| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NGB |
| Uniprot No | Q9NPG2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-151aa |
| 氨基酸序列 | MERPEPELIRQSWRAVSRSPLEHGTVLFARLFALEPDLLPLFQYNCRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVEDLSSLEEYLASLGRKHRAVGVKLSSFSTVGESLLYMLEKCLGPAFTPATRAAWSQLYGAVVQAMSRGWDGE |
| 预测分子量 | 32.9 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NGB(神经球蛋白)重组蛋白研究的参考文献示例(内容为模拟，供参考)：
1. **《Expression and Purification of Recombinant Human Neuroglobin in Escherichia coli》**
- 作者：A. Smith et al.
- 摘要：本研究报道了一种在大肠杆菌中高效表达重组人神经球蛋白(NGB)的方法，通过优化诱导条件和纯化步骤，获得高纯度蛋白，并证实其具有氧结合能力。
2. **《Neuroprotective Role of Recombinant Neuroglobin in Hypoxia-Induced Neuronal Damage》**
- 作者：B. Li & C. Wang
- 摘要：通过体外实验验证重组NGB对缺氧环境下神经元细胞的保护作用，发现其通过调节线粒体功能减少细胞凋亡，提示潜在治疗价值。
3. **《Structural Insights into Recombinant Neuroglobin Using X-ray Crystallography》**
- 作者：K. Tanaka et al.
- 摘要：利用X射线晶体学解析重组NGB的三维结构，揭示其与氧分子结合的关键氨基酸位点，为理解其神经保护机制提供结构基础。
4. **《Recombinant Neuroglobin Delivery Attenuates Oxidative Stress in Ischemic Stroke Models》**
- 作者：M. Rodriguez & J. Kim
- 摘要：在小鼠脑缺血模型中，重组NGB通过抑制活性氧(ROS)显著减轻脑损伤，表明其在中风治疗中的潜在应用。
注：以上文献信息为示例性质，建议通过学术数据库(如PubMed、Web of Science)检索真实文献。
**Background of Recombinant Neuroglobin (NGB)**
Neuroglobin (NGB), a member of the vertebrate globin family, was first identified in 2000 as a neuron-specific oxygen-binding protein. Structurally, it shares homology with hemoglobin and myoglobin but is distinguished by its six-coordinate heme-binding motif, where both proximal and distal histidines coordinate the iron atom. NGB is predominantly expressed in the central and peripheral nervous systems, retina, and endocrine tissues, suggesting roles beyond oxygen storage and transport.
Research highlights NGB’s neuroprotective functions, particularly under hypoxic or ischemic conditions. It mitigates oxidative stress by scavenging reactive oxygen species (ROS) and regulating nitric oxide (NO) metabolism. NGB overexpression in experimental models reduces neuronal apoptosis, potentially through interactions with mitochondrial pathways, such as modulating cytochrome c release or influencing Bax/Bcl-2 balance. Additionally, NGB may support neuroplasticity and cognitive function, though these mechanisms remain less defined.
The production of recombinant NGB leverages genetic engineering to express and purify the protein in bacterial (e.g., *E. coli*) or eukaryotic systems. This enables detailed biophysical and functional studies, revealing its oxygen-binding kinetics, redox properties, and tertiary structure dynamics. Recombinant NGB also holds therapeutic promise, with preclinical studies exploring its potential in treating stroke, Alzheimer’s disease, and traumatic brain injury. Challenges include optimizing delivery methods and understanding its context-dependent roles *in vivo*.
Current research focuses on elucidating NGB’s signaling pathways, its interplay with other neuroprotective molecules, and translational applications. Advances in recombinant technology and protein engineering may accelerate its development as a therapeutic agent or biomarker for neurological disorders.
×
