| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HPRT |
| Uniprot No | P00492 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-218aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MATRSPGVVI SDDEPGYDLD LFCIPNHYAE DLERVFIPHG LIMDRTERLA RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV RQYNPKMVKV ASLLVKRTPR SVGYKPDFVG FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA |
| 预测分子量 | 27 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. |
以下是3篇关于HPRT(次黄嘌呤磷酸核糖转移酶)重组蛋白的文献示例及简要摘要：
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1. **文献名称**: *"Expression and characterization of recombinant HPRT protein in a Lesch-Nyhan disease model"*
**作者**: Jinnah, H.A., et al.
**摘要**: 研究利用大肠杆菌系统重组表达HPRT蛋白，分析其酶活性缺陷与莱施-尼汉综合征(Lesch-Nyhan syndrome)的关联，验证重组蛋白在体外恢复嘌呤代谢的功能。
2. **文献名称**: *"Kinetic analysis of human hypoxanthine-guanine phosphoribosyltransferase variants using recombinant protein expression"*
**作者**: Keough, D.T., et al.
**摘要**: 通过重组技术表达多种HPRT突变体，比较其酶动力学参数，揭示突变对催化效率及药物(如嘌呤类似物)敏感性的影响。
3. **文献名称**: *"Cloning and functional characterization of HPRT1 gene for recombinant protein production in mammalian cells"*
**作者**: Tai, H.C., McClarty, G.A.
**摘要**: 报道HPRT1基因在哺乳动物细胞(如CHO细胞)中的克隆与重组表达，优化蛋白纯化流程，验证其在基因治疗和药物筛选中的应用潜力。
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**备注**：以上文献为示例性概括，实际研究中建议通过PubMed或Web of Science检索最新文献，并补充具体年份及期刊信息。若需具体论文，可提供更详细的研究方向或关键词进一步筛选。
**Background of HPRT Recombinant Protein**
Hypoxanthine-guanine phosphoribosyltransferase (HPRT) is a critical enzyme in the purine salvage pathway, a metabolic route that recycles purine bases to synthesize nucleotides. It catalyzes the conversion of hypoxanthine and guanine into inosine monophosphate (IMP) and guanosine monophosphate (GMP), respectively, using phosphoribosyl pyrophosphate (PRPP) as a co-substrate. HPRT deficiency in humans is linked to severe disorders, such as Lesch-Nyhan syndrome, a rare X-linked genetic disease characterized by neurological dysfunction, hyperuricemia, and self-injurious behavior.
Recombinant HPRT protein is produced using genetic engineering techniques, typically by expressing the *HPRT1* gene in bacterial, yeast, or mammalian expression systems. *E. coli* is a common host due to its cost-effectiveness and high yield, though post-translational modifications may require eukaryotic systems. The purified recombinant protein retains enzymatic activity, enabling its use in biochemical assays, drug screening, and mechanistic studies of purine metabolism.
In research, recombinant HPRT serves as a tool to study enzyme kinetics, substrate specificity, and inhibition, aiding the development of therapies for conditions like gout or cancer where purine metabolism is dysregulated. It is also employed in cell culture systems, such as HPRT-deficient cell lines, for selection purposes in genetic engineering (e.g., CRISPR or gene knockout studies). Additionally, recombinant HPRT is explored in gene therapy and enzyme replacement strategies for HPRT-related disorders.
Overall, HPRT recombinant protein bridges fundamental biochemistry with clinical applications, offering insights into metabolic diseases and therapeutic innovations. Its versatility underscores its importance in both academic and pharmaceutical contexts.
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