Description

  • Product name

    Recombinant Human ATP5E protein
  • Expression system

    Wheat germ
  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      MVAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAEKTSGSNVKIVKVKK E
    • Amino acids

      1 to 51
    • Tags

      GST tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab157933 in the following tested applications.

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

  • Applications

    ELISA

    Western blot

  • Form

    Liquid
  • Additional notes

    Protein concentration is above or equal to 0.05 mg/ml.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.31% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names

    • ATP 5E
    • ATP synthase epsilon chain mitochondrial
    • ATP synthase H+ transporting mitochondrial F1 complex epsilon subunit
    • ATP synthase subunit epsilon
    • ATP5E
    • ATP5E_HUMAN
    • ATPase subunit epsilon
    • ATPE
    • F(0)F(1) ATPase
    • H(+) transporting two sector ATPase
    • MGC104243
    • mitochondrial
    • Mitochondrial ATP synthase epsilon chain
    • Mitochondrial ATPase
    see all
  • Function

    Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
  • Tissue specificity

    Ubiquitous.
  • Sequence similarities

    Belongs to the eukaryotic ATPase epsilon family.
  • Cellular localization

    Mitochondrion. Mitochondrion inner membrane.
  • Information by UniProt

Images

  • ab157933 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab157933 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

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