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.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB:1:500~1:1000 IHC:1:50~1:200
Application Notes:
ATP6V1H polyclonal antibody detects endogenous levels of ATP6V1H protein.
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