纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | NPS |
Uniprot No | P0C0P6 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 70-89aa |
氨基酸序列 | S FRNGVGTGMK KTSFQRAKS |
预测分子量 | 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NPS(神经肽S)重组蛋白的模拟参考文献示例,内容为虚构,仅供格式参考:
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1. **文献名称**:*Expression and Functional Analysis of Recombinant Neuropeptide S in Mammalian Cells*
**作者**:A. Tanaka, M. Kimura
**摘要**:本研究利用哺乳动物表达系统成功制备了高纯度重组NPS蛋白,验证了其通过激活NPS受体(NPSR)介导的细胞内钙信号通路活性,为体外药理学研究提供了工具。
2. **文献名称**:*Crystal Structure of Recombinant Neuropeptide S Bound to Its Receptor*
**作者**:L. Müller et al.
**摘要**:通过X射线晶体学解析了重组NPS与其受体的复合物结构,揭示了关键氨基酸残基在配体结合中的作用,为靶向NPSR的药物设计提供结构基础。
3. **文献名称**:*Recombinant NPS Attenuates Anxiety-like Behavior in Rodent Models via Central Administration*
**作者**:S. Patel, R. Costa
**摘要**:动物实验表明,重组NPS通过侧脑室注射显著减少小鼠焦虑样行为,提示其在中枢神经系统的潜在治疗应用。
4. **文献名称**:*Optimization of Recombinant NPS Production in Pichia pastoris*
**作者**:J. Zhang et al.
**摘要**:优化毕赤酵母表达系统以提高重组NPS的产量,并证明其生物活性与天然肽一致,适用于大规模制备研究。
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**注**:以上文献为模拟示例,非真实存在。实际研究中建议通过PubMed或SciHub等平台检索关键词(如“Neuropeptide S recombinant”“NPSR signaling”)获取最新文献。
**Background of NPS Recombinant Protein**
Recombinant proteins, including NPS (Neuroendocrine Protein Secretagogin), are engineered through genetic modification to produce specific proteins in controlled laboratory settings. The development of recombinant DNA technology in the 1970s revolutionized protein synthesis, enabling the production of proteins like NPS in heterologous systems such as *E. coli*, yeast, or mammalian cells. This approach bypasses the limitations of extracting proteins directly from native tissues, ensuring higher purity, scalability, and customization.
NPS, a calcium-binding protein initially identified in neuroendocrine tissues, plays roles in cell adhesion, secretion, and neuronal differentiation. Its recombinant version is generated by inserting the NPS gene into expression vectors, which are then transfected into host cells. Post-translationally modified forms may require mammalian systems to preserve functional integrity.
The applications of recombinant NPS span biomedical research and therapeutic development. It serves as a tool to study neuroendocrine signaling pathways, cancer biology (due to its expression in tumors), and neurological disorders. In therapeutics, recombinant NPS could potentially aid in drug delivery or act as a biomarker. Challenges include optimizing expression yields, ensuring proper folding, and minimizing immunogenicity in clinical settings.
Advances in protein engineering, such as CRISPR and AI-driven design, continue to refine recombinant protein production. For NPS, ongoing research focuses on enhancing stability and functional efficacy, underscoring its potential in precision medicine and targeted therapies.
In summary, NPS recombinant protein exemplifies the intersection of genetic engineering and molecular biology, offering insights into complex biological mechanisms and paving the way for innovative treatments. Its development highlights the broader impact of recombinant technologies in addressing scientific and medical challenges.
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