Overview

  • Product name
    Recombinant Human ATP5E protein
  • Protein length
    Full length protein

Description

  • Nature
    Recombinant
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      MVAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAEKTSGSNVKIVKVKK E
    • Amino acids
      1 to 51
    • Tags
      proprietary 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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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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