Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • SpeciesHuman
    • SequenceGPIKTKQFAPIHAEAPEFMEMSVEQEILVTGIKVVDLLAPYAKGGKIGLF GGAGV GKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIES GVINLKDATSKV ALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDV LLFIDNIFRFTQAGSEVSA LLGRIPSAVGYQPTLATDMGTMQERITTT KKGSITSVQAIYVPADDLTDPAPATT FAHLDATTVLSRAIAELGIYPA VDPLDSTSRIMDPNIVGSEHYDVARGVQKILQD YKSLQDIIAILGMDE LSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLK ETIKGFQQ ILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHSS
    • Amino acids156 to 529

Specifications

Our Abpromise guarantee covers the use of ab92235 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

  • FormLyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: 0.5% Trehalose, 6M Urea, 100mM Sodium phosphate, 10mM Sodium chloride, pH 4.5

  • ReconstitutionReconstitution with 143 µl aqua dest.

General Info

  • Alternative names
    • ATP 5B
    • ATP synthase H+ transporting mitochondrial F1 complex beta polypeptide
    • ATP synthase subunit beta mitochondrial
    • ATP synthase subunit beta, mitochondrial
    • atp5b
    • ATPB
    • ATPB_HUMAN
    • ATPMB
    • ATPSB
    • Epididymis secretory protein Li 271
    • HEL-S-271
    • Mitochondrial ATP synthase beta subunit
    • Mitochondrial ATP Synthase Subunit Beta
    • Mitochondrial ATP synthetase beta subunit
    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. 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.
  • Sequence similaritiesBelongs to the ATPase alpha/beta chains family.
  • Cellular localizationMitochondrion. Mitochondrion inner membrane. Peripheral membrane protein.
  • Information by UniProt

Recombinant Human ATPB protein images

  • The image shows an electrophoretic assay performed using an Agilent 5100 ALP. In some images coloured control bands can be seen at 15 kDa (green) and/or 240 kDa (purple). The protein-specific band is blue.

References for Recombinant Human ATPB protein (ab92235)

ab92235 has not yet been referenced specifically in any publications.

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