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AB271731

Recombinant Human RHEB protein (His tag N-Terminus)

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Recombinant Human RHEB protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 181 aa range, expressed in Baculovirus infected Sf9 cells, with 90%, suitable for SDS-PAGE.

View Alternative Names

RHEB2, RHEB, GTP-binding protein Rheb, Ras homolog enriched in brain

1 Images
SDS-PAGE - Recombinant Human RHEB protein (His tag N-Terminus) (AB271731)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human RHEB protein (His tag N-Terminus) (AB271731)

SDS-PAGE analysis of 4 μg ab271731.

Key facts

Purity

90% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q15382

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.02% Potassium chloride

storage-buffer

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Complementary Products

Secondary Antibodies

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Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488)

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Primary Antibodies

AB92313

Anti-RHEB antibody [EPR2971]

BOND RX™ Validated|RabMAb|Recombinant

Immunocytochemistry/ Immunofluorescence - Anti-RHEB antibody [EPR2971] (AB92313)

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Proteins & Peptides

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Recombinant human PTEN protein

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Proteins & Peptides

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Recombinant Human IRS1 protein

SDS-PAGE - Recombinant Human IRS1 protein (AB70538)

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MPQSKSRKIAILGYRSVGKSSLTIQFVEGQFVDSYDPTIENTFTKLITVNGQEYHLQLVDTAGQDEYSIFPQTYSIDINGYILVYSVTSIKSFEVIKVIHGKLLDMVGKVQIPIMLVGNKKDLHMERVISYEEGKALAESWNAAFLESSAKENQTAVDVFRRIILEAEKMDGAASQGKSSC","proteinLength":"Full Length","predictedMolecularWeight":"23 kDa","actualMolecularWeight":null,"aminoAcidEnd":181,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Baculovirus infected Sf9 cells","accessionNumber":"Q15382","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

RHEB also known as Ras homolog enriched in brain is a small GTPase with a molecular mass of approximately 21 kDa. It is a member of the Ras superfamily and plays a role in the regulation of cell growth and proliferation. RHEB is widely expressed with concentrations found in the brain skeletal muscle and various other tissues. It functions as a molecular switch cycling between active GTP-bound and inactive GDP-bound states influencing signaling pathways linked to growth and metabolism.
Biological function summary

RHEB interacts with several components within the mTORC1 complex a major regulator of cell growth and autophagy. This protein positively regulates the mTORC1 pathway by activating mTOR leading to protein synthesis and cell growth when nutrients such as amino acids and energy are available. RHEB's regulation of mTORC1 is influenced by upstream modulation through the TSC1/2 complex acting as a sensor for cellular energy levels and growth signals. The role of RHEB in these regulatory mechanisms highlights its fundamental importance in cellular metabolic processes.

Pathways

RHEB plays a significant role in the mechanistic target of rapamycin (mTOR) signaling pathway which is important for regulating protein synthesis and cellular growth. RHEB acts downstream of the TSC1/2 complex with TSC2 acting as a GTPase-activating protein for RHEB. This interaction points RHEB as an essential regulator of mTORC1 activation. In connection with other proteins RHEB functions alongside mTOR and TSC1/2 to mediate responses to cellular nutrient status thereby adjusting growth and proliferation accordingly.

Mutations or dysregulation of RHEB have been linked to tuberous sclerosis complex (TSC) and cancer. In TSC where aberrant signaling occurs through the mTOR pathway RHEB's activity influences the mTORC1 pathway in cells lacking functional TSC1 or TSC2 leading to benign tumors. Additionally RHEB overexpression has been implicated in certain cancers due to its capacity to enhance cell proliferation via mTORC1. The interaction of RHEB with mTOR highlights its role in disease states where cell growth control is altered suggesting the potential for targeted therapies in treating these conditions.
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Specifications

Form

Liquid

Additional notes

Affinity purified.

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General info

Function

Small GTPase that acts as an allosteric activator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed : 12172553, PubMed : 12271141, PubMed : 12842888, PubMed : 12869586, PubMed : 12906785, PubMed : 15340059, PubMed : 15854902, PubMed : 16098514, PubMed : 20381137, PubMed : 22819219, PubMed : 24529379, PubMed : 29416044, PubMed : 32470140, PubMed : 33157014, PubMed : 25816988). In response to nutrients, growth factors or amino acids, specifically activates the protein kinase activity of MTOR, the catalytic component of the mTORC1 complex : acts by causing a conformational change that allows the alignment of residues in the active site of MTOR, thereby enhancing the phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) (PubMed : 29236692, PubMed : 33157014). RHEB is also required for localization of the TSC-TBC complex to lysosomal membranes (PubMed : 24529379). In response to starvation, RHEB is inactivated by the TSC-TBC complex, preventing activation of mTORC1 (PubMed : 24529379, PubMed : 33157014). Has low intrinsic GTPase activity (PubMed : 15340059).

Sequence similarities

Belongs to the small GTPase superfamily. Rheb family.

Post-translational modifications

Farnesylation is important for efficiently activating mTORC1-mediated signaling.. Polyubiquitinated in response to amino acid, promoting its interaction with MTOR and mTORC1 activation (PubMed:33157014). Deubiquitination by ATXN3 promotes recruitment of the TSC-TBC complex and RHEB inactivation by TSC2 (PubMed:33157014). Monoubiquitinated at Lys-8 by RNF152, promoting its association with the TSC-TBC complex (PubMed:30514904). Deubiquitinated at Lys-8 by USP4, promoting mTORC1 activation (PubMed:30514904).. Phosphorylation by MAPKAPK5 impairs GTP-binding and inactivation.

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Product protocols

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Target data

Small GTPase that acts as an allosteric activator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed : 12172553, PubMed : 12271141, PubMed : 12842888, PubMed : 12869586, PubMed : 12906785, PubMed : 15340059, PubMed : 15854902, PubMed : 16098514, PubMed : 20381137, PubMed : 22819219, PubMed : 24529379, PubMed : 29416044, PubMed : 32470140, PubMed : 33157014, PubMed : 25816988). In response to nutrients, growth factors or amino acids, specifically activates the protein kinase activity of MTOR, the catalytic component of the mTORC1 complex : acts by causing a conformational change that allows the alignment of residues in the active site of MTOR, thereby enhancing the phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) (PubMed : 29236692, PubMed : 33157014). RHEB is also required for localization of the TSC-TBC complex to lysosomal membranes (PubMed : 24529379). In response to starvation, RHEB is inactivated by the TSC-TBC complex, preventing activation of mTORC1 (PubMed : 24529379, PubMed : 33157014). Has low intrinsic GTPase activity (PubMed : 15340059).
See full target information RHEB
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