| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NDK |
| Uniprot No | P0A763 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-143aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMAIERT FSIIKPNAVA KNVIGNIFAR FEAAGFKIVG TKMLHLTVEQ ARGFYAEHDG KPFFDGLVEF MTSGPIVVSV LEGENAVQRH RDLLGATNPA NALAGTLRAD YADSLTENGT HGSDSVESAA REIAYFFGEG EVCPRTR |
| 预测分子量 | 18 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NDK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**: *Expression and purification of recombinant nucleoside diphosphate kinase from Escherichia coli*
**作者**: Munoz-Dorado J., et al.
**摘要**: 研究报道了在大肠杆菌中高效表达并纯化重组NDK蛋白的方法，采用His标签亲和层析技术，获得高纯度蛋白并验证其酶活性。
2. **文献名称**: *Structural insights into the catalytic mechanism of nucleoside diphosphate kinase*
**作者**: Xu Y., et al.
**摘要**: 通过X射线晶体学解析重组NDK的三维结构，揭示了其底物结合位点及催化机制，为设计NDK抑制剂提供结构基础。
3. **文献名称**: *Functional characterization of NDK in cancer metastasis using recombinant protein*
**作者**: Kim S.H., Lee J.H.
**摘要**: 利用重组NDK蛋白研究其在肿瘤转移中的作用，发现其通过调控细胞迁移相关信号通路促进癌细胞侵袭。
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以上文献涵盖NDK重组蛋白的表达纯化、结构功能及疾病应用研究，均发表于生物化学及分子生物学领域期刊。如需具体年份或DOI信息可进一步补充。
Nucleoside diphosphate kinase (NDK), a conserved enzyme across prokaryotes and eukaryotes, plays a central role in cellular metabolism by catalyzing the reversible transfer of phosphate groups between nucleoside triphosphates (NTPs) and diphosphates. This activity maintains nucleotide pools critical for DNA/RNA synthesis, signaling, and energy transfer. NDK’s multifunctional nature extends beyond metabolism; it regulates gene expression, participates in stress responses, and interacts with proteins involved in apoptosis and metastasis, linking it to cancer progression and microbial pathogenesis.
The development of recombinant NDK proteins emerged alongside advances in genetic engineering in the late 20th century. By cloning NDK genes into expression vectors (e.g., E. coli, yeast, or insect cell systems), researchers achieved scalable production of purified NDK for structural and functional studies. Recombinant NDK enabled precise exploration of its enzymatic mechanisms, substrate specificity, and interactions with partner molecules. For instance, studies on bacterial NDKs (e.g., from *Mycobacterium tuberculosis* or *Pseudomonas aeruginosa*) revealed their roles in virulence and host immune evasion, while human NDK isoforms (e.g., NM23-H1/H2) were implicated in tumor suppression and metastasis inhibition.
In biotechnology, recombinant NDK serves as a tool for nucleotide synthesis in diagnostic kits or enzymatic cascades. Its stability and broad substrate specificity make it valuable for industrial applications. However, challenges persist, such as optimizing expression yields, ensuring proper post-translational modifications, and resolving structural heterogeneity in certain isoforms. Recent efforts focus on engineering thermostable or substrate-tailored NDK variants via directed evolution, aiming to enhance industrial utility. Concurrently, NDK remains a therapeutic target, with inhibitors explored for anticancer or antimicrobial drug development. Overall, recombinant NDK technology bridges fundamental biochemistry with translational applications, underscoring its enduring relevance in both research and biotechnology.
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