Overview

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Sequence
      MGSSHHHHHH SSGLVPRGSH MGSLILYALS KEIYVISAET FTALSVLGVM VYGIKKYGPF VADFADKLNE QKLAQLEEAK QASIQHIQNA IDTEKSQQAL VQKRHYLFDV QRNNIAMALE VTYRERLYRV YKEVKNRLDY HISVQNMMRR KEQEHMINWV EKHVVQSIST QQEKETIAKC IADLKLLAKK AQAQPVM
    • Molecular weight
      23 kDa including tags
    • Amino acids
      83 to 256
    • Tags
      His tag N-Terminus
    • Additional sequence information
      (NP_001679).

Associated products

Specifications

Our Abpromise guarantee covers the use of ab177591 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
    > 80 % SDS-PAGE.

  • 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.

    Information available upon request.

General Info

  • Alternative names
    • AT5F1_HUMAN
    • ATP synthase B chain mitochondrial
    • ATP synthase subunit b
    • ATP synthase subunit b mitochondrial
    • ATP synthase, H+ transporting, mitochondrial F0 complex, subunit b,
    • ATP synthase, H+ transporting, mitochondrial F0 complex, subunit b, isoform 1
    • ATP synthase, H+ transporting, mitochondrial F0 complex, subunit B1
    • ATP5F1
    • ATPase subunit b
    • Cell proliferation inducing protein 47
    • H+ ATP synthase subunit b
    • MGC24431
    • mitochondrial
    • PIG47
    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(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 similarities
    Belongs to the eukaryotic ATPase B chain family.
  • Cellular localization
    Mitochondrion. Mitochondrion inner membrane.
  • Information by UniProt

Images

  • 15% SDS-PAGE analysis of ab177591 (3μg).

References

ab177591 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"

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