Description

  • Product name

    Recombinant Human ATP5D protein
  • Purity

    > 95 % SDS-PAGE.
    ab109956 was purified using conventional chromatography.
  • Expression system

    Escherichia coli
  • Accession

  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      MGSSHHHHHHSSGLVPRGSHMAEAAAAPAAASGPNQMSFTFASPTQVFFN GANVRQVDVPTLTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSS GSIAVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQAELVGTADEATRA EIQIRIEANEALVKALE
    • Predicted molecular weight

      17 kDa including tags
    • Amino acids

      23 to 168
    • Tags

      His tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab109956 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

    Mass Spectrometry

  • Mass spectrometry

    MALDI-TOF
  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

    pH: 8.00
    Constituents: 0.316% Tris HCl, 20% Glycerol, 0.058% Sodium chloride

General Info

  • Alternative names

    • ATP synthase subunit delta, mitochondrial
    • ATP synthase, H+ transporting, mitochondrial F1 complex, delta subunit
    • ATP5D
    • ATPD_HUMAN
    • F ATPase delta subunit
    • F-ATPase delta subunit
    • Mitochondrial ATP synthase complex delta subunit precusor
    • Mitochondrial ATP synthase delta subunit
    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 turnover 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.
  • Sequence similarities

    Belongs to the ATPase epsilon chain family.
  • Cellular localization

    Mitochondrion. Mitochondrion inner membrane.
  • Information by UniProt

Images

  • 15% SDS-PAGE analysis of 3 µg ab109956.

References

ab109956 has not yet been referenced specifically in any publications.

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