| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NUP107 |
| Uniprot No | P57740 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-925aa |
| 氨基酸序列 | MDRSGFGEISSPVIREAEVTRTARKQSAQKRVLLQASQDENFGNTTPRNQVIPRTPSSFRQPFTPTSRSLLRQPDISCILGTGGKSPRLTQSSGFFGNLSMVTNLDDSNWAAAFSSQRSGLFTNTEPHSITEDVTISAVMLREDDPGEAASMSMFSDFLQSFLKHSSSTVFDLVEEYENICGSQVNILSKIVSRATPGLQKFSKTASMLWLLQQEMVTWRLLASLYRDRIQSALEEESVFAVTAVNASEKTVVEALFQRDSLVRQSQLVVDWLESIAKDEIGEFSDNIEFYAKSVYWENTLHTLKQRQLTSYVGSVRPLVTELDPDAPIRQKMPLDDLDREDEVRLLKYLFTLIRAGMTEEAQRLCKRCGQAWRAATLEGWKLYHDPNVNGGTELEPVEGNPYRRIWKISCWRMAEDELFNRYERAIYAALSGNLKQLLPVCDTWEDTVWAYFRVMVDSLVEQEIQTSVATLDETEELPREYLGANWTLEKVFEELQATDKKRVLEENQEHYHIVQKFLILGDIDGLMDEFSKWLSKSRNNLPGHLLRFMTHLILFFRTLGLQTKEEVSIEVLKTYIQLLIREKHTNLIAFYTCHLPQDLAVAQYALFLESVTEFEQRHHCLELAKEADLDVATITKTVVENIRKKDNGEFSHHDLAPALDTGTTEEDRLKIDVIDWLVFDPAQRAEALKQGNAIMRKFLASKKHEAAKEVFVKIPQDSIAEIYNQCEEQGMESPLPAEDDNAIREHLCIRAYLEAHETFNEWFKHMNSVPQKPALIPQPTFTEKVAHEHKEKKYEMDFGIWKGHLDALTADVKEKMYNVLLFVDGGWMVDVREDAKEDHERTHQMVLLRKLCLPMLCFLLHTILHSTGQYQECLQLADMVSSERHKLYLVFSKEELRKLLQKLRESSLMLLDQGLDPLGYEIQL |
| 预测分子量 | 106,3 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NUP107重组蛋白的3篇代表性文献及其简要摘要：
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1. **文献名称**: *Structural and functional analysis of the Nup107-160 complex in nuclear pore assembly*
**作者**: Walther TC et al.
**摘要**: 该研究通过重组表达NUP107及其复合物成员(NUP133、NUP96等)，解析了其在核孔复合体(NPC)组装中的关键作用。实验表明，NUP107重组蛋白复合体能够自发形成类核孔结构，并参与核膜重建和mRNA运输调控。
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2. **文献名称**: *NUP107 interacts with NUP62 to regulate nuclear pore complex formation in human cells*
**作者**: Harel A et al.
**摘要**: 利用重组NUP107蛋白进行体外结合实验，发现其与NUP62存在直接互作，并通过荧光共振能量转移(FRET)验证了动态结合过程。研究揭示了NUP107在维持核孔通透性及选择性运输中的分子机制。
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3. **文献名称**: *Mutation in NUP107 causes steroid-resistant nephrotic syndrome with neurological defects*
**作者**: Braun DA et al.
**摘要**: 通过重组NUP107突变体(如p.R401C)的功能研究，发现其导致核孔复合体稳定性下降，影响细胞核-质运输功能。该研究首次将NUP107突变与遗传性肾病及神经发育异常关联，为疾病机制提供了分子证据。
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如需更多文献或具体领域(如癌症、结构生物学)的研究，可进一步补充说明。
NUP107 is a critical component of the nuclear pore complex (NPC), a large protein assembly embedded in the nuclear envelope that regulates nucleocytoplasmic transport. As part of the conserved NUP107-160 subcomplex, NUP107 plays structural and functional roles in maintaining NPC integrity and mediating interactions between the NPC and transport machinery. This subcomplex, composed of multiple nucleoporins (e.g., NUP133. NUP160), forms the NPC's outer ring and anchors it to the nuclear membrane. Structurally, NUP107 contains α-helical solenoid domains and β-propeller folds, enabling protein-protein interactions essential for NPC assembly.
Beyond transport, NUP107 is implicated in mitosis, where it participates in spindle assembly and chromosome segregation. Dysregulation of NUP107 is linked to diseases, including steroid-resistant nephrotic syndrome, gonadal dysgenesis, and cancers, often due to mutations disrupting NPC stability or mitotic functions. Its role in cell cycle regulation and genome stability has made it a focus in oncology research.
Recombinant NUP107 protein, typically produced in bacterial (e.g., E. coli) or mammalian expression systems with tags (e.g., His-tag), enables in vitro studies of NPC architecture, transport mechanisms, and disease-associated mutations. Purification methods like affinity chromatography ensure high specificity. Researchers use it to investigate interactions with transport receptors (e.g., importins), map binding domains, or model NPC assembly in reconstitution experiments. In cellular studies, recombinant NUP107 helps rescue phenotypic defects in NUP107-depleted systems, clarifying its functional domains. Its applications extend to drug screening for NPC-related pathologies and mechanistic studies of viral hijacking of nuclear transport.
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