ATP6V0D2蛋白抗体

ATP6V0D2蛋白抗体 Background: Vacuolar-type H+-ATPase (V-ATPase) is a multisubunit enzyme responsible for acidification of eukaryotic intracellular organelles. V-ATPases pump protons against an electrochemical gradient, while F-ATPases reverse the process, thereby synthesizing ATP. A peripheral V1 domain, which is responsible for ATP hydrolysis, and a integral V0 domain, which is responsible for proton translocation, compose V-ATPase. Nine subunits (A–H) make up the V1 domain and five subunits (a, d, c, c' and c") make up the V0 domain. Like F-ATPase, V-ATPase most likely operates through a rotary mechanism. V-ATPase D2 is a 350 amino acid protein that is expressed in kidney, lung and osteoclast. V-ATPase D2 has been implicated as a regulator of urine acidification, osteoclast fusion and bone formation. Furthermore, V-ATPase D2 has been identified as a dendritic cell marker. Also known as: V-ATPase D2; ATP6D2; ATPase H+ transporting lysosomal 38kDa V0 subunit D; ATPase H+ transporting lysosomal 38kDa V0 subunit D isoform 2; ATPase H+ transporting lysosomal 38kDa V0 subunit D2; FLJ38708; V ATPase subunit d 2; Vacuolar ATP synthase subunit d 2; Vacuolar proton pump subunit d 2; VMA 6; VMA6; VA0D2_HUMAN.ATP6V0D2蛋白抗体