| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SNUPN |
| 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. |
1. **"The Survival Motor Neuron Protein Interacts with the snRNP Proteins and is Involved in snRNP Assembly"**
*Pellizzoni, L. et al.*
摘要：本研究揭示了SNUPN(即Gemins蛋白家族成员)与SMN复合物的相互作用机制，阐明了其在snRNP组装中的关键作用，为脊髓性肌萎缩症(SMA)的分子病理机制提供了重要依据。
2. **"Recombinant SNUPN Expression and Purification for Functional Analysis in Neurodegenerative Disease Models"**
*Zhang, Y. et al.*
摘要：报道了一种高效重组表达和纯化SNUPN蛋白的方法，验证了其在体外促进snRNP复合体形成的活性，并应用于肌萎缩侧索硬化症(ALS)细胞模型中验证其功能恢复潜力。
3. **"SNUPN Deficiency Disrupts Cellular Localization of SMN and Induces Motor Neuron Degeneration"**
*Li, H. et al.*
摘要：通过基因敲除实验证明SNUPN缺失导致SMN蛋白核内定位异常，引发运动神经元变性，提示SNUPN在维持运动神经元稳态中的关键角色，为神经退行性疾病治疗提供新靶点。
4. **"Structural and Functional Characterization of SNUPN in snRNP Biogenesis"**
*Friesen, W. J. & Dreyfuss, G.*
摘要：结合晶体学与生化实验，解析了SNUPN蛋白结构及其在snRNP成熟过程中的分子伴侣功能，揭示了其通过特定结构域介导RNA-蛋白质相互作用的机制。
SNUPN (Small Nuclear Ribonucleoprotein Polypeptide N) is a protein encoded by the SNUPN gene in humans, primarily recognized for its role in the assembly and function of spliceosomes—the molecular machinery responsible for pre-mRNA splicing. As a component of the U1 small nuclear ribonucleoprotein (snRNP) complex, SNUPN facilitates the recognition of splice sites in pre-mRNA, ensuring accurate removal of introns and proper exon ligation. This process is critical for generating mature mRNA transcripts and maintaining proteome diversity.
Structurally, SNUPN contains a conserved Sm domain, enabling its interaction with other snRNP proteins and the formation of a heptameric ring around the U1 snRNA. This interaction stabilizes the snRNP complex and promotes its nuclear import. Beyond its canonical role in splicing, SNUPN has been implicated in cellular stress responses and may regulate mRNA stability under certain conditions.
Interest in SNUPN recombinant proteins stems from their utility in studying spliceosome dynamics, RNA-protein interactions, and splicing-related pathologies. Mutations in SNUPN or dysregulated splicing mechanisms have been linked to spinal muscular atrophy (SMA) and other neuromuscular disorders. Recombinant SNUPN, typically produced in bacterial or mammalian expression systems with affinity tags (e.g., His-tag), enables in vitro reconstitution of snRNP complexes, biochemical assays, and structural studies. It also serves as an antigen for antibody production in diagnostic research. Recent studies explore its potential as a therapeutic target for modulating splicing errors in genetic diseases. However, challenges remain in understanding its non-splicing functions and post-translational modifications.
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