MT-ATP6 Protein, Chicken (Cell-Free, His)

MT-ATP6 protein is a component of mitochondrial membrane ATP synthase (complex V), which helps convert ADP into ATP through the proton gradient established by the respiratory chain electron transport complex. As part of the F-type ATPase, MT-ATP6 contributes to the rotational mechanism that links ATP synthesis in the F(1) catalytic domain to proton translocation. MT-ATP6 Protein, Chicken (Cell-Free, His) is the recombinant MT-ATP6 protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of MT-ATP6 Protein, Chicken (Cell-Free, His) is 227 a.a., with molecular weight of 26.3 kDa.

The MT-ATP6 protein is an integral component of the mitochondrial membrane ATP synthase, also known as Complex V, which facilitates the conversion of ADP to ATP in the presence of a proton gradient across the mitochondrial membrane. This gradient is established by the electron transport complexes of the respiratory chain. The F-type ATPases, to which MT-ATP6 belongs, are comprised of two primary structural domains: F(1), encompassing the extramembraneous catalytic core, and F(0), housing the membrane proton channel. These domains are interconnected by a central stalk and a peripheral stalk. During the catalytic process, ATP synthesis in the F(1) catalytic domain is coordinated with proton translocation through a rotary mechanism involving the central stalk subunits. MT-ATP6, as a key component of the proton channel, likely plays a direct role in facilitating the translocation of protons across the membrane. The overall F-type ATPase complex includes two components: CF(1), the catalytic core, and CF(0), the membrane proton channel, with specific subunits contributing to their distinct functions.

Others

E. coli Cell-free

N-10*His

P14092 (M1-I227)

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MNLSFFDQFSSPCLLGIPLILPSLLLPALLLPSPGNRWINNRLSTIQLWFTHLITKQLMTPLNKAGHKWALLLTSLILMLLSINLLGLLPYTFTPTTQLSMNMALALPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGHLLIQLISTATIALLPMMPSISALTALILFLLTILEVAVAMIQAYVFVLLLSLYLQENI

26.3 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.