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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NGF |
| Uniprot No | P01138 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 122-241aa |
| 氨基酸序列 | SSSHPIFHRG EFSVCDSVSV WVGDKTTATD IKGKEVMVLG EVNINNSVFK QYFFETKCRD PNPVDSGCRG IDSKHWNSYC TTTHTFVKAL TMDGKQAAWR FIRIDTACVC VLSRKAVRRA SSSHPIFHRG EFSVCDSVSV WVGDKTTATD IKGKEVMVLG EVNINNSVFK QYFFETKCRD PNPVDSGCRG IDSKHWNSYC TTTHTFVKAL TMDGKQAAWR FIRIDTACVC VLSRKAVRRA |
| 预测分子量 | 27 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NGF重组蛋白的3篇代表性文献示例(内容为模拟概括，仅供参考)：
1. **《Expression and purification of recombinant human nerve growth factor in Escherichia coli》**
- 作者：Smith A, et al.
- 摘要：研究通过大肠杆菌表达系统生产重组人NGF，优化了诱导条件并采用亲和层析纯化，验证了重组蛋白的生物活性，为大规模生产提供了方法。
2. **《Recombinant human NGF accelerates corneal epithelial wound healing in vivo》**
- 作者：Lee C, et al.
- 摘要：通过动物实验证明，重组人NGF滴眼液能显著促进角膜上皮损伤修复，机制涉及细胞增殖和抗炎作用，提示其治疗角膜疾病的潜力。
3. **《Structural and functional characterization of a novel NGF variant produced in mammalian cells》**
- 作者：Zhang Y, et al.
- 摘要：利用哺乳动物细胞表达系统生产高纯度重组NGF变体，通过晶体结构和体外神经元培养验证其与天然NGF相似的构象和促神经生长功能。
**提示**：实际文献需通过PubMed、Web of Science等平台检索，建议结合关键词“recombinant NGF protein”+“expression/therapy/structure”查找最新研究。
Nerve Growth Factor (NGF), first discovered in the 1950s by Rita Levi-Montalcini and Stanley Cohen, is a neurotrophic protein essential for the development, survival, and function of neurons. As a member of the neurotrophin family, NGF binds to two receptors: the high-affinity TrkA tyrosine kinase receptor and the low-affinity p75 neurotrophin receptor. It plays a critical role in the growth and maintenance of sensory and sympathetic neurons, as well as in regulating synaptic plasticity and inflammatory responses.
Recombinant NGF (rhNGF) is produced using genetic engineering techniques, typically by expressing the human NGF gene in bacterial, yeast, or mammalian cell systems. Mammalian systems (e.g., CHO cells) are preferred for generating glycosylated, bioactive forms. The recombinant protein retains the biological activity of native NGF, enabling its use in research and therapeutic applications.
In biomedical research, rhNGF is employed to study neurodevelopmental processes, neurodegenerative diseases (e.g., Alzheimer’s), and nerve injury repair mechanisms. Therapeutically, it has been explored for treating neuropathies, corneal ulcers, and glaucoma. Notably, rhNGF-based eye drops (e.g., cenegermin) were approved in 2018 for neurotrophic keratitis, marking a milestone in clinical translation.
Despite its potential, challenges remain. NGF’s dual role in promoting both neuronal survival and pain signaling complicates therapeutic targeting. Additionally, delivery barriers (e.g., blood-brain penetration) and side effects (e.g., hyperalgesia) limit systemic applications. Ongoing research focuses on engineered variants, localized delivery systems, and combination therapies to enhance efficacy and safety.
Overall, rhNGF represents a pivotal tool in neuroscience and a promising candidate for addressing unmet needs in neurology and regenerative medicine.
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