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Item No. 32343

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Helicobacter pylori (H. pylori) is a Gram-negative bacterium that can infect and colonize the stomach, leading to chronic gastritis, stomach inflammation and oxidative stress, peptic ulcer disease, and gastric cancer.1 H. pylori urease is a nickel-dependent enzyme that catalyzes the hydrolysis of urea to produce ammonia and bicarbonate, an effect that protects H. pylori by neutralizing stomach acid and contributes to the pathogenesis of H. pylori infection.2,3 It exists as a dodecamer of four αβ heterotrimers composed of UreB and UreA subunits, which contain the catalytic active sites and mediate subunit association, respectively.3,4 H. pylori urease is expressed predominantly in the cytoplasm but is also present on the cell surface.3 The activity of H. pylori urease has been used as a biomarker for H. pylori infection.5 Cayman's Urease Helicobacter pylori Rabbit Monoclonal Antibody (RM412) can be used for ELISA.
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1. Role of bacteria in oncogenesis. Clin. Microbiol. Rev. 23(4), 837-857 (2010).
2. Metalloregulation of Helicobacter pylori physiology and pathogenesis. Front. Microbiol. 6, 911 (2015).
3. Supramolecular assembly and acid resistance of Helicobacter pylori urease. Nat. Struct. Biol. 8(6), 505-509 (2001).
4. Surface properties of Helicobacter pylori urease complex are essential for persistence. PLoS One 5(11), e15042 (2010).
5. Helicobacter pylori urease for diagnosis of Helicobacter pylori infection: A mini review. J. Adv. Res. 13, 51-57 (2018).