Overview

Description

  • Nature

    Recombinant
  • Source

    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species

      Human
    • Sequence

      QKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAE EMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVG EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGI KAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGSDEKKKLY CIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSG CSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY LHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQI FLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREV AAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVR GYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRADGKISEQSDAKLKEI VTNFLAGFEA
    • Molecular weight

      59 kDa including tags
    • Amino acids

      44 to 553
    • Tags

      His tag N-Terminus
    • Additional sequence information

      N-terminal 6xHis-tagged. Full length mature chain without transit peptide.

Specifications

Our Abpromise guarantee covers the use of ab235862 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

    > 90 % SDS-PAGE.

  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

    Constituents: Tris buffer, 50% Glycerol

General Info

  • Alternative names

    • ATP synthase alpha chain
    • ATP synthase alpha chain, mitochondrial
    • ATP synthase subunit alpha
    • ATP synthase subunit alpha mitochondrial
    • ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle
    • ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, 1
    • ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, isoform 1, cardiac muscle
    • ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, isoform 2, non-cardiac muscle-like 2
    • ATP sythase (F1 ATPase) alpha subunit
    • ATP5A
    • Atp5a1
    • ATP5AL2
    • ATPA_HUMAN
    • ATPM
    • Epididymis secretory sperm binding protein Li 123m
    • hATP1
    • HEL-S-123m
    • MC5DN4
    • mitochondrial
    • Mitochondrial ATP synthetase
    • Mitochondrial ATP synthetase oligomycin resistant
    • Modifier of Min 2
    • Modifier of Min 2 mouse homolog
    • Modifier of Min 2, mouse, homolog of
    • MOM2
    • OMR
    • ORM
    • OTTHUMP00000163475
    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. Subunits alpha and beta form the catalytic core in F(1). 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. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites.
  • Tissue specificity

    Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord.
  • Sequence similarities

    Belongs to the ATPase alpha/beta chains family.
  • Post-translational
    modifications

    The N-terminus is blocked.
  • Cellular localization

    Mitochondrion inner membrane. Peripheral membrane protein.
  • Information by UniProt

Images

  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel analysis of ab235862.

References

ab235862 has not yet been referenced specifically in any publications.

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