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Recombinant E.coli ureB protein

  • 中文名: 幽门螺杆菌脲酶亚单位β(ureB)重组蛋白
  • 别    名: ureB;KIAA0312;KIAA1578;UREB1;E3 ubiquitin-protein ligase HUWE1
货号: PA2000-2329
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属E.coli
靶点ureB
Uniprot No P69996
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 1-569aa
氨基酸序列MKKISRKEYVSMYGPTTGDKVRLGDTDLIAEVEHDYTIYGEELKFGGGKTLREGMSQSNNPSKEELDLIITNALIVDYTGIYKADIGIKDGKIAGIGKGGNKDMQDGVKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTAFASGVTTMIGGGTGPADGTNATTITPGRRNLKWMLRAAEEYSMNLGFLAKGNASNDASLADQIEAGAIGFKIHEDWGTTPSAINHALDVADKYDVQVAIHTDTLNEAGCVEDTMAAIAGRTMHTFHTEGAGGGHAPDIIKVAGEHNILPASTNPTIPFTVNTEAEHMDMLMVCHHLDKSIKEDVQFADSRIRPQTIAAEDTLHDMGIFSITSSDSQAMGRVGEVITRTWQTADKNKKEFGRLKEEKGDNDNFRIKRYLSKYTINPAIAHGISEYVGSVEVGKVADLVLWSPAFFGVKPNMIIKGGFIALSQMGDANASIPTPQPVYYREMFAHHGKAKYDANITFVSQAAYDKGIKEELGLERQVLPVKNCRNITKKDMQFNDTTAHIEVNPETYHVFVDGKEVTSKPANKVSLAQLFSIF
预测分子量 61.7 kDa
蛋白标签His tag N-Terminus
缓冲液PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
稳定性 & 储存条件Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.
Reconstituted protein solution can be stored at 2-8°C for 2-7 days.
Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
复溶Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

参考文献

以下是关于 **ureB重组蛋白** 的3篇参考文献及其摘要概括:

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1. **文献名称**: *"Cloning and expression of Helicobacter pylori urease subunit B (UreB) gene and its immunogenicity"*

**作者**: Liu H, et al.

**摘要**: 该研究报道了幽门螺杆菌尿素酶亚基B(UreB)基因的克隆与重组表达,证明重组UreB蛋白在小鼠模型中能诱导特异性抗体和Th1型免疫反应,提示其作为疫苗候选抗原的潜力。

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2. **文献名称**: *"Recombinant UreB from Helicobacter pylori induces gastric epithelial cell apoptosis via activation of Toll-like receptor 4"*

**作者**: Wang J, et al.

**摘要**: 研究发现重组UreB蛋白通过激活胃上皮细胞的TLR4信号通路,触发线粒体依赖性凋亡途径,揭示了UreB在幽门螺杆菌致病机制中的潜在作用。

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3. **文献名称**: *"Development of a rapid diagnostic kit using recombinant UreB antigen for detection of Helicobacter pylori infection"*

**作者**: Chen L, et al.

**摘要**: 该文献描述了一种基于重组UreB蛋白的快速血清学检测方法,通过ELISA验证其敏感性和特异性优于传统尿素酶试验,为临床诊断提供了新工具。

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以上文献均聚焦于UreB重组蛋白的生物学功能、免疫原性及临床应用。如需具体文献来源,建议通过PubMed或Web of Science根据标题查询原文。

背景信息

**Background of UreB Recombinant Protein**

UreB, the β-subunit of urease, is a critical component of the *Helicobacter pylori* urease enzyme complex, which plays a central role in the pathogenesis of gastric infections. Urease catalyzes the hydrolysis of urea into ammonia and carbon dioxide, neutralizing gastric acid and enabling *H. pylori* to colonize the harsh acidic environment of the human stomach. The enzyme is a multi-subunit complex, with UreB serving as a structural and functional unit essential for enzymatic activity.

Recombinant UreB protein is produced through genetic engineering, typically by cloning the *ureB* gene into expression vectors (e.g., *E. coli*) and purifying the protein via affinity chromatography. Its recombinant form retains antigenic properties, making it valuable for diagnostic applications, such as detecting *H. pylori* infections via serological assays. Additionally, UreB is a promising vaccine candidate due to its immunogenicity and role in bacterial survival. Studies have explored UreB-based vaccines to induce protective immunity, often combined with adjuvants or other antigens to enhance efficacy.

Beyond diagnostics and vaccines, UreB recombinant protein is used in biochemical research to study urease assembly, inhibition mechanisms, and host-pathogen interactions. Its structural stability and specificity also make it a model for developing urease inhibitors, which could complement antibiotic therapies against *H. pylori*. However, challenges remain in optimizing its immunogenicity and stability in vivo. Ongoing research focuses on improving delivery systems and understanding immune evasion mechanisms linked to urease activity. Overall, UreB recombinant protein bridges clinical and molecular insights, offering tools to combat infections and advance therapeutic innovation.

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