| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IDO |
| Uniprot No | P14902 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-403aa |
| 氨基酸序列 | MAHAMENSWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG |
| 预测分子量 | 49.3kDa |
| 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IDO(吲哚胺2.3-双加氧酶)重组蛋白研究的参考文献摘要：
1. **文献名称**：*"Expression and Purification of Recombinant Human Indoleamine 2.3-Dioxygenase (IDO) for Structural Studies"*
**作者**：Smith A, et al.
**摘要**：研究报道了人源IDO蛋白在大肠杆菌中的高效表达与纯化方法，通过优化表达条件获得可溶性重组IDO，并利用X射线晶体学解析其三维结构，为后续抑制剂开发奠定基础。
2. **文献名称**：*"Functional Characterization of Recombinant IDO1 in Cancer Immunotherapy"*
**作者**：Li Y, Wang H.
**摘要**：通过哺乳动物细胞表达系统制备功能性IDO1重组蛋白，验证其催化色氨酸代谢的活性，并证明其在肿瘤微环境中抑制T细胞功能的机制，为免疫检查点疗法提供实验依据。
3. **文献名称**：*"Engineering a Thermostable IDO Variant for High-Throughput Inhibitor Screening"*
**作者**：Zhang Q, et al.
**摘要**：通过定向进化技术改造IDO蛋白，获得热稳定性增强的重组突变体，适用于高通量筛选平台，显著提高了IDO抑制剂的筛选效率及药物开发成功率。
注：以上文献信息为示例性概括，具体研究需以实际发表的论文为准。建议通过PubMed或Web of Science检索关键词“IDO1 recombinant”“IDO protein expression”获取最新文献。
Indoleamine 2.3-dioxygenase (IDO) is a heme-containing enzyme that catalyzes the rate-limiting step in the degradation of tryptophan along the kynurenine pathway. Initially identified in the 1960s, IDO gained significant attention in the 2000s for its role in immune regulation. It is expressed in various tissues, particularly in antigen-presenting cells, and is strongly induced by inflammatory signals like interferon-gamma (IFN-γ). By depleting local tryptophan and generating immunomodulatory metabolites (e.g., kynurenine), IDO suppresses T-cell activation and promotes regulatory T-cell differentiation, creating an immunosuppressive microenvironment. This mechanism is critical in physiological processes like maternal-fetal tolerance but is hijacked by tumors to evade immune surveillance.
Recombinant IDO proteins are produced using genetic engineering techniques, typically expressed in bacterial (e.g., *E. coli*) or mammalian cell systems to ensure proper folding and enzymatic activity. These proteins retain the functional domains necessary for binding tryptophan and molecular oxygen, enabling researchers to study IDO's structure-function relationships, screen inhibitors, or develop diagnostic tools. Purification processes often involve affinity chromatography and quality validation through enzymatic assays or mass spectrometry.
The therapeutic relevance of IDO surged with the discovery that cancer cells overexpress IDO to dampen anti-tumor immunity. Preclinical studies showed that IDO inhibitors could enhance the efficacy of chemotherapy and immune checkpoint therapies. However, clinical trials of early IDO inhibitors yielded mixed results, prompting deeper investigations into IDO's complex biology, including its isoforms (IDO1 and IDO2) and interactions with other immune checkpoints. Today, recombinant IDO proteins remain vital tools for elucidating metabolic immunosuppression mechanisms and refining cancer immunotherapies, as well as exploring roles in neurodegenerative diseases and chronic inflammation.
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