Product Name :ATP6AP1 polyclonal antibody
Reactivity :Human,Mouse,Rat
Application_all :WB: 1:500~1:1000
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, 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.
Product :Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Purification&Purity :The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Storage&Stability :Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.
Specificity :ATP6AP1 polyclonal antibody detects endogenous levels of ATP6AP1 protein.
Note :For research use only, not for use in diagnostic procedure.
Alternative Name :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
Immunogen :A synthetic peptide corresponding to residues in Human ATP6AP1.
Modification :Unmodification