Anti-Proton Pump (H,K-ATPase beta subunit) (Mouse) mAb

WB - 2-10 ug/mL (chemiluminescence detection system) IP - 5-10 ug/200-300 uL of cell extract IHC - 2-10 ug/mL

Hydrogen-potassium adenosine triphosphatase (H + , K + -ATPase) belongs to a family of P-type cation-transporting ATPases that also includes Ca 2+ -ATPase and Na + , K + -ATPase. H + , K + -ATPase is responsible for acid secre tion into the stomach and catalyzes electroneutral excha nge of cytoplasmic hydrogen ions and external potassium ions coupled with ATP hydrolysis. The enzyme is found in gastric parietal cells where it is located in cytoplasmi c vesicles or apical plasma membranes of the secretory canaliculus. H + , K + -ATPase is a heterodimer consisting of a high molecular weight catalytic α subunit and a smaller but heavily glycosylated α subunit. The α subunit of H + , K + -ATPase has 10 transmembrane domains and contains sites for ATP binding and its acylphosphorylation, binding sites of proton pump inhibitors, and sites responsible for ion recognition.

1 mg/ml

100ug IgG in 100ul volume of PBS containing 50% glycerol, pH 7.2. No preservative is contained.

Human: 496 Mouse: 11945 Rat: 24217

Hybridoma, fusion of spleen cells Balb / c nu removal of thymus cells and induce Sp2/0-Ag14 myeloma, autoimmune gastritis / + mouse neonatal

This antibody reacts with human, mouse, rat and bovine H + , K + -ATPase α subunit.

1 year

This antibody was purified from hybridoma (clone 2B6) supernatant using protein A agarose. This hybridoma was established by fusion of mouse myeloma cell Sp2/0-Ag14 with Balb/c nu/+ mouse splenocyte with neonatal thymectomy-induced autoimmune gastritis.

Proton pump