Rabbit Polyclonal UREA antibody. Suitable for ELISA and reacts with Canavalia ensiformis samples. Cited in 2 publications.
Preservative: 0.01% Sodium azide
Constituents: 0.88% Sodium chloride, 0.164% Sodium phosphate
| ELISA | |
|---|---|
| Canavalia ensiformis | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Canavalia ensiformis | Dilution info Use at an assay dependent concentration. | Notes - |
Urea hydrolase involved in nitrogen recycling from ureide, purine, and arginine catabolism (PubMed:26690979). Is known to be highly toxic and lethal when given by intravenous route, producing convulsions and other signs of central nervous system intoxication associated with the high levels of ammonia formed in the blood of mice and rabbits (PubMed:26690979). Is neurotoxic in mammals, when directly injected into hippocampus (PubMed:33631299). It may induce seizures by acting at a neuronal network level, thereby disturbing electroencephalographic rhythms and causing metabolic alterations in key areas related to epileptogenesis and to neurogenic pulmonary edema (PubMed:33631299). It increases calcium influx and neuronal firing rate in the hippocampus (PubMed:33631299). Is able to insert itself into lipid bilayers, altering physicochemical properties of artificial membranes, and forming cation-selective ion channels (PubMed:24583269). In vitro, has the ability to induce platelet aggregation, platelet granules secretion and release of ATP (PubMed:11696010). In contrast to canatoxin, another urease from C.ensiformis, is not lethal to mice when intraperitoneally injected (PubMed:11696010).
Urease, Jack bean urease, Urea amidohydrolase, JBU
Rabbit Polyclonal UREA antibody. Suitable for ELISA and reacts with Canavalia ensiformis samples. Cited in 2 publications.
Preservative: 0.01% Sodium azide
Constituents: 0.88% Sodium chloride, 0.164% Sodium phosphate
Anti-Urease (Jack Bean) (Rabbit) Antibody was prepared from monospecific antiserum by a delipidation and defibrination.
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Urease also known as urea amidohydrolase is an enzyme with a significant role in nitrogen metabolism. It mechanically catalyzes the hydrolysis of urea into carbon dioxide and ammonia. This enzyme is commonly associated with a molecular mass ranging from 480 kDa to 600 kDa depending on species and isoform. Urease expresses predominantly in bacteria fungi and plants with significant incidence in gastrointestinal tract microorganisms like Helicobacter pylori. It is also present in some invertebrates but not usually in vertebrates.
Urease plays a significant role in nitrogen metabolism by assisting the recycling of nitrogenous waste products and facilitating nutrient acquisition. It functions mainly as part of a multi-subunit complex usually composed of alpha beta and gamma subunits. These subunits coordinate to form a metalloenzyme that requires nickel ions to be catalytically active. This enzyme's ability to convert urea into ammonia makes it essential for nitrogen economy in various ecological settings.
Urease is an integral component of the nitrogen cycle and is active in the urea degradation pathway. This pathway is important for recycling nitrogen in nature affecting soil fertility and plant growth. Urease links to proteins involved in ammonia assimilation such as glutamine synthetase which helps incorporate ammonia into amino acids. This relationship facilitates nitrogen availability for living organisms and enhances ecosystem productivity.
Urease relates to conditions like gastric ulcers and certain kidney stones. Helicobacter pylori employs urease to neutralize stomach acid enabling its survival and leading to gastritis and peptic ulcer disease. Also urease activity contributes to the formation of struvite stones in the urinary tract where urea-splitting bacteria like Proteus mirabilis produce ammonia leading to stone formation. These conditions illustrate urease’s involvement with bacterial proteins like flagellar proteins and virulence factors that facilitate colonization and infection.
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