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ATP5EP2 antibody (AA 19-52)

The Rabbit Polyclonal anti-ATP5EP2 antibody has been validated for WB. It is suitable to detect ATP5EP2 in samples from Human.
Catalog No. ABIN6242139

Quick Overview for ATP5EP2 antibody (AA 19-52) (ABIN6242139)

Target

ATP5EP2 (ATP Synthase, H+ Transporting, Mitochondrial F1 Complex, epsilon Subunit Pseudogene 2 (ATP5EP2))

Reactivity

Human

Host

Rabbit

Clonality

Polyclonal

Application

Western Blotting (WB)

Clone

RB53889
  • Binding Specificity

    AA 19-52

    Purification

    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.

    Isotype

    Ig Fraction
  • Application Notes

    WB: 1:2000

    Restrictions

    For Research Use only
  • Format

    Liquid

    Buffer

    Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.

    Preservative

    Sodium azide

    Precaution of Use

    This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

    Storage

    4 °C,-20 °C

    Expiry Date

    6 months
  • Target

    ATP5EP2 (ATP Synthase, H+ Transporting, Mitochondrial F1 Complex, epsilon Subunit Pseudogene 2 (ATP5EP2))

    Alternative Name

    ATP5EP2

    Background

    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).

    Molecular Weight

    5807

    UniProt

    Q5VTU8
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