| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | D13L |
| Uniprot No | P68441 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-230aa |
| 氨基酸序列 | MNNTIINSLIGGDDSIKRSNVFAVDSQIPTLYMPQYISLSGVMTNDGPDNQAIASFEIRDQYITALNHLVLSLELPEVKGMGRFGYVPYVGYKCINHVSISSCNGVIWEIEGEELYNNCINNTIALKHSGYSSELNDISIGLTPNDTIKEPSTVYVYIKTPFDVEDTFSSLKLSDSKITVTVTFNPVSDIVIRDSSFDFETFNKEFVYVPELSFIGYMVKNVQIKPSFIE |
| 预测分子量 | 33.2 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D13L重组蛋白的模拟参考文献示例(注：部分内容为假设性概括，实际文献需通过学术数据库验证)：
1. **文献名称**: "Structural characterization of the vaccinia virus D13L recombinant protein as a key scaffold in viral assembly"
**作者**: Smith A, et al.
**摘要**: 本研究利用重组技术表达并纯化了痘苗病毒D13L蛋白，通过冷冻电镜解析其三维结构，揭示了其在病毒粒子组装过程中形成的晶格结构对膜形态发生的关键作用。
2. **文献名称**: "Functional analysis of D13L recombinant protein in poxvirus replication inhibition"
**作者**: Chen L, et al.
**摘要**: 通过体外实验证实重组D13L蛋白可与病毒膜结构结合，干扰痘病毒早期包膜形成，为基于D13L靶点的新型抗病毒药物开发提供了理论依据。
3. **文献名称**: "D13L recombinant protein as a novel vaccine adjuvant: enhancing immune responses in murine models"
**作者**: González R, et al.
**摘要**: 将重组D13L蛋白作为佐剂与流感疫苗联用，在小鼠模型中观察到显著增强的Th1型免疫应答，提示其在疫苗研发中的潜在应用价值。
4. **文献名称**: "Expression optimization and purification of D13L recombinant protein in E. coli for antigenic studies"
**作者**: Wang X, et al.
**摘要**: 报道了在大肠杆菌系统中高效表达可溶性D13L重组蛋白的工艺优化，经Western blot验证其与天花病毒感染者血清抗体的特异性结合能力。
**注意**：以上文献信息为基于领域知识的模拟生成，实际研究中请通过PubMed、Web of Science等平台以关键词"D13L recombinant protein"+"vaccinia"或结合具体研究方向检索最新文献。
D13L recombinant protein is derived from the vaccinia virus (VACV), a member of the Poxviridae family. The D13L gene encodes the D13 protein, a major structural component critical for virion morphogenesis. Discovered as a key player in viral assembly, D13 forms a hexagonal lattice scaffolding that shapes the immature virion (IV) during the early stages of VACV replication. Its structural role was elucidated through cryo-electron microscopy and crystallography studies, revealing its resemblance to capsid proteins of icosahedral viruses, despite poxviruses lacking a traditional capsid.
The D13 protein is a 62 kDa polypeptide that oligomerizes into trimers, creating a curved scaffold to guide membrane curvature and IV formation. It interacts with viral membrane proteins (e.g., A36) and the viral A32 ATPase, coordinating membrane remodeling and genome packaging. Notably, D13 is dispensable for viral replication but essential for producing infectious mature virions (MV), making it a target for antiviral strategies. Rifampicin, a well-known antibiotic, inhibits VACV assembly by binding to D13. underscoring its functional significance.
Recombinant D13L protein is produced via heterologous expression systems (e.g., E. coli or baculovirus) for structural and functional studies. It serves as a tool to investigate poxvirus assembly mechanisms, screen antiviral compounds, and develop vaccines. As VACV is closely related to variola virus (the causative agent of smallpox), understanding D13's role has implications for combating orthopoxvirus infections. Additionally, recombinant D13 is used in antibody production for diagnostic assays and as an antigen in subunit vaccine research. Its conserved nature across poxviruses makes it a valuable target for broad-spectrum antiviral research, bridging fundamental virology and translational applications.
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