| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SNRNP70 |
| Uniprot No | P08621 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-210aa |
| 氨基酸序列 | MTQFLPPNLLALFAPRDPIPYLPPLEKLPHEKHHNQPYCGIAPYIREFEDPRDAPPPTRAETREERMERKRREKIERRQQEVETELKMWDPHNDPNAQGDAFKTLFVARVNYDTTESKLRREFEVYGPIKRIHMVYSKRSGKPRGYAFIEYEHERDMHSAYKHADGKKIDGRRVLVDVERGRTVKGWRPRRLGGGLGGTRRGGADVNIRH |
| 预测分子量 | 28.7 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SNRNP70重组蛋白的3篇参考文献示例(虚构，供参考)：
1. **文献名称**：*Recombinant SNRNP70 Facilitates Spliceosome Assembly in Vitro*
**作者**：Krämer A. et al.
**摘要**：研究利用大肠杆菌表达系统纯化重组SNRNP70蛋白，验证其在体外剪接体组装中的关键作用，证明其与U1 snRNP的结合能力及对前体mRNA剪接的调控。
2. **文献名称**：*Structural Insights into SNRNP70 Function via Recombinant Protein Analysis*
**作者**：Lei J. & Shi Y.
**摘要**：通过重组SNRNP70蛋白的晶体结构解析，揭示其RNA识别基序(RRM)的结构特征，并阐明其参与剪接体早期组装的具体分子机制。
3. **文献名称**：*SNRNP70 Mutations Disrupt mRNA Splicing in Neurodegenerative Disorders*
**作者**：Zhang L. & Cooper TA.
**摘要**：利用重组SNRNP70蛋白进行功能拯救实验，发现其突变导致剪接异常，与脊髓性肌萎缩症(SMA)等疾病的病理过程相关。
4. **文献名称**：*Optimized Expression and Purification of Human SNRNP70 for Functional Studies*
**作者**：Pellizzoni L. et al.
**摘要**：开发了一种高效的真核表达系统(如HEK293细胞)制备重组SNRNP70蛋白，优化纯化步骤以提高蛋白活性，并应用于剪接体复合物的体外重构。
(注：以上文献为示例，实际引用需根据具体研究内容检索真实数据库。)
**Background of SNRNP70 Recombinant Protein**
SNRNP70 (Small Nuclear Ribonucleoprotein U1 Subunit 70), also known as U1-70K, is a key component of the U1 small nuclear ribonucleoprotein (U1 snRNP) complex, which plays a central role in pre-mRNA splicing. This protein is part of the spliceosome, a dynamic molecular machinery responsible for removing introns and ligating exons during mRNA processing. SNRNP70 specifically binds to the 5' splice site of pre-mRNA through its interaction with U1 snRNA, ensuring accurate recognition of exon-intron boundaries.
Structurally, SNRNP70 contains three conserved domains: an N-terminal RNA recognition motif (RRM), a central disordered glycine-rich region, and a C-terminal domain involved in protein-protein interactions. The RRM facilitates RNA binding, while the glycine-rich region mediates interactions with other splicing factors, such as components of the Sm protein complex.
Recombinant SNRNP70 is produced using heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its biochemical properties, spliceosome assembly, and regulatory mechanisms. It is often tagged (e.g., His-tag, GST-tag) for purification and detection. Researchers utilize this protein to investigate splicing anomalies linked to diseases, including cancer and neurodegenerative disorders, where aberrant splicing contributes to pathogenesis.
Additionally, SNRNP70 is a known autoantigen in autoimmune conditions like systemic lupus erythematosus (SLE), making its recombinant form valuable for studying autoimmune responses. Studies also explore its post-translational modifications (e.g., phosphorylation) and how these affect splicing efficiency or interactions within the spliceosome. Overall, SNRNP70 recombinant protein serves as a critical tool for dissecting RNA splicing mechanisms and their implications in health and disease.
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