| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IYD |
| Uniprot No | Q6PHW0-3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-214aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSDRSMEKKKGEPRTRAEARPWVDEDLKD SSDLHQAEEDADEWQESEENVEHIPFSHNHYPEKEMVKRSQEFYELLNKR RSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIR KIIEEEEEINYMKRMGHRWVTDLKKLRTNWIKEYLDTAPILILIFKQVHG FAANGKKKVH YYNE |
| 预测分子量 | 25 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IYD(碘酪氨酸脱碘酶)重组蛋白的参考文献示例，涵盖结构、功能及表达研究：
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1. **文献名称**：*Crystal Structure of Human Iodotyrosine Deiodinase Reveals Catalytic Mechanism*
**作者**：McTamney PM, Rokita SE
**摘要**：该研究通过X射线晶体学解析了人源IYD的晶体结构，揭示了其底物结合位点及催化机制。重组蛋白在大肠杆菌中表达并纯化，实验证实了黄素辅因子在脱碘反应中的关键作用，为甲状腺激素代谢异常疾病的药物设计提供了结构基础。
2. **文献名称**：*Heterologous Expression and Characterization of Recombinant IYD in Mammalian Cells*
**作者**：Schiffmann S, et al.
**摘要**：本研究在哺乳动物细胞系(HEK293)中成功表达重组IYD蛋白，并通过酶活测定验证其功能。结果显示，重组IYD能够高效催化单碘酪氨酸的脱碘反应，且其活性依赖还原型黄素腺嘌呤二核苷酸(FADH₂)，为体外酶活性分析提供了可靠方法。
3. **文献名称**：*Engineering Thermostable IYD Variants for Industrial Applications*
**作者**：Lee JH, Kim D, Park C
**摘要**：通过定向进化技术改造IYD，获得热稳定性显著提高的重组突变体。突变酶在60℃下仍保留80%活性，适用于高温环境下的工业催化过程，如含碘废水处理或药物中间体合成，展现了其生物技术应用潜力。
4. **文献名称**：*Functional Role of Conserved Residues in Recombinant Mouse IYD*
**作者**：Thomas J, et al.
**摘要**：通过定点突变分析小鼠重组IYD的保守氨基酸，发现His220和Arg114对底物结合及催化不可或缺。研究结合动力学实验与分子模拟，阐明了这些残基在维持酶活性中的具体作用机制。
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**注**：以上文献为示例性内容，实际引用时建议通过PubMed、Web of Science等数据库检索最新且经同行评议的研究，并核对作者、期刊及摘要准确性。
**Background of Recombinant IYD Protein**
Iodotyrosine deiodinase (IYD), also known as *dehalogenase 1*, is a key enzyme involved in thyroid hormone metabolism. It catalyzes the reductive deiodination of mono- and di-iodotyrosines (MIT, DIT), recycling iodide from degraded thyroid hormones to maintain iodine homeostasis—a critical process for synthesizing thyroxine (T4) and triiodothyronine (T3), which regulate metabolism, growth, and development. Mutations in the *IYD* gene are linked to congenital hypothyroidism and iodine deficiency disorders, highlighting its physiological significance.
Recombinant IYD protein is produced using genetic engineering techniques, where the *IYD* gene is cloned into expression vectors and expressed in heterologous systems like *E. coli*, yeast, or mammalian cells (e.g., CHO or HEK293). This approach allows large-scale production of purified, functional IYD for research and therapeutic applications. Structural studies of recombinant IYD have revealed its dependency on flavin adenine dinucleotide (FAD) as a cofactor and its unique mechanism of substrate recognition, involving a conserved nitroreductase fold.
The development of recombinant IYD holds promise for multiple applications. It serves as a tool to study thyroid hormone dysregulation and screen potential drugs for iodine metabolism disorders. Additionally, recombinant IYD could be engineered for bioremediation to degrade iodinated pollutants or act as a biosensor in diagnostic assays. Challenges remain in optimizing its stability and activity *in vitro*, but advances in protein engineering and structural biology continue to refine its functional characterization. Overall, recombinant IYD bridges basic research and translational medicine, offering insights into thyroid physiology and novel therapeutic strategies.
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