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

ATPC1 Protein (AA 43-161, partial) (GST tag)

ATPC1 Origine: Humain Hôte: Escherichia coli (E. coli) Recombinant > 90 % SDS
N° du produit ABIN5712073
  • Antigène Voir toutes ATPC1 Protéines
    ATPC1 (ATP Synthase gamma Chain 1 (ATPC1))
    Type de proteíne
    Recombinant
    Attributs du protein
    AA 43-161, partial
    Origine
    • 2
    • 1
    Humain
    Source
    • 2
    • 1
    Escherichia coli (E. coli)
    Purification/Conjugué
    Cette ATPC1 protéine est marqué à la GST tag.
    Application
    SDS-PAGE (SDS)
    Séquence
    ASPTQVFFNG ANVRQVDVPT LTGAFGILAA HVPTLQVLRP GLVVVHAEDG TTSKYFVSSG SIAVNADSSV QLLAEEAVTL DMLDLGAAKA NLEKAQAELV GTADEATRAE IQIRIEANE
    Purification
    SDS-PAGE
    Pureté
    > 90 %
  • Indications d'application
    Optimal working dilution should be determined by the investigator.
    Restrictions
    For Research Use only
  • Format
    Liquid
    Concentration
    0.1-2 mg/mL
    Buffer
    20 mM Tris-HCl based buffer, pH 8.0
    Stock
    -80 °C,4 °C,-20 °C
    Stockage commentaire
    Store at -20°C, for extended storage, conserve at -20°C or -80°C. Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Antigène
    ATPC1 (ATP Synthase gamma Chain 1 (ATPC1))
    Autre désignation
    ATPD (ATPC1 Produits)
    Synonymes
    T19J18.4 Protein, T19J18_4 Protein, ATPase, F1 complex, gamma subunit protein Protein, ATPC1 Protein
    Sujet
    Mitochondrial mbrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the mbrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extrambraneous catalytic core, and F0 - containing the mbrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F1 domain and of the central stalk which is part of the complex rotary elent. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
    Poids moléculaire
    39.8 kDa
    UniProt
    P30049
Vous êtes ici:
Support technique