin complex 1 (mTORC1). Raptor itself has a molecular mass of around 150 kDa. It is expressed in many tissues with high levels found in muscle liver and brain. Raptor plays a mechanical role as a scaffolding protein which facilitates the recruitment of substrates to mTORC1 and regulates its activity. By binding with mTOR and other components Raptor ensures proper signaling involving growth factors energy levels and nutrient availability.
Raptor serves as an essential part of cell growth and proliferation by being a constituent of the mTORC1 complex. This complex is sensitive to nutrients energy oxygen and stress signals allowing cells to adjust their functions based on environmental conditions. Raptor aids mTORC1 in translating these cellular inputs into appropriate responses such as protein synthesis and autophagy inhibition. It therefore plays a pivotal role in coordinating cellular adaptation and homeostasis.
The mTOR signaling which involves Raptor is significant for the regulation of cell growth and metabolism. The two main pathways where Raptor shows importance are the PI3K/AKT/mTOR and AMP-activated protein kinase (AMPK) pathways. Raptor interacts with other proteins like Akt and TSC2 providing a link between growth factor signals and cellular metabolic processes. These interactions help balance energy consumption and storage maintaining cellular and organismal energy stability.
Raptor has links to cancer and type 2 diabetes. Aberrant mTORC1 activity influenced by dysregulation of Raptor contributes to tumorigenesis through uncontrolled cell proliferation. Similarly alterations in Raptor function affect insulin signaling pathways leading to metabolic disturbances observed in type 2 diabetes. In both contexts Raptor interacts with proteins like TSC1 and PRAS40 further influencing disease progression and therapeutic outcomes.
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ab112419 analysed on a 12.5% SDS-PAGE gel stained with Coomassie Blue.
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