| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NT |
| Uniprot No | P34130 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 81-210aa |
| 氨基酸序列 | M+GVSETAPASRRGELAVCDAVSGWVTDRRTAVDLRGREVEVLGEVPAAG GSPLRQYFFETRCKADNAEEGGPGAGGGGCRGVDRRHWVSECKAKQSYVR ALTADAQGRVGWRWIRIDTACVCTLLSRTGRA |
| 预测分子量 | 28 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NT(神经营养因子)重组蛋白的3-4条参考文献示例(文献为模拟内容，仅供参考)：
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1. **文献名称**：*High-level expression and purification of recombinant human nerve growth factor (NGF) in Escherichia coli*
**作者**：Barde, Y. A., et al.
**摘要**：研究通过大肠杆菌表达系统高效表达重组人神经生长因子(NGF)，优化纯化工艺并验证其生物活性，证实重组NGF可促进神经元存活与分化。
2. **文献名称**：*Therapeutic potential of recombinant BDNF in a transgenic mouse model of Alzheimer’s disease*
**作者**：Tuszynski, M. H., et al.
**摘要**：探讨重组脑源性神经营养因子(BDNF)在阿尔茨海默病模型中的治疗作用，证明其能改善突触可塑性和认知功能，为临床转化提供依据。
3. **文献名称**：*Functional characterization of recombinant neurotrophin-3 (NT-3) produced in mammalian cell culture*
**作者**：Rosenthal, A., et al.
**摘要**：利用哺乳动物细胞(HEK293)系统表达重组NT-3.分析其与受体结合的特异性及促神经元生长活性，为规模化生产提供技术基础。
4. **文献名称**：*Optimization of CHO cell systems for large-scale production of bioactive neurotrophic factors*
**作者**：Huang, L., et al.
**摘要**：研究通过中国仓鼠卵巢(CHO)细胞优化重组神经营养因子的生产工艺，显著提高产量并保持蛋白稳定性，适用于工业化应用。
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**注**：以上文献为示例，实际引用时需根据具体研究方向检索真实数据库(如PubMed、Web of Science)获取权威信息。
**Background of NT Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biomedical research and therapeutic development. Among these, NT (N-terminal or nucleocapsid-tripartite) recombinant proteins represent a specialized class designed to mimic or modify specific functional domains of natural proteins, often targeting critical biological pathways. The "NT" designation typically refers to engineered constructs incorporating functional regions, such as receptor-binding domains, enzymatic active sites, or signaling motifs, optimized for stability, solubility, or enhanced interaction with cellular targets.
The development of NT recombinant proteins is rooted in advances in molecular cloning, codon optimization, and expression systems (e.g., *E. coli*, yeast, mammalian cells). These proteins are frequently utilized in therapeutics (e.g., monoclonal antibodies, cytokines), diagnostics (e.g., antigen-based assays), and vaccines (e.g., subunit vaccines targeting viral epitopes). For instance, NT-truncated spike proteins of SARS-CoV-2 were pivotal in COVID-19 vaccine design, focusing on the immunodominant N-terminal domain to elicit neutralizing antibodies.
Challenges in NT recombinant protein production include ensuring proper folding, post-translational modifications, and scalability. Innovations like cell-free systems, AI-driven protein design, and high-throughput screening have accelerated their development. Additionally, NT tags (e.g., His-tag, FLAG-tag) are often fused to facilitate purification and detection.
Beyond medicine, NT recombinant proteins are applied in agriculture (e.g., engineered enzymes for crop protection) and industrial biotechnology (e.g., biofuel production). Their versatility and specificity continue to drive breakthroughs in precision medicine and synthetic biology, underscoring their transformative role in modern science.
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