This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogen
This ATP5D antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 156-188 amino acids from the C-terminal region of human ATP5D.
fk58f09 antikoerper, zgc:73303 antikoerper, wu:fk58f09 antikoerper, MGC85306 antikoerper, GB17255 antikoerper, DDBDRAFT_0216607 antikoerper, DDBDRAFT_0238330 antikoerper, DDB_0216607 antikoerper, DDB_0238330 antikoerper, 0610008F14Rik antikoerper, 1500000I11Rik antikoerper, AA960090 antikoerper, AI876556 antikoerper, AU020773 antikoerper, C85518 antikoerper, ATP synthase, H+ transporting, mitochondrial F1 complex, delta subunit antikoerper, ATP synthase, H+ transporting, mitochondrial F1 complex, delta subunit L homeolog antikoerper, ATP synthase F1 delta antikoerper, atp5d antikoerper, atp5d.L antikoerper, ATP5D antikoerper, LOC552682 antikoerper, atp5D antikoerper, Atp5d antikoerper
Hintergrund
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.