ATP6V1H polyclonal antibody

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 an 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. The H subunit of V-ATPase, also designated SDF is comprised of two polypeptides derived from the same gene. This regulatory subunit plays a critical role in the functional coupling of ATP hydrolysis activity to proton transport in the V-ATPase pump.

V-type proton ATPase subunit H; V-ATPase subunit H; Nef-binding protein 1; NBP1; Protein VMA13 homolog; V-ATPase 50/57 kDa subunits; Vacuolar proton pump subunit H; Vacuolar proton pump subunit SFD; ATP6V1H; CGI-11

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of ATP6V1H polyclonal antibody at 1:500 dilution LaneA:H9C2 whole cell lysate LaneB:MEF whole cell lysate LaneC:A549 whole cell lysate LaneD:HepG2 whole cell lysate