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.

Description: Rabbit polyclonal to ATP6V0D2

Immunogen: KLH conjugated synthetic peptide derived from ATP6V0D2

Specificity:  ·Reacts with Human, Mouse, Pig, Dog and Rat.

·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 40 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;

·Immunocytochemistry/Immunofluorescence: 1/100;

·Immunoprecipitation: 1/50;

·ELISA: 1/500;

·Optimal working dilutions must be determined by the end user.