ATP6V0A2 polyclonal antibody

Vacuolar-type H+-ATPase (V-ATPase) is a multisubunit enzyme responsible for the 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 an integral V0 domain, which is responsible for proton translocation, comprise the V-ATPase complex. Nine subunits (A–H) make up the V1 domain and five subunits (A, D, C, C' and C") make up the V0 domain. As part of the V0 domain, V-ATPase A2 (ATPase, H+ transporting, lysosomal V0 subunit a2), consists of 856 amino acids and is also known as ATP6V0A2, V-type proton ATPase subunit a isoform 2, vacuolar proton translocating ATPase subunit a isoform 2, lysosomal H(+)-transporting ATPase V0 subunit a2 or TJ6. V-ATPase A2 is a multi-pass membrane protein with localization in the cell membrane, endosome membrane and the subapical vesicles of the kidney’s proximal tubules. V-ATPase A2 plays an important role in Golgi function by regulating pH. Wrinkly skin syndrome (WSS) and cutis laxa type II (ARCL type II) are caused as a result of V-ATPase A2 defects.