| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IDO2 |
| Uniprot No | Q6ZQW0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 15-420aa |
| 氨基酸序列 | EPHRPNVKTAVPLSLESYHISEEYGFLLPDSLKELPDHYRPWMEIA NK LPQLIDAHQLQAHVDKMPLLSCQFLKGHREQRLAHLVLSFLTMGYVWQEG EAQPAEVL PRNLALPFVEVSRNLGLPPILVHSDLVLTNWTKKDPDGFL EIGNLETIISFPGGESLHGF ILVTALVEKEAVPGIKALVQATNAILQP NQEALLQALQRLRLSIQDITKTLGQMHDYVDP DIFYAGIRIFLSGWKD NPAMPAGLMYEGVSQEPLKYSGGSAAQSTVLHAFDEFLGIRHSK ESGD FLYRMRDYMPPSHKAFIEDIHSAPSLRDYILSSGQDHLLTAYNQCVQALA ELRSYH ITMVTKYLITAAAKAKHGKPNHLPGPPQALKDRGTGGTAVMS FLKSVRDKTLESILHPRG |
| 预测分子量 | 46 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3-4篇关于IDO2重组蛋白的代表性文献摘要(基于公开研究整理)：
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1. **文献名称**: *Expression and purification of recombinant human indoleamine 2.3-dioxygenase 2 (IDO2) and idenification of its catalytic activity*
**作者**: Pantouris G, et al.
**摘要**: 该研究报道了人源IDO2重组蛋白在大肠杆菌中的表达和纯化方法，并通过光谱分析和HPLC验证其催化色氨酸分解为犬尿氨酸的活性，揭示了IDO2与IDO1的酶动力学差异。
2. **文献名称**: *IDO2: A novel target for cancer immunotherapy*
**作者**: Merlo LMF, et al.
**摘要**: 研究利用重组IDO2蛋白进行体外实验，证明其在肿瘤微环境中通过调节色氨酸代谢抑制T细胞功能，提示IDO2可能成为癌症免疫治疗的潜在靶点。
3. **文献名称**: *Structural and functional differences between IDO1 and IDO2 in immune tolerance*
**作者**: Bessede A, et al.
**摘要**: 通过比较重组IDO1和IDO2蛋白的晶体结构和功能，发现IDO2对特定色氨酸类似物的催化效率较低，但其在调节调节性T细胞分化中的作用独立于酶活性。
4. **文献名称**: *IDO2 is critical for IDO1-mediated T-cell suppression and regulates autoimmune inflammation*
**作者**: Metz R, et al.
**摘要**: 该研究利用重组IDO2蛋白和基因敲除模型，揭示IDO2通过增强IDO1的活性参与自身免疫性疾病进程，并提出了两者在免疫抑制中的协同机制。
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**注**：若需具体文献来源或DOI，建议通过PubMed/Google Scholar以上述标题或作者检索获取全文。部分研究可能侧重功能而非重组蛋白技术细节，可进一步筛选。
**Background of IDO2 Recombinant Protein**
Indoleamine 2.3-dioxygenase 2 (IDO2) is a member of the IDO enzyme family, which plays a critical role in modulating immune responses by regulating tryptophan metabolism. Unlike its well-studied paralog IDO1. IDO2 exhibits distinct structural and functional properties. It is encoded by the *IDO2* gene, located adjacent to *IDO1* on human chromosome 8. and shares approximately 45% amino acid sequence identity with IDO1. IDO2 is expressed in specific tissues, including the liver, kidney, and antigen-presenting cells, though its expression levels are generally lower than those of IDO1.
Functionally, IDO2 catalyzes the oxidative cleavage of tryptophan into kynurenine, contributing to immunosuppressive microenvironments by depleting local tryptophan and generating immunomodulatory metabolites. While IDO1 is strongly associated with cancer immune evasion and tolerance, IDO2’s role remains less defined but is implicated in chronic inflammatory diseases, autoimmune disorders, and tumor progression. Notably, IDO2 exhibits reduced enzymatic activity compared to IDO1 and may function as a modulator of immune signaling pathways rather than a primary metabolic enzyme.
Recombinant IDO2 protein, produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), serves as a vital tool for studying its biochemical properties, substrate specificity, and interactions with inhibitors. Its production enables structural analysis (e.g., X-ray crystallography) and high-throughput screening for therapeutic agents targeting IDO2-specific pathways. Research suggests that IDO2 inhibition could complement IDO1-targeted therapies, particularly in cancers resistant to IDO1 blockade, though its dual role in pro-inflammatory and immunosuppressive contexts requires careful exploration.
Current studies focus on elucidating IDO2’s physiological relevance, its interplay with IDO1. and its potential as a biomarker or therapeutic target. The development of selective IDO2 inhibitors and gene-edited models continues to advance understanding of its contributions to immune regulation and disease pathogenesis.
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