| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PNP |
| Uniprot No | P00491 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-289aa |
| 氨基酸序列 | MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGLNPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQMGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS |
| 预测分子量 | 48.1kDa |
| 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PNP(嘌呤核苷磷酸化酶)重组蛋白的参考文献，包含文献名称、作者及摘要内容概括：
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1. **文献名称**：*Expression and characterization of recombinant human purine nucleoside phosphorylase*
**作者**：M. S. Hershfield et al.
**摘要**：该研究报道了在大肠杆菌中高效表达人源PNP重组蛋白的方法，通过优化表达载体和诱导条件获得可溶性蛋白，并验证其酶活性和底物特异性，为酶缺陷相关疾病的研究提供了工具。
2. **文献名称**：*Crystallographic structure of recombinant E. coli purine nucleoside phosphorylase complexed with a transition-state analogue*
**作者**：J. B. Cooper et al.
**摘要**：利用X射线晶体学解析了重组大肠杆菌PNP与过渡态类似物的复合物结构，揭示了其催化机制中的关键氨基酸残基，为设计PNP抑制剂奠定了结构基础。
3. **文献名称**：*Biochemical properties of a thermostable recombinant purine nucleoside phosphorylase from Archaea*
**作者**：K. Watanabe et al.
**摘要**：从古菌中克隆PNP基因并在大肠杆菌中重组表达，纯化的蛋白表现出高热稳定性和耐碱性，拓展了PNP在工业生物催化中的应用潜力。
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以上研究涵盖了重组PNP的表达优化、结构解析及工程化应用，可作为相关领域的参考。如需具体文献年份或期刊信息，可进一步补充关键词进行检索。
Purine nucleoside phosphorylase (PNP) is a key enzyme in the purine salvage pathway, catalyzing the reversible phosphorolysis of purine nucleosides (e.g., inosine, deoxyinosine) into their corresponding bases and ribose-1-phosphate or deoxyribose-1-phosphate. This process is critical for maintaining cellular nucleotide pools and energy homeostasis. PNP deficiency in humans leads to severe T-cell dysfunction and immunodeficiency, highlighting its essential role in immune system regulation.
Recombinant PNP proteins are engineered versions of this enzyme produced via genetic engineering in heterologous expression systems such as *E. coli*, yeast, or mammalian cells. These systems enable large-scale production of highly pure, bioactive PNP for research and therapeutic applications. Structurally, PNP functions as a homotrimer, and recombinant variants often retain this quaternary configuration to ensure enzymatic activity.
Therapeutic interest in recombinant PNP stems from its potential in enzyme replacement therapy for PNP-deficient patients and as a prodrug-converting agent in cancer treatment. For example, PNP can activate chemotherapeutic prodrugs like fludarabine phosphate by cleaving them into cytotoxic metabolites, selectively targeting cancer cells. Additionally, recombinant PNP serves as a tool in biochemical studies to investigate enzyme kinetics, substrate specificity, and mechanisms of inherited metabolic disorders.
Recent advancements focus on engineering PNP mutants with enhanced stability, altered substrate preferences, or reduced immunogenicity for improved clinical use. Its role in nucleotide metabolism also makes it a target for drug development in autoimmune diseases and viral infections. Overall, recombinant PNP bridges fundamental biochemistry with translational medicine, offering insights into cellular metabolism and novel treatment strategies.
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