| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ODC |
| Uniprot No | P11926 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-461aa |
| 氨基酸序列 | MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQFQNPDFPPEVEEQDASTLPVSCAWESGMKRHRAACASASINV |
| 预测分子量 | 71.1 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ODC(鸟氨酸脱羧酶)重组蛋白研究的3篇代表性文献示例(注：以下文献信息为示例性质，具体内容需根据实际文献调整)：
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1. **文献名称**: "Expression and Purification of Recombinant Human Ornithine Decarboxylase in E. coli"
**作者**: Zhang, Y. et al.
**摘要**: 本研究报道了人源ODC基因在大肠杆菌中的高效表达及纯化策略，通过优化诱导条件和亲和层析技术获得高活性重组ODC蛋白，并验证其酶动力学特性。
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2. **文献名称**: "Structural Insights into the Regulation of ODC by Antizyme: A Cryo-EM Study"
**作者**: Thompson, R.L. & Williams, K.
**摘要**: 利用冷冻电镜技术解析了重组ODC与抗酶蛋白(Antizyme)的复合物结构，揭示了抗酶介导的ODC降解分子机制，为靶向ODC的癌症治疗提供理论依据。
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3. **文献名称**: "Role of Recombinant ODC in Polyamine Biosynthesis and Cell Proliferation"
**作者**: Gupta, S. et al.
**摘要**: 通过体外实验证明重组ODC过表达显著增加细胞内多胺水平，并促进肿瘤细胞增殖，提示ODC可能作为癌症治疗的潜在靶点。
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如需获取真实文献，建议在PubMed或Web of Science中检索关键词："recombinant ornithine decarboxylase" 或 "ODC protein expression"。
Ornithine decarboxylase (ODC) is a pivotal enzyme in polyamine biosynthesis, catalyzing the decarboxylation of ornithine to produce putrescine, a precursor for spermidine and spermine. These polyamines are essential for cell growth, proliferation, and differentiation, influencing processes like DNA stabilization, protein synthesis, and stress response. Dysregulation of ODC activity is linked to pathological conditions, including cancer, neurodegenerative disorders, and parasitic infections, making it a target for therapeutic intervention.
Recombinant ODC proteins are engineered using genetic engineering techniques, where the ODC gene is cloned into expression vectors (e.g., E. coli, yeast, or mammalian systems) to produce purified enzyme variants. This approach allows precise control over protein production, enabling studies on ODC structure, kinetics, and regulatory mechanisms. Recombinant ODC retains catalytic activity and interaction capabilities, facilitating research into its allosteric regulation by antizyme proteins or post-translational modifications.
The development of recombinant ODC has advanced drug discovery, particularly for cancers and tropical diseases like African sleeping sickness. Inhibitors such as α-difluoromethylornithine (DFMO), which targets ODC, exemplify its therapeutic relevance. Additionally, recombinant ODC serves as a tool in diagnostic assays and agricultural biotechnology to modulate polyamine levels in crops for stress resilience.
Structural studies using recombinant ODC have elucidated its pyridoxal phosphate-dependent mechanism and dimeric architecture, providing insights for rational inhibitor design. Despite progress, challenges remain in understanding tissue-specific regulation and ODC’s role in cellular homeostasis. Ongoing research leverages recombinant protein technology to explore these complexities, underscoring ODC’s dual significance as a biochemical catalyst and a biomedical target.
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