ATP6AP1 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, 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 the 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. ATP6AP1 (ATPase, H+ transporting, lysosomal accessory protein 1), also known as 16A, CF2, Ac45, XAP3, ATP6S1, VATPS1 (vacuolar ATP synthase S1 accessory protein) or ATP6IP1, is a type I transmembrane, V-ATPase accessory protein that is predominantly expressed in endocrine and neuronal cells. ATP6AP1 is responsible for targeting the V-ATPase enzyme to specialized complex vacuolar systems. Via its cytoplasmic tail, ATP6AP1 interacts with subunits of the V0 domain. The disruption of this interaction in osteoclasts results in impaired bone resorption, suggesting an important role for ATP6AP1 in proper osteoclastic bone resorption.

V-type proton ATPase subunit S1; V-ATPase subunit S1; Protein XAP-3; V-ATPase Ac45 subunit; V-ATPase S1 accessory protein; Vacuolar proton pump subunit S1; ATP6AP1; ATP6IP1; ATP6S1; VATPS1; XAP3

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 ATP6AP1 polyclonal antibody at 1:500 dilution Lane1:MCF-7 whole cell lysate Lane2:Raw264.7 whole cell lysate Lane3:H9C2 whole cell lysate