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| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MLN |
| Uniprot No | P12872 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-115aa |
| 氨基酸序列 | FVPIFTYGELQRMQEKERNKGQKKSLSVWQRSGEEGPVDPAEPIREEENEMIKLTAPLEIGMRMNSRQLEKYPATLEGLLSEMLPQHAAK |
| 预测分子量 | 45.5 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MLN重组蛋白的模拟参考文献示例，涵盖不同研究方向，供参考：
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1. **文献名称**：*Recombinant MLN Protein Induces Apoptosis in Cancer Cells via p53 Activation*
**作者**：Zhang S, et al.
**摘要**：本研究通过大肠杆菌表达系统制备MLN重组蛋白，发现其能显著激活p53信号通路，诱导多种肿瘤细胞凋亡，为抗癌药物开发提供潜在候选分子。
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2. **文献名称**：*Structural and Functional Analysis of MLN Recombinant Protein in Immune Regulation*
**作者**：Wang L, et al.
**摘要**：通过X射线晶体学解析MLN重组蛋白的三维结构，揭示其与T细胞表面受体的相互作用机制，实验表明该蛋白可调节Th1/Th2免疫平衡，缓解自身免疫性疾病模型小鼠症状。
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3. **文献名称**：*Optimized Expression of MLN Recombinant Protein in Insect Cells and Its Antiviral Activity*
**作者**：Kim Y, et al.
**摘要**：利用杆状病毒-昆虫细胞系统高效表达MLN重组蛋白，纯化产物显示广谱抗病毒活性，尤其对包膜病毒(如HSV-1)的入侵具有显著抑制作用。
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4. **文献名称**：*MLN Recombinant Fusion Protein Enhances Wound Healing through Angiogenesis Promotion*
**作者**：Chen X, et al.
**摘要**：构建MLN与VEGF的融合蛋白，实验证明其通过协同作用促进血管内皮细胞迁移和血管生成，显著加速糖尿病小鼠皮肤创伤修复过程。
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**说明**：以上文献为模拟示例，聚焦于MLN重组蛋白的制备、结构功能研究及在不同疾病模型中的应用。实际研究中建议通过学术数据库(如PubMed、Web of Science)以关键词“MLN recombinant protein”或结合具体研究领域进一步检索。
MLN recombinant protein refers to a class of engineered proteins designed for research and therapeutic applications, often associated with studies in cancer biology, immunology, and cellular signaling. The term "MLN" may specifically relate to proteins linked to pathways such as the mammalian target of rapamycin (mTOR), proteasome regulation, or cytokine signaling, depending on the context. These recombinant proteins are typically produced using expression systems like *E. coli*, yeast, or mammalian cells to ensure proper folding and post-translational modifications, mirroring native protein functions.
A prominent example includes MLN recombinant proteins targeting the ubiquitin-proteasome system (UPS), which plays a critical role in protein degradation and cellular homeostasis. Dysregulation of UPS components is implicated in cancers and neurodegenerative diseases, making MLN-based proteins valuable tools for studying disease mechanisms or developing inhibitors. For instance, MLN4924 (a small molecule, not a protein) is a well-known NEDD8-activating enzyme inhibitor, but recombinant proteins in this category may serve as binding partners or decoy receptors to modulate such pathways.
In oncology, MLN recombinant proteins have been explored for their ability to interfere with tumor growth by mimicking natural ligands or blocking receptor interactions. They may also act as immunomodulators, enhancing antitumor immune responses. Additionally, these proteins are used in structural biology to resolve molecular interaction sites, aiding drug design.
The development of MLN recombinant proteins often involves codon optimization, affinity tag incorporation (e.g., His-tag), and rigorous quality control to ensure bioactivity. Their applications span *in vitro* assays, animal models, and clinical trials, highlighting their versatility in bridging basic research and therapeutic innovation. Continued advancements in protein engineering and CRISPR-based editing technologies further expand their potential in precision medicine.
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