Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • SpeciesHuman
    • SequenceMASMTGGQQM GRGSASMPQS KSRKIAILGY RSVGKSSLTI QFVEGQFVDS YDPTIENTFT KLITVNGQEY HLQLVDTAGQ DEYSIFPQTY SIDINGYILV YSVTSIKSFE VIKVIHGKLL DMVGKVQIPI MLVGNKKDLH MERVISYEEG KALAESWNAA FLESSAKENQ TAVDVFRRII LEAEKMDGAA SQGKSSC

Specifications

Our Abpromise guarantee covers the use of ab78768 in the following tested applications.

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

  • Applications

    SDS-PAGE

  • Purity> 95 % SDS-PAGE.
    ab78768 is purified using conventional chromatography techniques.
  • 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: None
    Constituents: 10% Glycerol, 20mM Tris, 1mM DTT, pH 8.0

General Info

  • Alternative names
    • Ras homolog enriched in brain 2, formerly
    • GTP binding protein Rheb
    • GTP-binding protein Rheb
    • MGC111559
    • Ras homolog enriched in brain
    • Ras homolog enriched in brain 2
    • Rheb
    • RHEB 2
    • RHEB_HUMAN
    • RHEB2
    • RHEB2, formerly
    see all
  • FunctionStimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Activates the protein kinase activity of mTORC1. Has low intrinsic GTPase activity.
  • Tissue specificityUbiquitous. Highest levels observed in skeletal and cardiac muscle.
  • Sequence similaritiesBelongs to the small GTPase superfamily. Rheb family.
  • Post-translational
    modifications
    Farnesylation is important for efficiently activating mTORC1-mediated signaling.
  • Cellular localizationCell membrane.
  • Information by UniProt

Recombinant Human RHEB protein images

  • 15% SDS-PAGE showing ab76768 at approximately 22kDa (3µg).

References for Recombinant Human RHEB protein (ab78768)

ab78768 has not yet been referenced specifically in any publications.

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