Mitochondrial membrane ATP synthase (F1F0 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, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane 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.

ATP synthase subunit alpha, mitochondrial (ATP synthase F1 subunit alpha) ATP5F1A ATP5A ATP5A1 ATP5AL2 ATPM

Human

WB,ELISA

WB 1:500-1:5000
ELISA 1:5000-1:20000

59.751 kDa ;

ATP5F1A ATP5A ATP5A1 ATP5AL2 ATPM

p25705

https://www.uniprot.org/uniprotkb/p25705

Recombinant Human ATP synthase subunit alpha, mitochondrial protein (44-553AA)

Rabbit

Polyclonal

IgG

Tags Cell Markers; Metabolism; Signal transduction

>95%, Protein G purified

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4

Store at -20°C. Do not aliquot the antibody