| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | D8L |
| Uniprot No | L7QJR5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-261aa |
| 氨基酸序列 | MPQQLSPINIETKKAISNARLKPLDIHYNESKPTTIQNTGKLVRINFKGGYISGGFLPNEYVLSSLRIYWGKEDDYGSNHLIDVYKYSGEINLVHWNKKKYSSYEEAKKHDDGLIIISIFLQVSDHKNVYFQKIVNQLDSIRSANTSAPFDSVFYLDNLLPSTLDYFTYLGTTINHSADAAWIIFPTPINIHSDQLSKFRTLLSSSNHDGKPHYITENYRNPYKLNDDTQVYYSGEIIRAATTSPARDNYFMRWLSDLRET |
| 预测分子量 | 37.5 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D8L重组蛋白的虚构参考文献示例(非真实文献，仅供格式参考)：
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1. **文献名称**: *Expression and Purification of Recombinant D8L Protein in Prokaryotic Systems*
**作者**: Zhang, L. et al.
**摘要**: 本研究利用大肠杆菌原核表达系统成功表达并纯化了牛痘病毒D8L重组蛋白，优化了表达条件，验证了其抗原性，为后续疫苗开发提供了基础。
2. **文献名称**: *Structural Analysis of D8L Protein Reveals Its Role in Viral Attachment*
**作者**: Smith, J.R. & Müller, K.
**摘要**: 通过X射线晶体学解析D8L重组蛋白的三维结构，揭示了其与宿主细胞表面硫酸乙酰肝素结合的分子机制，为抗病毒药物设计提供结构依据。
3. **文献名称**: *D8L Recombinant Protein as a Diagnostic Antigen for Orthopoxvirus Detection*
**作者**: Gupta, S. et al.
**摘要**: 评估D8L重组蛋白作为诊断抗原的敏感性，开发出基于ELISA的检测方法，可特异性识别正痘病毒属感染，适用于流行病学筛查。
4. **文献名称**: *Immunogenicity of D8L-based Subunit Vaccine against Vaccinia Virus*
**作者**: Li, X. et al.
**摘要**: 在小鼠模型中验证D8L重组蛋白亚单位疫苗的免疫原性，结果显示其诱导高水平中和抗体，显著降低病毒载量，具有潜在临床价值。
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注：以上内容为模拟生成，实际文献需通过学术数据库(如PubMed、Web of Science)检索确认。
The D8L recombinant protein is derived from the vaccinia virus, a member of the Orthopoxvirus genus, which gained prominence as the live vaccine strain used to eradicate smallpox. D8L is a key viral envelope protein involved in host cell attachment and entry. Structurally, it belongs to the poxvirus A-type inclusion (ATI) protein family and contains a conserved N-terminal domain with lectin-like properties. This domain facilitates binding to cell surface glycosaminoglycans (GAGs), such as heparan sulfate, enabling viral adsorption to susceptible cells.
Recombinant D8L is typically produced using expression systems like Escherichia coli or mammalian cell cultures, followed by purification via affinity chromatography. Its soluble, truncated form retains receptor-binding functionality while avoiding viral replication risks, making it valuable for studying poxvirus entry mechanisms. Researchers utilize D8L to map host-pathogen interactions, screen antiviral compounds, and develop subunit vaccines targeting orthopoxviruses, including monkeypox and variola.
In recent years, D8L has gained renewed attention due to concerns about zoonotic poxvirus outbreaks. It serves as a critical antigen in serological assays for detecting prior orthopoxvirus exposure and evaluating cross-neutralizing antibody responses. Additionally, structural studies of D8L have informed the design of synthetic inhibitors that block viral attachment. Current efforts focus on optimizing its stability and immunogenicity for next-generation vaccines, leveraging platforms like virus-like particles or mRNA technology.
As a non-infectious recombinant protein, D8L provides a safe tool for both basic virology and translational applications, bridging gaps between poxvirus biology and therapeutic innovation.
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