ATP5A1
Origine: Rat
Hôte: Levure
Recombinant
> 90 %
ELISA
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.
atp5a Protein, MGC108350 Protein, AI035633 Protein, AL022851 Protein, AL023067 Protein, Atpm Protein, D18Ertd206e Protein, Mom2 Protein, ATP5A Protein, ATP5AL2 Protein, ATPM Protein, MC5DN4 Protein, MOM2 Protein, OMR Protein, ORM Protein, hATP1 Protein, zgc:154103 Protein, ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle L homeolog Protein, ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle Protein, ATP synthase subunit alpha, mitochondrial Protein, ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1 Protein, atp5a1.L Protein, ATP5A1 Protein, atp5a1 Protein, LOC100395383 Protein, Atp5a1 Protein
Sujet
Mitochondrial membrane 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 synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites .