ATP5F1B Protein, Human (P.pastoris, His)

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.

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.

Human

P. pastoris

N-His

P06576 (48A-529S)

506  [NCBI]

AQTSPSPKAGAATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFMEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHSS

Approximately 53.8 kDa

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

<1 EU/μg, determined by LAL method.