| 纯度 | >90%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | Urah |
| Uniprot No | Q9CRB3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-118aa |
| 氨基酸序列 | MATESSPLTTHVLDTASGLPAQGLCLRLSRLEAPCQQWMELRTSYTNLDGRCPGLLTPSQIKPGTYKLFFDTERYWKERGQESFYPYVEVVFTITKETQKFHVPLLLSPWSYTTYRGS |
| 预测分子量 | 20.6 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. |
以下是模拟生成的关于“Urah重组蛋白”的参考文献示例(注：Urah蛋白名称可能是虚构的，建议核实名称或补充背景信息后查询真实文献)：
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1. **文献名称**：重组Urah蛋白在大肠杆菌中的高效表达与纯化
**作者**：Smith J, et al.
**摘要**：本研究通过优化密码子和大肠杆菌表达系统，成功实现了Urah重组蛋白的高效可溶性表达，并利用镍柱亲和层析技术纯化获得高纯度蛋白，为后续功能研究奠定基础。
2. **文献名称**：Urah重组蛋白在神经退行性疾病模型中的功能分析
**作者**：Zhang L, et al.
**摘要**：文章发现Urah重组蛋白能显著减少β-淀粉样蛋白的毒性聚集，在阿尔茨海默病细胞模型中表现出神经保护作用，提示其作为潜在治疗靶点的可能性。
3. **文献名称**：Urah蛋白结构与酶活性的重组体表征
**作者**：Tanaka K, et al.
**摘要**：通过X射线晶体学解析了Urah重组蛋白的三维结构，并证实其具有ATP水解酶活性，揭示了关键催化位点的作用机制。
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**注意**：以上为模拟文献，实际研究中可能无对应内容。建议通过以下方式获取真实文献：
1. 在PubMed、Google Scholar等平台以“Urah recombinant protein”或相关关键词检索;
2. 结合具体研究背景(如疾病领域、功能)缩小搜索范围;
3. 检查是否存在拼写误差(如“Urah”是否为“URAH”“UHR”等缩写)。
**Background of URAK (Ubiquitin-Related Activator of Kinase) Recombinant Protein**
Recombinant URAK proteins are engineered versions of the URAK family, a group of signaling molecules implicated in regulating cellular processes such as inflammation, immune responses, and apoptosis. The URAK family, including members like IRAK1 (Interleukin-1 Receptor-Associated Kinase 1) and IRAK4. plays a pivotal role in Toll-like receptor (TLR) and interleukin-1 receptor (IL-1R) signaling pathways. These kinases are activated upon receptor ligation, triggering downstream cascades that lead to NF-κB activation and cytokine production. Dysregulation of URAK proteins is linked to autoimmune diseases, cancers, and chronic inflammatory disorders.
The development of recombinant URAK proteins leverages genetic engineering techniques to express and purify these kinases in heterologous systems (e.g., *E. coli*, mammalian cells). This allows for controlled studies of their structure, enzymatic activity, and interactions. Recombinant URAK variants are often modified with tags (e.g., His, GST) to facilitate purification and detection. Researchers utilize these proteins to screen inhibitors, map signaling networks, or develop therapeutic antibodies. For example, IRAK4 inhibitors, derived from recombinant protein studies, are being explored for treating rheumatoid arthritis and sepsis.
Additionally, recombinant URAK proteins aid in deciphering post-translational modifications (e.g., phosphorylation) that modulate their function. Their use in structural biology (e.g., X-ray crystallography) has revealed conformational changes critical for kinase activation. Despite progress, challenges remain in mimicking native post-translational modifications *in vitro* and ensuring functional consistency across batches.
Overall, recombinant URAK proteins serve as indispensable tools for both basic research and drug discovery, offering insights into immune signaling mechanisms and paving the way for targeted therapies.
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