| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | FCY1 |
| Uniprot No | Q12178 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-158aa |
| 氨基酸序列 | MVTGGMASKWDQKGMDIAYEEAALGYKEGGVPIGGCLINNKDGSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGKVYKDTTLYTTLSPCDMCTGAIIMYGIPRCVVGENVNFKSKGEKYLQTRGHEVVVVDDERCKKIMKQFIDERPQDWFEDIGE |
| 预测分子量 | 25.0 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FCY1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**: *Cloning and expression of the FCY1 gene encoding cytosine deaminase from Saccharomyces cerevisiae*
**作者**: Erbs, P. et al.
**摘要**: 该研究克隆了酿酒酵母的FCY1基因，并在大肠杆菌中成功表达重组胞嘧啶脱氨酶(CD)。实验验证了重组酶对5-氟胞嘧啶(5-FC)的催化活性，为后续自杀基因疗法奠定基础。
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2. **文献名称**: *Enzymatic characterization of a recombinant yeast cytosine deaminase fused to tumor-targeting peptides*
**作者**: Kievit, E. et al.
**摘要**: 研究团队将FCY1重组蛋白与肿瘤靶向肽融合，优化其酶动力学参数，证明融合蛋白在体外可高效转化5-FC为5-FU，增强对结肠癌细胞的杀伤效果。
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3. **文献名称**: *Heterologous expression of FCY1 in lactic acid bacteria for prodrug activation therapy*
**作者**: Song, H. et al.
**摘要**: 文章报道了在乳酸菌中异源表达FCY1重组蛋白，用于激活前药5-FC。体内实验显示，该工程菌可靶向肿瘤微环境，显著抑制小鼠模型中的肿瘤生长。
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**备注**：以上文献信息为示例，实际引用需根据具体研究通过PubMed或Web of Science等平台检索原文。
The FCY1 recombinant protein is derived from the *FCY1* gene, which encodes cytosine deaminase (CDase) in *Saccharomyces cerevisiae*. This enzyme catalyzes the deamination of cytosine to uracil and 5-fluorocytosine (5-FC) to 5-fluorouracil (5-FU), playing a critical role in pyrimidine salvage pathways. Recombinant FCY1 is produced through heterologous expression in bacterial or eukaryotic systems, enabling scalable purification for research and therapeutic applications. Its ability to convert non-toxic 5-FC into the chemotherapeutic agent 5-FU has positioned it as a key component in gene-directed enzyme prodrug therapy (GDEPT) strategies, particularly in cancer treatment. In GDEPT, FCY1-expressing vectors are delivered to tumor cells, allowing localized activation of 5-FC, thereby minimizing systemic toxicity.
Structurally, FCY1 functions as a homodimer requiring zinc ions for catalytic activity. Studies have explored engineering FCY1 variants to enhance enzyme stability, substrate affinity, and efficiency under physiological conditions. Beyond oncology, FCY1 is utilized in antifungal research, as many pathogenic fungi rely on endogenous cytosine deaminase for 5-FC susceptibility. Additionally, it serves as a molecular tool in synthetic biology for metabolic engineering and nucleotide biosynthesis studies. Recent advances include its integration into biosensors and enzyme-prodrug systems combined with CRISPR/Cas9 technologies for precision medicine. Despite its broad utility, challenges remain in optimizing delivery mechanisms and minimizing off-target effects in therapeutic contexts. Overall, FCY1 recombinant protein bridges fundamental biochemistry and translational applications, underscoring its versatility in both industrial and biomedical fields.
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