ATP6 Protein, Human (His)

ATP6 Protein, Human (His) is the recombinant human-derived ATP6 protein, expressed by E. coli, with N-10*His tag.

ATP6 is subunit a of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V), which synthesizes ATP from ADP in the presence of a proton gradient across the membrane generated by the electron transport complexes of the respiratory chain (Probable). The ATP synthase complex consists of a soluble F(1) head domain (the catalytic core) and a membrane-bound F(0) domain (the proton channel) (by similar: PubMed:37244256). These two domains are connected by a central stalk rotating within the F(1) region and a stationary peripheral stalk (by similar: PubMed:37244256). During catalysis, ATP synthesis in the F(1) catalytic domain is coupled to proton translocation via a rotary mechanism of the central stalk subunits (Probable). Together with subunit c (ATP5MC1), ATP6 forms the proton-conducting channel in the F(0) domain, which contains two critical half-channels (inlet and outlet) that facilitate proton movement from the mitochondrial intermembrane space (IMS) into the matrix (by similar: PubMed:37244256). Protons are taken up via the inlet half-channel and released through the outlet half-channel, following a Grotthuss mechanism (by similar: PubMed:37244256).

Human

E. coli

N-10*His

P00846 (M1-T226)

4580

Full Length

MNENLFASFIAPTILGLPAAVLIILFPPLLIPTSKYLINNRLITTQQWLIKLTSKQMMTMHNTKGRTWSLMLVSLIIFIATTNLLGLLPHSFTPTTQLSMNLAMAIPLWAGTVIMGFRSKIKNALAHFLPQGTPTPLIPMLVIIETISLLIQPMALAVRLTANITAGHLLMHLIGSATLAMSTINLPSTLIIFTILILLTILEIAVALIQAYVFTLLVSLYLHDNT

Approximately 24 kDa, based on SDS-PAGE under reducing conditions.

Greater than 85% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.