Tel:
+49 (0)241 95 163 153
Fax:
+49 (0)241 95 163 155
E-Mail:
orders@anticorps-enligne.fr

ATP5EP2 anticorps (AA 19-52)

L’anticorps Lapin Polyclonal anti-ATP5EP2 a été validé pour WB. Il convient pour détecter ATP5EP2 dans des échantillons de Humain.
N° du produit ABIN6242139

Aperçu rapide pour ATP5EP2 anticorps (AA 19-52) (ABIN6242139)

Antigène

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

Reactivité

Humain

Hôte

Lapin

Clonalité

Polyclonal

Application

Western Blotting (WB)

Clone

RB53889
  • Épitope

    AA 19-52

    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.

    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

    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
Vous êtes ici:
Chat with us!