| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SNUPN1 |
| Uniprot No | O95149 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-360aa |
| 氨基酸序列 | MEELSQALAS SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRRLLEL QKSKRLDYVN HARRLAEDDW TGMESEEENK KDDEEMDIDT VKKLPKHYAN QLMLSEWLID VPSDLGQEWI VVVCPVGKRA LIVASRGSTS AYTKSGYCVN RFSSLLPGGN RRNSTAKDYT ILDCIYNEVN QTYYVLDVMC WRGHPFYDCQ TDFRFYWMHS KLPEEEGLGE KTKLNPFKFV GLKNFPCTPE SLCDVLSMDF PFEVDGLLFY HKQTHYSPGS TPLVGWLRPY MVSDVLGVAV PAGPLTTKPD YAGHQLQQIM EHKKSQKEGM KEKLTHKASE NGHYELEHLS TPKLKGSSHS PDHPGCLMEN |
| 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SNUPN1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*SNUPN1调控mRNA出核转运的分子机制研究*
**作者**：Li, X. 等 (2022)
**摘要**：该研究通过重组SNUPN1蛋白体外实验，证实其与核转运复合体相互作用，调控特定mRNA的核质转运，揭示其在基因表达调控中的关键作用。
2. **文献名称**：*SNUPN1重组蛋白的纯化及其与E3泛素连接酶的互作分析*
**作者**：Zhang, Y. 等 (2020)
**摘要**：研究利用大肠杆菌系统表达重组SNUPN1蛋白，优化纯化条件，并发现其通过与E3泛素连接酶结合参与蛋白质泛素化通路，为癌症治疗提供潜在靶点。
3. **文献名称**：*SNUPN1在脊髓性肌萎缩症中的功能缺失机制*
**作者**：Wang, H. 等 (2019)
**摘要**：通过构建SNUPN1重组蛋白突变体，发现其与SMN复合物的结合能力下降，导致运动神经元功能障碍，为脊髓性肌萎缩症的病理机制提供新见解。
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**备注**：上述文献为虚拟示例，实际研究中建议通过PubMed或Web of Science检索关键词“SNUPN1 recombinant protein”获取最新实证研究。
**Background of SNUPN1 Recombinant Protein**
SNUPN1 (Snurportin-1) is a nuclear transport protein primarily involved in the assembly and recycling of the spliceosome, the macromolecular machinery responsible for pre-mRNA splicing. It specifically recognizes and binds to m³G-capped spliceosomal small nuclear ribonucleoproteins (snRNPs), facilitating their nuclear import via the importin-β pathway. Structurally, SNUPN1 contains an N-terminal importin-β-binding domain and a C-terminal m³G cap-binding domain, enabling its dual role in snRNP trafficking.
Recombinant SNUPN1 protein is engineered to study its molecular interactions, structural dynamics, and functional roles in spliceosome assembly and mRNA processing. Produced through heterologous expression systems (e.g., *E. coli* or mammalian cells*), the recombinant protein is purified to homogeneity, often with affinity tags (e.g., His-tag, GST) for experimental applications. Its production allows *in vitro* analyses, such as binding assays, structural studies (X-ray crystallography, cryo-EM), and investigations into snRNP biogenesis defects linked to diseases like spinal muscular atrophy or cancer.
SNUPN1 dysregulation has been implicated in cellular stress responses and neurodegenerative conditions, highlighting its broader biological significance. Recombinant SNUPN1 also serves as a tool for developing therapeutic strategies targeting spliceosome-related disorders. Studies leveraging this protein have advanced understanding of nuclear transport mechanisms and their crosstalk with RNA metabolism, offering insights into fundamental cell biology and disease pathogenesis.
*(Note: Mammalian systems may be preferred for proper post-translational modifications.)*
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