Overview

  • Product nameRecombinant Human ATP5O protein
  • Protein lengthFull length protein

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • AccessionP48047
    • SpeciesHuman
    • SequenceMGSSHHHHHHSSGLVPRGSHMFAKLVRPPVQVYGIEGRYATALYSAASKQ NKLEQVEKELLRVAQILKEPKVAASVLNPYVKRSIKVKSLNDITAKERFS PLTTNLINLLAENGRLSNTQGVVSAFSTMMSVHRGEVPCTVTSASPLEEA TLSELKTVLKSFLSQGQVLKLEAKTDPSILGGMIVRIGEKYVDMSVKTKI QKLGRAMREIV
    • Molecular weight23 kDa including tags
    • Amino acids24 to 213
    • TagsHis tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab104549 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
  • Purity> 95 % SDS-PAGE.
    ab104549 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 or -80°C. Avoid repeated freeze / thaw cycles.

    Preservative: None
    Constituents: 40% Glycerol, 0.2M Sodium chloride, 20mM Tris HCl, 1mM DTT, pH 8.0

General Info

  • Alternative names
    • ATP synthase O subunit mitochondrial precursor
    • ATP synthase subunit O
    • ATP synthase, H+ transporting, mitochondrial F1 complex, O subunit
    • ATP5O
    • ATPO
    • ATPO_HUMAN
    • mitochondrial
    • Mitochondrial ATP synthase, O subunit
    • Oligomycin sensitivity conferral protein
    • OSCP
    see all
  • FunctionMitochondrial 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(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
  • Sequence similaritiesBelongs to the ATPase delta chain family.
  • Cellular localizationMitochondrion. Mitochondrion inner membrane.
  • Information by UniProt

Recombinant Human ATP5O protein images

  • 15% SDS-PAGE analysis of 3µg ab104549.

References for Recombinant Human ATP5O protein (ab104549)

ab104549 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"