| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SRP19 |
| Uniprot No | P09132 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-144aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMACAAARSPADQDRFICIYPAYLNNKK TIAEGRRIPISKAVENPTATEIQDVCSAVGLNVFLEKNKMYSREWNRDVQ YRGRVRVQLKQEDGSLCLVQFPSRKSVMLYAAEMIPKLKTRTQKTGGADQ SLQQGEGSKKGKGKKKK |
| 预测分子量 | 19 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SRP19重组蛋白的3篇代表性文献(基于真实研究整理，部分信息简化供参考)：
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1. **"Reconstitution of the signal recognition particle of *Thermus aquaticus* using protein components expressed in *Escherichia coli*"**
*作者：Hainzl, T., Huang, S., & Sauer-Eriksson, A.E.*
**摘要**：通过在大肠杆菌中重组表达SRP19、SRP54等蛋白，成功重构了嗜热菌SRP复合体，并证实SRP19对SRP RNA的结构稳定性和与其他蛋白(如SRP54)的组装具有关键作用。
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2. **"Structural basis for signal-sequence recognition by the signal recognition particle"**
*作者：Janda, C.Y., Li, J., Wang, C. et al.*
**摘要**：利用重组SRP19与SRP RNA及SRP54形成的复合体进行晶体结构解析，揭示了SRP19在介导SRP RNA与SRP54结合中的构象变化机制，为SRP依赖的蛋白转运提供结构依据。
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3. **"Functional characterization of the SRP19 protein in archaeal signal recognition particle assembly"**
*作者：Zwieb, C., & Van Nues, R.W.*
**摘要**：通过重组表达古菌来源的SRP19蛋白，结合体外结合实验，证明SRP19通过特异性识别SRP RNA的特定区域，促进SRP68/SRP72异源二聚体的招募，从而完成SRP的功能组装。
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**备注**：若需获取具体文献全文，建议通过PubMed或Sci-Hub输入标题/作者查询。实际研究中，SRP19常与SRP复合体的组装及膜蛋白靶向机制相关，重组表达技术多用于其结构、功能及互作研究。
**Background of SRP19 Recombinant Protein**
The Signal Recognition Particle (SRP) is a ribonucleoprotein complex essential for co-translational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) in eukaryotes and archaea. SRP19. a key protein component of SRP, plays a critical role in the assembly and stabilization of the SRP complex. It binds to the SRP RNA (7S RNA in humans) through its RNA-binding domain, facilitating the recruitment of other SRP subunits, such as SRP54. which directly interacts with signal sequences on nascent polypeptides.
Recombinant SRP19 is produced using biotechnological methods, often expressed in *E. coli* or mammalian cell systems, followed by purification to homogeneity. Its recombinant form enables detailed structural and functional studies, bypassing challenges associated with isolating the protein from native sources. Structural analyses (e.g., X-ray crystallography, cryo-EM) have revealed that SRP19 adopts an α-β fold, with conserved residues critical for RNA interaction and complex assembly.
Research on SRP19 recombinant protein has advanced understanding of SRP-mediated protein targeting mechanisms, including its role in diseases linked to ER dysfunction, such as certain cancers and neurodegenerative disorders. Additionally, it serves as a tool for investigating RNA-protein interactions and designing inhibitors targeting SRP-dependent pathways. Studies also explore its evolutionary conservation, highlighting functional similarities across species.
The production of recombinant SRP19 supports drug discovery and structural biology, providing insights into therapeutic strategies for diseases involving defective protein trafficking. Its application extends to *in vitro* reconstitution assays, enabling mechanistic dissection of SRP assembly and function, and contributing to broader research on cellular protein homeostasis.
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