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Recombinant Human ATP5F1 protein (ab152211)

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SDS-PAGE - Recombinant Human ATP5F1 protein (ab152211)

    Key features and details

    • Expression system: Wheat germ
    • Suitable for: SDS-PAGE, WB, ELISA

    Description

    • Product name

      Recombinant Human ATP5F1 protein
    • Expression system

      Wheat germ
    • Accession

      P24539
    • Protein length

      Full length protein
    • Animal free

      No
    • Nature

      Recombinant
      • Species

        Human
      • Sequence

        MLSRVVLSAAATAAPSLKNAAFLGPGVLQATRTFHTGQPHLVPVPPLPEY GGKVRYGLIPEEFFQFLYPKTGVTGPYVLGTGLILYALSKEIYVISAETF TALSVLGVMVYGIKKYGPFVADFADKLNEQKLAQLEEAKQASIQHIQNAI DTEKSQQALVQKRHYLFDVQRNNIAMALEVTYRERLYRVYKEVKNRLDYH ISVQNMMRRKEQEHMINWVEKHVVQSISTQQEKETIAKCIADLKLLAKKA QAQPVM
      • Predicted molecular weight

        55 kDa including tags
      • Amino acids

        1 to 256

    Associated products

    • Related Products

      • Anti-ATP5F1 antibody [9D1BC4] (ab117991)

    Specifications

    Our Abpromise guarantee covers the use of ab152211 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

      Western blot

      ELISA

    • Form

      Liquid
    • Additional notes

       

       

    • 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

      • 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.
    • Target information above from: UniProt accession P24539 The UniProt Consortium
      The Universal Protein Resource (UniProt) in 2010
      Nucleic Acids Res. 38:D142-D148 (2010) .

      Information by UniProt

    Images

    • SDS-PAGE - Recombinant Human ATP5F1 protein (ab152211)
      SDS-PAGE - Recombinant Human ATP5F1 protein (ab152211)
      12.5% SDS-PAGE analysis of ab152211 stained with Coomassie Blue.

    Protocols

    To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.

    Click here to view the general protocols

    Datasheets and documents

    • Datasheet
  • References (0)

    Publishing research using ab152211? Please let us know so that we can cite the reference in this datasheet.

    ab152211 has not yet been referenced specifically in any publications.

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