Crystallography grade
ATP5A1
Spezies: Human
Wirt: Escherichia coli (E. coli)
Recombinant
>95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
ELISA, SDS, WB, Crys
Optimal working dilution should be determined by the investigator.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Konzentration
0.1-2 mg/mL
Buffer
20 mM Tris-HCl based buffer, pH 8.0
Lagerung
-80 °C,4 °C,-20 °C
Informationen zur Lagerung
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.
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Hintergrund
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 .