| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NPL |
| Uniprot No | Q9BXD5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-320aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAFPKKKLQGLVAATITPMTENGEINFSVI GQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLDQ VIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFLKE VAAAAPALPFYYYHIPALTGVKIRAEELLDGILDKIPTFQGLKFSDTDLL DFGQCVDQNRQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQM LEAFEQKDFSLALNYQFCIQRFINFVVKLGFGVSQTKAIMTLVSGIPMGP PRLPLQKASREFTDSAEAKLKSLDFLSFTDLKDGNLEAGS |
| 预测分子量 | 37 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NPL重组蛋白的3-4条示例性参考文献(注：文献为虚构，仅作格式示例)：
---
1. **文献名称**：*High-Yield Expression and Characterization of Recombinant NPL Protein in Pichia pastoris*
**作者**：Chen L, Wang X, et al.
**摘要**：本研究利用毕赤酵母表达系统高效生产NPL重组蛋白，通过密码子优化和发酵条件调控，将蛋白产量提升至1.2 g/L，并验证其具有天然构象和酶活性，为工业化生产奠定基础。
2. **文献名称**：*Functional Analysis of NPL Recombinant Protein in Glycan Biosynthesis Pathways*
**作者**：Smith J, Tanaka K, et al.
**摘要**：通过体外酶活实验和质谱分析，揭示NPL重组蛋白在唾液酸合成通路中的关键作用，证明其可催化特定糖基转移反应，为糖工程领域提供新工具。
3. **文献名称**：*Cryo-EM Structure Determination of NPL Recombinant Protein Reveals Allosteric Regulation*
**作者**：Zhang Y, Müller P, et al.
**摘要**：采用冷冻电镜技术解析NPL重组蛋白的3.2 Å分辨率结构，发现其变构调节域，结合分子动力学模拟阐明底物诱导的构象变化机制。
4. **文献名称**：*Therapeutic Potential of NPL Recombinant Protein in Inflammatory Disease Models*
**作者**：Gupta R, Li M, et al.
**摘要**：在小鼠模型中验证NPL重组蛋白通过抑制NLRP3炎症小体减轻炎症反应，表明其作为新型抗炎药物的开发潜力。
---
以上示例涵盖表达优化、功能研究、结构解析及医学应用方向，可根据实际研究方向调整关键词和内容。如需真实文献，建议在PubMed或Web of Science中以“NPL recombinant protein”结合具体物种或功能进行检索。
**Background of NPL Recombinant Proteins**
Recombinant proteins, including NPL (Neuropolypeptide-Like) recombinant proteins, are engineered through genetic engineering techniques to mimic or modify naturally occurring proteins. The concept originated in the 1970s with advances in recombinant DNA technology, enabling scientists to insert genes encoding specific proteins into host organisms (e.g., bacteria, yeast, or mammalian cells) for large-scale production. NPL recombinant proteins, though not as widely studied as other therapeutic proteins, represent a niche area of interest, particularly in neuroscience and regenerative medicine.
NPL proteins are hypothesized to play roles in neural development, synaptic plasticity, or neuroprotection, drawing parallels to naturally occurring neurotrophic factors. Their recombinant versions are designed to enhance stability, bioavailability, or targeted functionality compared to native peptides. For instance, modifying expression systems (e.g., E. coli or CHO cells) allows precise control over post-translational modifications, critical for bioactivity.
The development of NPL recombinant proteins aligns with broader trends in biopharmaceuticals, where recombinant technology addresses challenges like scalability, cost, and immunogenicity. Applications range from research tools for studying neurodegenerative diseases (e.g., Alzheimer’s or Parkinson’s) to potential therapeutics for nerve repair. However, challenges remain, including optimizing delivery methods and ensuring efficacy in complex biological systems.
Overall, NPL recombinant proteins exemplify the intersection of molecular biology and translational medicine, offering tailored solutions for understanding and treating neurological disorders while leveraging the versatility of recombinant protein platforms.
×
