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ATP5EP2 anticorps (AA 19-52)

ATP5EP2 Reactivité: Humain WB Hôte: Lapin Polyclonal RB53889 unconjugated
N° du produit ABIN6242139
  • Antigène
    ATP5EP2 (ATP Synthase, H+ Transporting, Mitochondrial F1 Complex, epsilon Subunit Pseudogene 2 (ATP5EP2))
    Épitope
    AA 19-52
    Reactivité
    Humain
    Hôte
    Lapin
    Clonalité
    Polyclonal
    Application
    Western Blotting (WB)
    Purification
    This antibody is purified through a protein A column, followed by peptide affinity purification.
    Immunogène
    This ATP5EP2 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 19-52 amino acids from the Central region of human ATP5EP2.
    Clone
    RB53889
    Isotype
    Ig Fraction
  • Indications d'application
    WB: 1:2000
    Restrictions
    For Research Use only
  • Format
    Liquid
    Buffer
    Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
    Agent conservateur
    Sodium azide
    Précaution d'utilisation
    This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
    Stock
    4 °C,-20 °C
    Date de péremption
    6 months
  • Antigène
    ATP5EP2 (ATP Synthase, H+ Transporting, Mitochondrial F1 Complex, epsilon Subunit Pseudogene 2 (ATP5EP2))
    Autre désignation
    ATP5EP2
    Synonymes
    anticorps ATP synthase, H+ transporting, mitochondrial F1 complex, epsilon subunit pseudogene 2, anticorps ATP5EP2
    Sujet
    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(1) domain and of the central stalk which is part of the complex rotary element. 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 (By similarity).
    Poids moléculaire
    5807
    UniProt
    Q5VTU8
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