| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TDO |
| Uniprot No | P48775 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-406aa |
| 氨基酸序列 | MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEK VLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNG HVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTALDFNDFREYLSPA SGFQSLQFRLLENKIGVLQNMRVPYNRRHYRDNFKGEENELLLKSEQEKT LLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIRIQAKEESEEK EEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYRE EPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGSSGYHY LRSTVSDRYKVFVDLFNLSTYLIPRHWIPKMNPTIHKFLYTAEYCDSSYF SSDESD |
| 预测分子量 | 48 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3篇关于TDO(色氨酸2.3-双加氧酶)重组蛋白的文献摘要概括(内容基于模拟文献，仅供参考)：
---
1. **文献名称**: "Recombinant Human Tryptophan 2.3-Dioxygenase: Expression, Purification, and Structural Characterization"
**作者**: Smith J, et al.
**摘要**: 本研究报道了人源TDO重组蛋白在大肠杆菌中的高效表达与纯化方法，通过X射线晶体学解析了其三维结构，揭示了底物结合位点的关键氨基酸残基。
2. **文献名称**: "Functional Analysis of Recombinant TDO in Cancer-Associated Immune Suppression"
**作者**: Chen L, et al.
**摘要**: 通过体外表达重组TDO蛋白，研究证明其催化色氨酸降解的能力可抑制T细胞活性，提示TDO在肿瘤微环境中的免疫逃逸机制及潜在治疗靶点。
3. **文献名称**: "Enzymatic Properties of Recombinant TDO from Drosophila melanogaster"
**作者**: Tanaka K, et al.
**摘要**: 利用昆虫细胞系统表达果蝇来源的TDO重组蛋白，分析了其酶动力学参数及血红素辅因子的依赖性，为比较进化生物学研究提供数据支持。
---
(注：以上文献为示例性内容，实际文献需通过PubMed、Web of Science等数据库检索。)
Tryptophan 2.3-dioxygenase (TDO), a heme-containing enzyme, plays a critical role in the kynurenine pathway by catalyzing the oxidative cleavage of tryptophan into N-formylkynurenine. This reaction represents the first and rate-limiting step in tryptophan catabolism, linking amino acid metabolism to immune regulation, neurological function, and cancer biology. TDO is primarily expressed in the liver but has gained significant attention for its extrahepatic expression in tumors and immune cells, where it contributes to immunosuppressive microenvironments by depleting local tryptophan and accumulating immunosuppressive metabolites.
The development of recombinant TDO proteins emerged as a pivotal tool for studying its biochemical properties and therapeutic potential. Produced through heterologous expression systems (e.g., E. coli or mammalian cells), recombinant TDO retains enzymatic activity while enabling scalable purification. This technology has facilitated structural studies, including crystallographic analyses that revealed substrate-binding mechanisms and allosteric regulation sites.
Pharmaceutically, TDO inhibitors are being explored as immunomodulators for cancer therapy, necessitating recombinant proteins for high-throughput drug screening. Additionally, recombinant TDO serves as a biomarker in research linking tryptophan metabolism to depression, neurodegenerative diseases, and inflammatory disorders. Recent advances in protein engineering have improved stability and solubility, addressing challenges in handling this oxygen-sensitive enzyme. Current research focuses on isoform-specific functions and tissue-specific roles, with recombinant variants enabling precise mechanistic studies across disease models.
×
