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ATP5EP2 Antikörper (AA 19-52)

ATP5EP2 Reaktivität: Human WB Wirt: Kaninchen Polyclonal RB53889 unconjugated
Produktnummer ABIN6242139
  • Target
    ATP5EP2 (ATP Synthase, H+ Transporting, Mitochondrial F1 Complex, epsilon Subunit Pseudogene 2 (ATP5EP2))
    Bindungsspezifität
    AA 19-52
    Reaktivität
    Human
    Wirt
    Kaninchen
    Klonalität
    Polyklonal
    Applikation
    Western Blotting (WB)
    Aufreinigung
    This antibody is purified through a protein A column, followed by peptide affinity purification.
    Immunogen
    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.
    Klon
    RB53889
    Isotyp
    Ig Fraction
  • Applikationshinweise
    WB: 1:2000
    Beschränkungen
    Nur für Forschungszwecke einsetzbar
  • Format
    Liquid
    Buffer
    Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
    Konservierungsmittel
    Sodium azide
    Vorsichtsmaßnahmen
    This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
    Lagerung
    4 °C,-20 °C
    Haltbarkeit
    6 months
  • Target
    ATP5EP2 (ATP Synthase, H+ Transporting, Mitochondrial F1 Complex, epsilon Subunit Pseudogene 2 (ATP5EP2))
    Andere Bezeichnung
    ATP5EP2
    Synonyme
    ATP synthase, H+ transporting, mitochondrial F1 complex, epsilon subunit pseudogene 2 antikoerper, ATP5EP2 antikoerper
    Hintergrund
    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).
    Molekulargewicht
    5807
    UniProt
    Q5VTU8
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