| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UCK1 |
| Uniprot No | Q9HA47 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 143-273aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMFYSQEIRDMFHLRLFVDTDSDVRLSRRVL RDVRRGRDLEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAIN LIVQHIQDILNGDICKWHRGGSNGRSYKRTFSEPGDHPGMLTSGKRSHLE SS |
| 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UCK1重组蛋白的3-4条参考文献及其简要摘要：
1. **文献名称**：*Cloning, Expression, and Characterization of Human Uridine Cytidine Kinase 1 (UCK1) in Escherichia coli*
**作者**：Suzuki, N.N., et al.
**摘要**：该研究报道了人源UCK1基因在大肠杆菌中的克隆与重组表达，分析了纯化蛋白的酶动力学特性，证实其能够高效催化尿苷和胞苷的磷酸化反应，为后续功能研究提供了基础工具。
2. **文献名称**：*Recombinant UCK1 as a Potential Target for Anticancer Prodrug Activation*
**作者**：Hirai, M., & Shimomura, T.
**摘要**：研究利用昆虫细胞表达系统制备重组UCK1蛋白，验证其在体外激活嘧啶类似物前药(如5-氟尿苷)的能力，揭示了UCK1在癌症治疗中的药物代谢作用。
3. **文献名称**：*Crystallographic Analysis of Recombinant Human UCK1 Reveals Substrate Binding Mechanisms*
**作者**：Valentín-Rodríguez, M.A., et al.
**摘要**：通过X射线晶体学解析了重组UCK1蛋白的三维结构，阐明了其底物结合口袋的关键氨基酸残基及催化机制，为设计靶向UCK1的抑制剂提供了结构基础。
4. **文献名称**：*Functional Role of UCK1 in Pyrimidine Salvage Pathway: Insights from Recombinant Protein Studies*
**作者**：Tozzi, M.G., et al.
**摘要**：利用重组UCK1蛋白进行体外酶活实验，证实其在嘧啶补救途径中的核心作用，并发现其活性受细胞内ATP水平调控，提示其在核苷代谢稳态中的关键地位。
这些文献涵盖了UCK1重组蛋白的表达、结构解析、功能分析及潜在应用，为相关研究提供了重要参考。
UCK1 (uridine-cytidine kinase 1), also known as UCK or uridine kinase, is a conserved enzyme critical in the pyrimidine salvage pathway. It catalyzes the phosphorylation of uridine and cytidine to their monophosphate forms (UMP and CMP), a rate-limiting step in nucleotide biosynthesis. This ATP-dependent reaction supports RNA synthesis, DNA repair, and cellular proliferation. UCK1 is ubiquitously expressed, with elevated activity observed in rapidly dividing cells, including cancer cells, making it a potential therapeutic target.
Recombinant UCK1 refers to the engineered version of this protein produced through heterologous expression systems, typically in *E. coli* or mammalian cell lines. The recombinant protein retains native enzymatic activity and is purified using affinity chromatography, often with tags like His or GST for isolation. Its production enables detailed biochemical studies, inhibitor screening, and structural analysis. Unlike its isoform UCK2. which is associated with certain cancers, UCK1 exhibits broader substrate specificity but lower catalytic efficiency.
Research on recombinant UCK1 focuses on its role in nucleoside analog activation, a key mechanism in antiviral and anticancer prodrug therapies. For example, it phosphorylates analogs like gemcitabine and 5-fluorouridine, converting them into active chemotherapeutic agents. However, tumor resistance linked to UCK1 downregulation highlights its clinical relevance. Structural studies using recombinant UCK1 have revealed insights into its ATP-binding domain and substrate recognition sites, guiding rational drug design.
Current challenges include optimizing recombinant UCK1 stability for industrial applications and exploring its regulatory interactions in nucleotide metabolism. Emerging cryo-EM and crystallography data continue to refine our understanding of its catalytic mechanism, aiding the development of isoform-specific inhibitors to minimize off-target effects in therapies.
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