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Recombinant Human UPRT protein

  • 中文名: 尿嘧啶磷酸核糖转移酶(UPRT)重组蛋白
  • 别    名: UPRT;Uracil phosphoribosyltransferase homolog
货号: PA1000-3421
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点UPRT
Uniprot NoQ96BW1
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-309aa
氨基酸序列MGSSHHHHHH SSGLVPRGSH MGSMATELQC PDSMPCHNQQ VNSASTPSPE QLRPGDLILD HAGGNRASRA KVILLTGYAH SSLPAELDSG ACGGSSLNSE GNSGSGDSSS YDAPAGNSFL EDCELSRQIG AQLKLLPMND QIRELQTIIR DKTASRGDFM FSADRLIRLV VEEGLNQLPY KECMVTTPTG YKYEGVKFEK GNCGVSIMRS GEAMEQGLRD CCRSIRIGKI LIQSDEETQR AKVYYAKFPP DIYRRKVLLM YPILSTGNTV IEAVKVLIEH GVQPSVIILL SLFSTPHGAK SIIQEFPEIT ILTTEVHPVA PTHFGQKYFG TD
预测分子量36 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3篇与UPRT重组蛋白相关的文献摘要示例(注:文献信息为模拟生成,仅供参考):

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1. **文献名称**: *Functional characterization of Toxoplasma gondii UPRT in 5-fluorouracil resistance*

**作者**: Smith A, et al.

**摘要**: 本研究通过重组表达弓形虫UPRT蛋白,证实其缺失导致对5-氟尿嘧啶(5-FU)的敏感性显著升高,揭示了UPRT通过代谢5-FU为毒性产物的机制,为抗寄生虫药物靶点研究提供依据。

2. **文献名称**: *Optimization of recombinant UPRT expression in E. coli for enzymatic studies*

**作者**: Chen L, et al.

**摘要**: 报道了一种高效重组UPRT蛋白的大肠杆菌表达系统,通过密码子优化和纯化策略改进,获得高活性酶用于动力学分析,为后续抑制剂筛选奠定基础。

3. **文献名称**: *Structural insights into UPRT catalytic mechanism by X-ray crystallography*

**作者**: Tanaka K, et al.

**摘要**: 解析了重组UPRT蛋白的晶体结构,发现其活性中心关键氨基酸残基与底物结合模式,阐明其催化尿嘧啶转化为UMP的分子机制,指导靶向药物设计。

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**说明**:以上文献方向覆盖功能研究、重组表达优化及结构分析。实际研究中建议通过PubMed或Web of Science以关键词“UPRT recombinant protein”或“Uracil Phosphoribosyltransferase expression”检索最新文章。

背景信息

**Background of UPRT Recombinant Protein**

Uracil phosphoribosyltransferase (UPRT) is a key enzyme involved in the pyrimidine salvage pathway, catalyzing the conversion of uracil to uridine monophosphate (UMP) using phosphoribosyl pyrophosphate (PRPP). This enzymatic activity is critical for nucleotide biosynthesis in organisms that rely on salvage pathways, including certain parasites, bacteria, and protozoa. In humans, however, UPRT is absent, making it a potential therapeutic target for pathogens dependent on this enzyme.

Recombinant UPRT refers to the protein produced through genetic engineering, typically expressed in heterologous systems like *E. coli* or mammalian cell lines. Its production enables detailed biochemical and structural studies, facilitating the exploration of substrate specificity, catalytic mechanisms, and inhibitor development. UPRT has garnered particular interest in parasitology, as pathogens such as *Toxoplasma gondii* and *Plasmodium* species (malaria parasites) require UPRT for survival. Inhibiting UPRT in these organisms disrupts nucleotide metabolism, offering a strategy for antiparasitic drug design.

Additionally, recombinant UPRT serves as a tool in molecular biology. For example, it is employed in 5-fluorouracil (5-FU) sensitivity assays, where UPRT activity converts 5-FU into toxic metabolites, enabling selective cell ablation in transgenic systems. This application is valuable in cancer research and neuroscience for studying cell lineage or targeted cell elimination.

Structural studies of recombinant UPRT have revealed conserved catalytic domains and species-specific variations, guiding the development of selective inhibitors. Furthermore, engineered UPRT variants with altered substrate preferences or enhanced stability have expanded its utility in biotechnological applications.

Overall, recombinant UPRT bridges fundamental research and translational medicine, providing insights into pathogen metabolism, drug discovery, and experimental tool development. Its unique role in non-mammalian systems underscores its importance as both a therapeutic target and a versatile research reagent.

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