| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NISCH |
| Uniprot No | Q9Y2I1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 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NISCH重组蛋白的3篇参考文献示例(注：文献为虚构示例，实际研究中请根据具体数据库检索验证)：
---
1. **标题**: *"Expression and Purification of Recombinant NISCH Protein in E. coli for Functional Studies"*
**作者**: Smith A, et al.
**摘要**: 研究报道了通过大肠杆菌表达系统高效生产NISCH重组蛋白的优化方法，包括密码子优化、可溶性表达条件及镍柱纯化步骤，为后续体外功能研究提供高纯度蛋白。
2. **标题**: *"Structural Insights into NISCH-Integrin Interaction Using Recombinant Protein Complexes"*
**作者**: Chen L, et al.
**摘要**: 利用重组NISCH蛋白与整合素β1亚基进行体外结合实验，结合X射线晶体学揭示了NISCH的C端结构域在调控细胞迁移中的关键作用，为靶向癌症转移研究奠定基础。
3. **标题**: *"Role of Recombinant NISCH in Suppressing Breast Cancer Cell Invasion via Rab14 Pathway"*
**作者**: Gupta R, et al.
**摘要**: 通过哺乳动物细胞表达系统获得重组NISCH蛋白，证明其通过调控Rab14依赖的囊泡运输抑制乳腺癌细胞侵袭，提示其在肿瘤治疗中的潜在应用价值。
---
**提示**：实际研究中建议通过PubMed或Web of Science以关键词“NISCH recombinant”“Nischarin expression”检索，并筛选涉及重组蛋白表达、功能或结构分析的文献。
NISCH (Nischarin), also known as imidazoline receptor antisera-selected protein (IRAS), is a multifunctional scaffolding protein encoded by the *NISCH* gene in humans. Initially identified as an imidazoline-1 receptor candidate, it plays diverse roles in cellular signaling, membrane trafficking, and disease pathogenesis. Structurally, NISCH contains multiple functional domains, including a phosphotyrosine-binding (PTB) domain and a conserved C-terminal region, enabling interactions with various partners like integrins, Rab14 GTPase, and PAK1 kinase. These interactions position NISCH as a critical regulator of cell migration, proliferation, and tumor suppression, particularly through its inhibition of the Rac1 signaling pathway.
Recombinant NISCH protein, produced via bacterial or mammalian expression systems, has become a vital tool for studying its molecular mechanisms. Researchers utilize it to investigate NISCH-mediated inhibition of breast cancer metastasis, modulation of neuronal outgrowth, and regulation of autophagy. Its role in insulin signaling and metabolic disorders has also gained attention, with studies linking NISCH dysfunction to hypertension and metabolic syndrome. The recombinant form enables precise biochemical assays, antibody development, and structural studies, overcoming challenges posed by low endogenous protein levels in tissues.
In therapeutic contexts, recombinant NISCH holds potential for cancer treatment strategies, given its tumor-suppressive effects, and as a biomarker for disease progression. However, production requires optimization due to its large molecular weight (~200 kDa) and post-translational modification needs. Ongoing research continues to unravel its tissue-specific functions and therapeutic applications across oncology, neurology, and metabolic diseases.
×
