Atp5a1 (NM_007505) Mouse Recombinant Protein

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. Subunits alpha and beta form the catalytic core in F (1) . 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. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity) . Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity) .[UniProtKB/Swiss-Prot Function]

Purified recombinant protein of Mouse ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1 (Atp5a1), with C-terminal MYC/DDK tag, expressed in HEK293T cells, 20ug

Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.