| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CDO1 |
| Uniprot No | Q16878 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-200aa |
| 氨基酸序列 | MEQTEVLKPRTLADLIRILHQLFAGDEVNVEEVQAIMEAYESDPTEWAMY AKFDQYRYTRNLVDQGNGKFNLMILCWGEGHGSSIHDHTNSHCFLKMLQG NLKETLFAWPDKKSNEMVKKSERVLRENQCAYINDSIGLHRVENISHTEP AVSLHLYSPPFDTCHAFDQRTGHKNKVTMTFHSKFGIRTPNATSGSLENN |
| 预测分子量 | 23 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CDO1重组蛋白的3篇示例参考文献(注：文献为示例性概括，实际文献需通过学术数据库查询)：
1. **文献名称**: *"Expression and Purification of Recombinant Human Cysteine Dioxygenase (CDO1) in Escherichia coli for Structural Studies"*
**作者**: Smith J, et al.
**摘要**: 本研究报道了人源CDO1重组蛋白在大肠杆菌中的高效表达及纯化方法。通过优化表达条件及亲和层析技术获得高纯度蛋白，并利用圆二色谱分析其二级结构，为后续CDO1的酶活性和晶体结构研究奠定基础。
2. **文献名称**: *"Functional Characterization of CDO1 Recombinant Protein in Cancer Cell Metabolism"*
**作者**: Wang L, et al.
**摘要**: 通过体外重组CDO1蛋白实验，验证其在半胱氨酸代谢中的催化功能，并发现CDO1缺失导致癌细胞中硫化氢水平异常升高。研究提示CDO1作为肿瘤抑制因子的潜在机制与其重组蛋白的酶活性密切相关。
3. **文献名称**: *"Structural Insights into CDO1 Catalytic Mechanism via Site-Directed Mutagenesis of Recombinant Protein"*
**作者**: Tanaka K, et al.
**摘要**: 利用重组CDO1蛋白进行定点突变实验，结合X射线晶体学解析关键活性位点(如His157和Arg60)对催化反应的影响，揭示了CDO1在底物结合和氧活化中的分子机制。
如需实际文献，建议通过 **PubMed/Google Scholar** 检索关键词：*CDO1 recombinant protein expression*、*CDO1 structural analysis*、*CDO1 enzymatic activity*。
CDO1 (Cysteine Dioxygenase Type 1) is a metalloenzyme encoded by the *CDO1* gene, primarily involved in regulating cysteine metabolism. It catalyzes the oxidation of L-cysteine to cysteine sulfinic acid, a critical step in taurine and hypotaurine biosynthesis, while maintaining cellular redox balance by controlling cysteine levels. Dysregulation of CDO1 has been linked to oxidative stress, neurodegenerative disorders, and cancer, particularly due to its role in modulating glutathione synthesis and sulfur-containing metabolite pathways.
Recombinant CDO1 protein is engineered using heterologous expression systems, such as *E. coli* or mammalian cell lines, to produce purified, functional enzyme for research and therapeutic applications. Its production often involves codon optimization, affinity tag fusion (e.g., His-tag), and post-translational modifications to enhance stability and activity. Researchers utilize recombinant CDO1 to study its enzymatic kinetics, structural properties, and interactions with substrates/inhibitors. In cancer biology, CDO1 is recognized as a tumor suppressor; hypermethylation of its promoter silences expression in malignancies like lung, breast, and gastric cancers, making it a potential epigenetic biomarker. Recombinant CDO1 also aids in developing diagnostic assays and exploring therapeutic strategies targeting cysteine metabolism in diseases such as liver fibrosis and neurodegenerative conditions. Current challenges include optimizing its catalytic efficiency *in vitro* and understanding tissue-specific regulatory mechanisms. Overall, recombinant CDO1 serves as a vital tool for deciphering metabolic dysregulation and advancing precision medicine approaches.
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