| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | deoD |
| Uniprot No | P0ABP8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-239aa |
| 氨基酸序列 | ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDKE |
| 预测分子量 | 52.8 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. |
以下是关于deoD重组蛋白的3篇参考文献，按文献名称、作者及摘要内容简要概括：
---
1. **文献名称**：*Cloning and Expression of the deoD Gene Encoding Purine Nucleoside Phosphorylase in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：该研究报道了从大肠杆菌中克隆deoD基因，并在重组系统中高效表达其编码的嘌呤核苷磷酸化酶(PNP)。通过体外酶活实验证实，重组蛋白具有催化肌苷分解为次黄嘌呤的活性，为后续酶学性质研究奠定基础。
2. **文献名称**：*Structural Characterization of Recombinant DeoD Protein from Bacillus subtilis*
**作者**：Zhang L, et al.
**摘要**：本文解析了枯草芽孢杆菌来源的deoD重组蛋白的晶体结构，揭示了其底物结合口袋的关键氨基酸残基。通过定点突变实验，证实了某些残基对酶催化效率的调控作用，为理性改造PNP提供了结构基础。
3. **文献名称**：*Application of Recombinant DeoD in the Biosynthesis of Antiviral Nucleoside Analogs*
**作者**：Kim H, et al.
**摘要**：研究利用重组deoD蛋白的转糖基活性，开发了一种新型酶法合成抗病毒核苷类似物(如阿昔洛韦)的工艺。与化学合成法相比，该生物催化途径显著提高了产物立体选择性和产率。
---
**注**：以上文献信息为模拟示例，实际文献需通过数据库(如PubMed、Web of Science)检索确认。建议结合具体研究方向补充关键词(如物种、应用场景)进一步筛选。
**Background of deoD Recombinant Protein**
The deoD gene encodes purine nucleoside phosphorylase (PNP), an enzyme critical in the salvage pathway of purine metabolism. It catalyzes the reversible phosphorolysis of purine nucleosides (e.g., inosine, guanosine) to generate free bases and ribose-1-phosphate, enabling nucleotide recycling. In humans, PNP deficiency is linked to severe T-cell immunodeficiency, underscoring its role in immune function. The *deoD* homolog in *Escherichia coli* has been extensively studied as a model system to understand PNP structure, kinetics, and substrate specificity.
Recombinant deoD protein is produced via heterologous expression in bacterial (e.g., *E. coli*) or eukaryotic systems, enabling high-yield purification for research and therapeutic applications. Its structure, resolved via X-ray crystallography, reveals a homo-trimeric quaternary arrangement with conserved active-site residues critical for catalysis. Studies on recombinant deoD have elucidated mechanisms of enzyme inhibition, aiding drug development for pathologies like cancers or autoimmune disorders, where PNP modulation is therapeutic.
In biotechnology, deoD recombinant protein serves as a tool for nucleoside analog activation in prodrug therapies and as a biomarker in metabolic studies. Its stability and catalytic efficiency also make it valuable for industrial biocatalysis. Research continues to explore engineered variants with enhanced properties, reflecting its versatility in both basic science and applied medicine.
×
