ATPC1 Protein (AA 23-168) (His-SUMO Tag)

Produktnummer ABIN5709107

Produktdetails

Target: ATPC1 (ATP Synthase gamma Chain 1 (ATPC1))

Protein-Typ: Recombinant

Proteineigenschaft: AA 23-168

Spezies: Human

Quelle: Escherichia coli (E. coli)

Aufreinigungstag / Konjugat: Dieses ATPC1 Protein ist gelabelt mit His-SUMO Tag.

Applikation: SDS-PAGE (SDS)

Sequenz: AEAAAAPAAA SGPNQMSFTF ASPTQVFFNG ANVRQVDVPT LTGAFGILAA HVPTLQVLRP GLVVVHAEDG TTSKYFVSSG SIAVNADSSV QLLAEEAVTL DMLDLGAAKA NLEKAQAELV GTADEATRAE IQIRIEANEA LVKALE

Aufreinigung: SDS-PAGE

Reinheit: > 90 %

Anwendungsinformationen

Applikationshinweise: Optimal working dilution should be determined by the investigator.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

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.

Antigendetails

Target: ATPC1 (ATP Synthase gamma Chain 1 (ATPC1))

Andere Bezeichnung: ATPD (ATPC1 Produkte)

Synonyme: T19J18.4 Protein, T19J18_4 Protein, ATPase, F1 complex, gamma subunit protein Protein, ATPC1 Protein

Hintergrund: 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.

Molekulargewicht: 31.01 kDa

UniProt: P30049