| 纯度 | >90%SDS-PAGE. |
| 种属 | Vaccinia |
| 靶点 | K3L |
| Uniprot No | P20639 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-88aa |
| 氨基酸序列 | MLAFCYSLPNAGDVIKGRVYEKDYALYIYLFDYPHSEAILAESVKMHMDRYVEYRDKLVGKTVKVKVIRVDYTKGYIDVNYKRMCRHQ |
| 预测分子量 | 26.5 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K3L重组蛋白的虚构参考文献示例(内容基于常见研究方向模拟，非真实文献)：
1. **《痘苗病毒K3L蛋白抑制宿主PKR通路的机制研究》**
作者：Smith J, et al.
摘要：本研究通过重组表达痘苗病毒K3L蛋白，证实其通过模拟真核生物eIF2α的结构，抑制宿主PKR激酶活性，从而阻断干扰素介导的抗病毒反应。
2. **《重组K3L蛋白在体外对细胞翻译调控的影响》**
作者：Lee H, et al.
摘要：利用大肠杆菌系统表达并纯化K3L重组蛋白，实验表明其能有效阻止PKR诱导的eIF2α磷酸化，维持宿主细胞蛋白质合成，为病毒逃逸机制提供依据。
3. **《K3L与PKR相互作用的晶体结构解析》**
作者：Wang Y, et al.
摘要：通过X射线衍射分析重组K3L蛋白与人类PKR的复合物结构，揭示了K3L通过关键氨基酸残基竞争性结合PKR的催化结构域，抑制其二聚化激活。
4. **《基于K3L重组蛋白的疫苗载体开发》**
作者：Garcia R, et al.
摘要：将K3L基因插入重组疫苗载体中，证明其可减弱宿主细胞抗病毒应答，提升外源抗原表达效率，为新型疫苗设计提供策略。
注：以上为模拟内容，实际文献需通过学术数据库(如PubMed、Web of Science)检索。
The K3L recombinant protein is derived from the vaccinia virus, a member of the poxvirus family. Originally identified as a viral host-range gene product, K3L plays a critical role in counteracting host antiviral defenses. Its biological significance lies in mimicking eukaryotic translation initiation factor 2α (eIF2α), a key regulatory protein in cellular stress responses. During viral infection, host cells activate protein kinase R (PKR) to phosphorylate eIF2α, thereby halting global protein synthesis to limit viral replication. K3L acts as a molecular decoy, binding to PKR to inhibit this antiviral mechanism, allowing the virus to maintain translational machinery for its own replication.
Recombinant K3L protein is produced using genetic engineering techniques, typically expressed in bacterial (e.g., E. coli) or eukaryotic systems. Its recombinant form retains the PKR-binding capability while being purified from viral components, making it safer for research applications. Scientists utilize K3L recombinant protein primarily to study PKR-eIF2α signaling pathways, interferon-mediated antiviral responses, and mechanisms of viral immune evasion. It serves as a valuable tool for investigating cellular stress responses, including endoplasmic reticulum stress and the integrated stress response (ISR).
Recent applications extend to drug discovery, where K3L is used to screen PKR inhibitors with potential therapeutic value in chronic inflammation, neurodegenerative diseases, and cancer. Its structural similarity to human eIF2α also makes it a model for studying phosphorylation-related pathologies. Commercial versions are available for in vitro studies, often accompanied by mutation variants to probe specific interaction domains. As research continues, K3L recombinant protein remains pivotal in unraveling virus-host interactions and developing strategies to modulate cellular stress pathways.
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