This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular compartments of eukaryotic cells. 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. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Clone
G5
Isotype
IgG2b/k
Host species
Mouse
Species Reactivity
Human, mouse, rat
Cellular Localization
cytoplasm
Positive Control
stomach, cerebellum, cerebral cortex, and kidney tissues
Applications
IHC, ELISA, ICC/IF, IP, WB
Intended Use
Research Use Only