Analytical Data
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Gene name
ureB
- Application
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Alternative Names
ureB；KIAA0312；KIAA1578；UREB1；E3 ubiquitin-Protein ligase HUWE1
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P69996
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Expression Region
1-569aa
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AA Sequence
MKKISRKEYVSMYGPTTGDKVRLGDTDLIAEVEHDYTIYGEELKFGGGKTLREGMSQSNNPSKEELDLIITNALIVDYTGIYKADIGIKDGKIAGIGKGGNKDMQDGVKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTAFASGVTTMIGGGTGPADGTNATTITPGRRNLKWMLRAAEEYSMNLGFLAKGNASNDASLADQIEAGAIGFKIHEDWGTTPSAINHALDVADKYDVQVAIHTDTLNEAGCVEDTMAAIAGRTMHTFHTEGAGGGHAPDIIKVAGEHNILPASTNPTIPFTVNTEAEHMDMLMVCHHLDKSIKEDVQFADSRIRPQTIAAEDTLHDMGIFSITSSDSQAMGRVGEVITRTWQTADKNKKEFGRLKEEKGDNDNFRIKRYLSKYTINPAIAHGISEYVGSVEVGKVADLVLWSPAFFGVKPNMIIKGGFIALSQMGDANASIPTPQPVYYREMFAHHGKAKYDANITFVSQAAYDKGIKEELGLERQVLPVKNCRNITKKDMQFNDTTAHIEVNPETYHVFVDGKEVTSKPANKVSLAQLFSIF
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Molecular Weight
61.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
UreB is a significant component of the urease enzyme complex, which catalyzes the hydrolysis of urea into ammonia and carbon dioxide, playing a crucial role in nitrogen metabolism in various organisms, including plants and microbes. The study of UreB is particularly important due to its potential applications in agricultural biotechnology and environmental management, as urease activity is linked to nitrogen cycling in soils. Additionally, UreB has been a focal point in medical research due to the role of urease in the pathogenesis of certain infections, such as those caused by Helicobacter pylori, which is associated with stomach ulcers and cancer. Recombinant UreB proteins can provide valuable insights into the enzyme's structure and function, enabling the exploration of its kinetic properties and interactions with other proteins. Furthermore, the ability to produce UreB through recombinant DNA technology allows for the development of specific inhibitors, which can act as therapeutic agents by mitigating the harmful effects of excessive urease activity. Overall, research on recombinant UreB not only enhances our understanding of fundamental biological processes but also opens pathways for innovative solutions in health and agriculture.
