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| 纯度 | >97%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NT4 |
| 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NT4(神经营养因子4)重组蛋白的3篇参考文献示例(注：文献信息为模拟示例，非真实存在)：
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1. **文献名称**：Expression and Purification of Recombinant Neurotrophin-4 in Escherichia coli
**作者**：Zhang L, Wang H, et al.
**摘要**：本研究利用大肠杆菌表达系统成功表达了具有生物活性的重组NT4蛋白，通过优化诱导条件和亲和层析纯化策略，获得了高纯度蛋白。体外细胞实验证实纯化的NT4能显著促进神经元轴突生长。
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2. **文献名称**：Structural and Functional Analysis of Recombinant NT4/5 Chimeric Protein
**作者**：Martinez R, Gomez-Perez A.
**摘要**：作者构建了NT4与神经营养因子5(NT5)的嵌合重组蛋白，通过X射线晶体学解析其三维结构，并证明该嵌合体在小鼠模型中增强了神经保护作用，为神经退行性疾病治疗提供新思路。
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3. **文献名称**：Large-scale Production of Recombinant Human NT4 in Mammalian Cell Culture
**作者**：Kim S, Lee J, et al.
**摘要**：开发了一种基于HEK293细胞的重组人NT4大规模生产工艺，采用无血清培养基和连续灌流技术，显著提高蛋白产量。纯化后的NT4通过了体外活性检测和体内安全性评估，适用于临床前研究。
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(注：如需真实文献，建议通过PubMed或Google Scholar检索关键词“Recombinant Neurotrophin-4”或“NT4 expression”获取。)
**Background of NT4 Recombinant Protein**
Neurotrophin-4 (NT4), also known as neurotrophin-5 (NT5) in some species, is a member of the neurotrophin family, a group of structurally related proteins critical for neuronal survival, development, and plasticity. Discovered in the early 1990s, NT4 shares functional and structural similarities with other neurotrophins, such as nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), and neurotrophin-3 (NT3). These proteins bind to specific tyrosine kinase (Trk) receptors and the p75 neurotrophin receptor, activating downstream signaling pathways that regulate neuronal maintenance, axonal growth, and synaptic connectivity.
Recombinant NT4 is produced using genetic engineering techniques, typically through expression in bacterial (e.g., *E. coli*) or mammalian cell systems. The recombinant form allows for high-purity, scalable production, bypassing challenges associated with isolating the protein from natural sources. Its production often involves cloning the NT4 gene into expression vectors, followed by purification steps like affinity chromatography to ensure biological activity.
NT4 has garnered interest in neuroscience research, particularly for its role in supporting sensory and sympathetic neurons. Studies suggest its potential therapeutic applications in neurodegenerative diseases, nerve injury repair, and conditions like glaucoma or hearing loss. Additionally, recombinant NT4 serves as a tool to investigate neurotrophin signaling mechanisms and their crosstalk with other growth factors.
Despite its lower abundance compared to BDNF or NGF, NT4's unique receptor interactions and tissue-specific effects highlight its importance in the neurotrophin network. Ongoing research aims to clarify its distinct physiological roles and harness its recombinant form for experimental or clinical use.
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