| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NUP210 |
| Uniprot No | Q8TEM1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-238aa |
| 氨基酸序列 | LNIPKVLLPFTRATRVNFTLEASEGCYRWLSTRPEVASIEPLGLDEQQCSQKAVVQARLTQPARLTSIIFAEDITTGQVLRCDAIVDLIHDIQIVSTTRELYLEDSPLELKIQALDSEGNTFSTLAGLVFEWTIVKDSEADRFSDSHNALRILTFLESTYIPPSYISEMEKAAKQGDTILVSGMKTGSSKLKARIQEAVYKNVRPAEVRLL |
| 预测分子量 | 27.6 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. |
以下是模拟生成的关于NUP210重组蛋白的参考文献示例(实际文献需通过学术数据库查询)：
---
1. **文献名称**: *NUP210 regulates myogenesis by modulating nuclear pore complex stability*
**作者**: Cohen, A. et al.
**摘要**: 研究利用重组NUP210蛋白揭示了其在骨骼肌分化中的作用，发现NUP210通过稳定核孔复合体结构，促进肌肉特异性基因的核质运输，从而调控肌细胞分化。
2. **文献名称**: *Recombinant NUP210 expression in cancer metastasis: Insights from in vitro models*
**作者**: Zhang, L. & Wang, H.
**摘要**: 该文献通过体外表达重组NUP210蛋白，证明其过表达可增强乳腺癌细胞的迁移能力，可能与核膜完整性破坏导致促转移因子异常分泌有关。
3. **文献名称**: *Structural analysis of the NUP210 C-terminal domain using recombinant protein crystallization*
**作者**: Müller, R. et al.
**摘要**: 利用重组NUP210蛋白的C端结构域进行晶体学研究，揭示了其与核膜磷脂相互作用的分子机制，为核孔复合体锚定模型提供结构依据。
---
**注**：以上为基于领域知识的模拟内容，实际文献需通过PubMed、Google Scholar等平台以关键词“NUP210 recombinant protein”或“NUP210 structure/function”检索获取。
**Background of NUP210 Recombinant Protein**
NUP210 (Nucleoporin 210), also known as gp210. is a transmembrane protein component of the nuclear pore complex (NPC), a large protein assembly embedded in the nuclear envelope that regulates nucleocytoplasmic transport. It plays a structural role in anchoring the NPC to the nuclear membrane and contributes to maintaining nuclear integrity. NUP210 is characterized by a large luminal domain, a single transmembrane region, and a short cytoplasmic tail. Its luminal domain contains multiple O-glycosylation sites and interacts with other nucleoporins to stabilize NPC architecture.
NUP210 is expressed in a tissue-specific manner, with high levels observed in muscle cells, neurons, and secretory cells. Studies suggest its involvement in cellular differentiation, particularly during myogenesis and neurogenesis. It also participates in regulating gene expression by influencing the spatial organization of chromatin near the nuclear periphery. Dysregulation of NUP210 has been linked to diseases, including cancers (e.g., breast, liver) and neurological disorders, where altered NPC function may disrupt cellular homeostasis.
Recombinant NUP210 protein is engineered for *in vitro* studies to investigate its interactions, post-translational modifications (e.g., glycosylation), and role in disease mechanisms. It serves as a tool for developing diagnostic assays or therapeutic strategies targeting NPC dysfunction. Research on NUP210 recombinant proteins also explores its potential as a biomarker, given its aberrant expression in certain malignancies. However, challenges remain in mimicking its native membrane-bound structure and glycosylation patterns, necessitating advanced expression systems for functional studies.
×
