Anti-ATP5D

Custom conjugation services for this antibody as available (eg. labeling of Anti-ATP5D with HRP. Available labels are AF: AF350, AF488, AF555, AF594, AF647, AF680, AF700, AF750. Proteins: HRP, Alkaline Phosphatase, Streptavidin. Tandems: APC, APC/Cy7, APC/AF750, APC/iFluor(TM) 700, APC/iFluor(TM) 750, PE, PE/Cy5, PE/Cy7, PE/AF610, PE/AF700, PE/iFluor(TM) 594, PE/iFluor(TM) 647, PE/iFluor(TM) 700, PE/iFluor(TM) 750, PE/Texas Red(R), PerCP, PerCP/Cy5.5. Small Molecules: Biotin. Traditional Dyes: FITC (Fluorescein), TRITC (Rhodamine), PacBlue, PacOrange, Cy3, Cy5. iFluor: 350, 405, 430, 450, 488, 514, 532, 546, 555, 560, 568, 594, 610, 633, 647, 660, 670, 680, 700, 710, 750, 790, 800, 810, 820, 840, 860, A7. mFluor: UV375, UV460, Violet 450, Violet 500, Violet 510, Violet 540, Blue 570, Green 620, Red 700, Red 780. Protein function: 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 (PubMed:29478781). 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 (PubMed:1531933). [The UniProt Consortium]