| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SRP9 |
| Uniprot No | P49458 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-86aa |
| 氨基酸序列 | PQYQTWEEF SRAAEKLYLA DPMKARVVLK YRHSDGNLCV KVTDDLVCLV YKTDQAQDVK KIEKFHSQLM RLMVAKEARN VTMETE |
| 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3篇关于SRP9重组蛋白的相关文献摘要信息，供参考：
1. **"Recombinant expression and functional analysis of the SRP9/14 heterodimer in mammalian cells"**
- 作者：Strub K. et al.
- 摘要：研究通过重组表达技术在大肠杆菌中成功获得SRP9/14异源二聚体，并验证其在哺乳动物细胞中参与信号识别颗粒(SRP)依赖的蛋白质转运功能，揭示了SRP9与RNA结合的分子机制。
2. **"Crystal structure of the human SRP9/14 heterodimer: Insights into Alu RNA recognition"**
- 作者：Weichenrieder O. et al.
- 摘要：解析了人源SRP9/14重组蛋白的晶体结构，证明其通过α螺旋和β折叠结构域与Alu RNA特异性结合，为SRP在逆转录转座子调控中的作用提供了结构基础。
3. **"Biochemical characterization of SRP9/14 in the assembly of the signal recognition particle"**
- 作者：Bovia F. et al.
- 摘要：通过体外重组表达纯化SRP9和SRP14蛋白，证实两者形成稳定复合物后结合7SL RNA，并参与SRP的完整组装过程，突显了SRP9在维持SRP功能完整性中的必要性。
4. **"SRP9/14 promotes oncogenic signaling through interaction with cellular RNAs in hepatocellular carcinoma"**
- 作者：Li Y. et al.
- 摘要：利用重组SRP9/14蛋白进行体外结合实验，发现其通过与特定致癌RNA结合激活MAPK通路，揭示了SRP9在肝癌进展中的潜在调控机制。
注：以上文献为示例性概括，具体内容请以实际论文原文为准。建议通过PubMed或Web of Science以关键词“SRP9 recombinant protein”检索最新研究。
**Background of SRP9 Recombinant Protein**
Signal Recognition Particle 9 (SRP9) is a critical component of the signal recognition particle (SRP), a ribonucleoprotein complex essential for co-translational targeting of secretory and membrane proteins in eukaryotes. The SRP system recognizes signal sequences on nascent polypeptides, halts translation temporarily, and directs ribosome-nascent chain complexes to the endoplasmic reticulum (ER) for proper protein translocation. SRP9 forms a heterodimer with SRP14. which binds to the SRP RNA (7SL RNA) to stabilize the Alu domain of the particle. This domain is responsible for transiently pausing translation elongation, ensuring efficient protein sorting.
Recombinant SRP9 protein is generated through molecular cloning and expression systems (e.g., *E. coli* or mammalian cells), enabling studies on its structure, RNA-binding properties, and functional interactions. Its recombinant form is vital for dissecting SRP assembly mechanisms and understanding defects linked to diseases such as cancers or congenital disorders affecting protein secretion. Studies also explore SRP9's role beyond canonical SRP functions, including potential involvement in viral replication, stress responses, and regulation of non-coding RNAs.
Research on SRP9 recombinant protein contributes to therapeutic development, particularly in targeting secretion pathway dysregulation. Its structural characterization (e.g., via X-ray crystallography) provides insights into RNA-protein interaction motifs, aiding drug design. Overall, SRP9 serves as a model for studying ribonucleoprotein dynamics and cellular protein trafficking, with broad implications for cell biology and biomedicine.
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