| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ODC1 |
| 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3-4条关于 **ODC1(鸟氨酸脱羧酶1)重组蛋白** 的模拟参考文献示例(实际文献需通过学术数据库进一步检索)：
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1. **文献名称**: *"Expression and Purification of Recombinant Human Ornithine Decarboxylase (ODC1) in Escherichia coli"*
**作者**: Mäkitie, L.T. et al.
**摘要**: 研究报道了通过大肠杆菌表达系统成功克隆、表达并纯化具有生物活性的重组人ODC1蛋白，分析了其酶动力学特性及多胺合成的调控作用。
2. **文献名称**: *"Role of ODC1 in Cell Proliferation: Insights from Recombinant Protein Studies"*
**作者**: Bernacki, R.J. et al.
**摘要**: 利用重组ODC1蛋白模型，揭示了其在肿瘤细胞增殖中的关键作用，并通过抑制剂实验验证了ODC1活性与多胺水平对癌细胞生长的直接影响。
3. **文献名称**: *"Structural Analysis of Recombinant ODC1 and Its Interaction with Antizyme"*
**作者**: Pegg, A.E. et al.
**摘要**: 通过X射线晶体学解析了重组ODC1的三维结构，阐明了其与调控蛋白Antizyme的结合机制，为靶向ODC1的药物设计提供了结构基础。
4. **文献名称**: *"Recombinant ODC1 as a Therapeutic Target in Neurodegenerative Diseases"*
**作者**: López-García, C. et al.
**摘要**: 研究利用重组ODC1蛋白模型，探讨了其在神经退行性疾病中异常多胺代谢的作用，并提出抑制ODC1活性可能缓解神经元损伤的假设。
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**注意**：以上为模拟文献条目，实际引用需通过PubMed、Google Scholar等平台检索真实文献(关键词：*ODC1 recombinant protein, ornithine decarboxylase expression*)。
Ornithine decarboxylase 1 (ODC1) is a rate-limiting enzyme in the biosynthesis of polyamines, essential organic cations critical for cell proliferation, differentiation, and apoptosis. It catalyzes the decarboxylation of ornithine to produce putrescine, the precursor for higher polyamines like spermidine and spermine. ODC1 is tightly regulated at transcriptional, translational, and post-translational levels, with its activity influenced by factors such as cellular stress, growth signals, and feedback inhibition by polyamines. Dysregulation of ODC1 is linked to pathological conditions, including cancer, neurodegenerative disorders, and parasitic infections, making it a therapeutic target of interest.
Recombinant ODC1 protein is produced via heterologous expression systems (e.g., E. coli, yeast, or mammalian cells) to study its structure, function, and regulatory mechanisms. Its recombinant form enables biochemical characterization, such as enzyme kinetics, inhibitor screening, and interaction studies with regulatory proteins like antizyme or ubiquitin ligases. Structural studies using X-ray crystallography or cryo-EM have revealed details about its homodimeric architecture, active-site residues, and allosteric binding pockets, aiding in drug design. For example, inhibitors like α-difluoromethylornithine (DFMO), an irreversible ODC1 inhibitor, are explored for cancer and parasitic disease treatment.
In research, recombinant ODC1 is used to investigate polyamine metabolism’s role in cellular processes, such as tumor progression, viral replication, and immune response modulation. It also serves as a tool to develop diagnostic assays or evaluate therapeutic efficacy in preclinical models. Despite challenges in maintaining its stability during purification, advances in protein engineering and expression optimization continue to enhance its utility in both basic and applied biomedical research.
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