| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NUP188 |
| Uniprot No | Q5SRE5 |
| 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NUP188重组蛋白的参考文献示例(注：文献为虚构示例，实际需根据具体研究补充)：
1. **标题**：*Structural and functional analysis of recombinant NUP188 in nuclear pore assembly*
**作者**：Smith A, et al.
**摘要**：研究通过重组表达人源NUP188蛋白，结合体外重建实验，揭示了NUP188在核孔复合体(NPC)组装中的关键作用，表明其C端结构域对维持核膜曲度至关重要。
2. **标题**：*NUP188 interacts with SEC13 to regulate endoplasmic reticulum morphology*
**作者**：Chen L, et al.
**摘要**：利用重组NUP188蛋白进行免疫共沉淀实验，发现其与SEC13的相互作用，并证明该互作通过调控内质网膜形态影响细胞分泌功能。
3. **标题**：*Recombinant NUP188 facilitates nucleocytoplasmic transport in a CRISPR-edited cell model*
**作者**：Tanaka K, et al.
**摘要**：通过重组NUP188蛋白回补实验，在NUP188敲除细胞中恢复了核质运输效率，证实其作为核孔支架蛋白对物质运输的直接调控。
4. **标题**：*Cryo-EM structure of the NUP188-containing subcomplex in the nuclear pore*
**作者**：Zhang Y, et al.
**摘要**：基于重组NUP188蛋白的冷冻电镜结构解析，阐明了其与NUP93、NUP205形成的亚复合体结构，为理解NPC稳定性提供了分子基础。
(注：以上文献为示例，实际引用需查询真实数据库如PubMed、Web of Science等。)
NUP188 (Nucleoporin 188) is a critical component of the nuclear pore complex (NPC), a large protein assembly embedded in the nuclear envelope that regulates bidirectional transport between the nucleus and cytoplasm. As a member of the nucleoporin family, NUP188 contributes to the structural integrity and selective permeability of the NPC. Unlike many nucleoporins that form the central channel or cytoplasmic filaments, NUP188 is part of the NPC’s scaffold architecture, stabilizing its framework and potentially modulating transport activity through interactions with other scaffold proteins like NUP93 and NUP205. Its name derives from its molecular weight of approximately 188 kDa.
Recombinant NUP188 proteins are engineered to study its molecular functions, interactions, and structural roles in vitro or in cellular models. These proteins are typically expressed in heterologous systems (e.g., bacteria, insect cells) using cDNA clones, enabling researchers to explore domains responsible for NPC assembly, membrane curvature regulation, or binding partners. Structurally, NUP188 contains multiple α-solenoid and transmembrane domains, suggesting roles in anchoring the NPC to the nuclear membrane. Dysregulation of NUP188 has been linked to diseases, including cardiomyopathies, neurodegenerative disorders, and cancers, where altered nucleocytoplasmic transport may drive pathogenesis. For example, NUP188 mutations disrupt cardiac development in zebrafish, while its overexpression in prostate cancer correlates with poor prognosis. Recombinant variants (e.g., tagged, truncated) are pivotal in dissecting these mechanisms, offering insights into NPC-related diseases and potential therapeutic targets. Despite progress, NUP188’s precise regulatory dynamics in vivo remain incompletely understood, highlighting the need for further research using recombinant tools.
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