protein

ATP5F1B Protein, Human (P.pastoris, His)

HY-P71716

20 μg;50 μg;100 μg

145;280;450 USD

ATP5F1B Protein, Human (P.pastoris, His)

proteins

P. pastoris

20 μg;50 μg;100 μg

145;280;450 USD

ATP5F1B protein is an important component of mitochondrial membrane ATP synthase (complex V). ATP5F1B Protein, Human (P.pastoris, His) is the recombinant human-derived ATP5F1B protein, expressed by P. pastoris , with N-His labeled tag. The total length of ATP5F1B Protein, Human (P.pastoris, His) is 482 a.a., with molecular weight of ~53.8 kDa.

Human

The ATP5F1B protein is an integral part of the mitochondrial membrane ATP synthase, also known as Complex V, responsible for ATP production from ADP in the presence of a proton gradient across the membrane generated by the electron transport complexes of the respiratory chain. F-type ATPases are composed of two structural domains: F(1), which houses the extramembraneous catalytic core, and F(0), containing 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) domain is coupled to proton translocation through a rotary mechanism of the central stalk subunits. The catalytic core in F(1) is formed by subunits alpha and beta, where the rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to the hydrolysis of ATP in three separate catalytic sites on the beta subunits. ATP5F1B plays a crucial role in this intricate process, contributing to the efficient synthesis of ATP within the mitochondrial membrane.

ATP 5B; ATP synthase H+ transporting mitochondrial F1 complex beta polypeptide; ATPB; ATPB_HUMAN; ATPMB; ATPSB

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

Lyophilized after extensive dialysis against solution in PBS, 6% Trehalose, pH 7.4.

Room temperature in continental US; may vary elsewhere.