protein

ATP5D Protein, Human (His)

HY-P72098

5 μg;10 μg

55;95 USD

ATP5D Protein, Human (His)

proteins

E. coli

5 μg;10 μg

55;95 USD

ATP5D Protein, a vital component of mitochondrial membrane ATP synthase (Complex V), facilitates ATP generation from ADP using the proton gradient established by respiratory chain electron transport complexes. As part of the F(1) domain and central stalk, ATP5D contributes to ATP hydrolysis through a rotary mechanism. The ATP synthase complex, involving ATP5D, is pivotal for cellular energy production via ATP synthesis. ATP5D Protein, Human (His) is the recombinant human-derived ATP5D protein, expressed by E. coli , with N-10*His labeled tag. The total length of ATP5D Protein, Human (His) is 146 a.a., with molecular weight of ~20 kDa.

Human

The ATP5D protein functions as a crucial component of the mitochondrial membrane ATP synthase, also known as Complex V. This enzyme is responsible for generating ATP from ADP by utilizing the proton gradient across the mitochondrial membrane, a gradient established by the electron transport complexes of the respiratory chain. The F-type ATPases, to which ATP5D belongs, consist of two main structural domains: F(1), housing the catalytic core, and F(0), housing the membrane proton channel. During catalysis, ATP turnover in the F(1) catalytic domain is linked to proton translocation through a rotary mechanism involving the central stalk subunits. ATP5D is part of both the F(1) domain and the central stalk, contributing to the rotation that leads to ATP hydrolysis. The ATP synthase complex, in which ATP5D participates, includes various subunits and plays a pivotal role in cellular energy production through ATP synthesis.

ATP synthase subunit delta; mitochondrial ; ATP synthase subunit delta; mitochondrial; ATP synthase; H+ transporting; mitochondrial F1 complex; delta subunit; ATP5D; ATPD_HUMAN; F ATPase delta subunit ; F-ATPase delta subunit; Mitochondrial ATP synthase complex delta subunit precusor ; Mitochondrial ATP synthase delta subunit

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

Lyophilized from a 0.2 μm solution of Tris-based buffer, 50% Glycerol or 50 mM Tris-HCL, 300 mM NaCL, pH 7.4.

Room temperature in continental US; may vary elsewhere.