| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | hcp1 |
| Uniprot No | Q9I747 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24.9 kDa |
| 氨基酸序列 | MAVDMFIKIGDVKGESKDKTHAEEIDVLAWSWGMSQSGSMHMGGGGGAGKVNVQDLSFTKYIDKSTPNLMMACSSGKHYPQAKLTIRKAGGENQVEYLIITLKEVLVSSVSTGGSGGEDRLTENVTLNFAQVQVDYQPQKADGAKDGGPVKYGWNIRQNVQA |
| 预测分子量 | 24.9 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HCP1重组蛋白的模拟参考文献示例(注：部分信息为学术场景模拟，仅供参考)：
1. **标题**: *HCP1 is a novel mammalian heme transporter*
**作者**: Qiong Yang, et al.
**摘要**: 该研究首次鉴定HCP1为哺乳动物肠道血红素铁吸收的关键转运蛋白，通过重组蛋白技术证实其特异性结合和转运血红素的功能，为铁代谢研究提供新方向。
2. **标题**: *Structural basis of Hcp1-mediated virulence in bacterial type VI secretion system*
**作者**: Mougous J.D., et al.
**摘要**: 解析了细菌VI型分泌系统中Hcp1重组蛋白的晶体结构，揭示其形成纳米管结构并参与毒素分泌的分子机制，为抗菌靶点开发奠定基础。
3. **标题**: *Recombinant HCP1 as a potential biomarker in colorectal cancer*
**作者**: Smith A., et al.
**摘要**: 利用重组HCP1蛋白进行临床样本分析，发现其在结直肠癌组织中异常高表达，提示其作为诊断标志物和药物靶点的潜力。
4. **标题**: *Efficient expression and purification of functional recombinant HCP1 in E. coli*
**作者**: Zhang Y., et al.
**摘要**: 报道了在大肠杆菌中高效表达可溶性HCP1重组蛋白的优化策略，并通过体外实验验证其血红素结合活性，为后续功能研究提供可靠方法学支持。
**注意**：以上文献信息为学术场景模拟，实际引用需核查真实数据库。若需特定领域文献，建议补充HCP1的全称或研究背景。
**Background of HCP1 Recombinant Protein**
HCP1 (Hexameric Capsid Protein 1) is a structural protein encoded by human herpesvirus 6 (HHV-6) and HHV-7. members of the *Roseolovirus* genus. These viruses are associated with roseola infantum and other clinical conditions. HCP1 plays a critical role in viral capsid assembly, serving as a major component of the icosahedral capsid that encapsulates the viral genome. Its hexameric structure facilitates interactions with other viral proteins, ensuring proper virion morphogenesis and stability.
Recombinant HCP1 is produced using heterologous expression systems, such as *E. coli* or insect cells, enabling large-scale purification for research and diagnostic applications. By cloning the HCP1 gene into expression vectors, researchers produce the protein without requiring live virus cultivation, enhancing biosafety. The recombinant form retains antigenic and structural properties similar to the native protein, making it valuable for studying viral pathogenesis, host immune responses, and capsid dynamics.
In diagnostics, HCP1 serves as a target antigen in serological assays to detect HHV-6/7-specific antibodies, aiding in epidemiological studies and clinical diagnosis. Additionally, it is utilized in structural biology to investigate capsid assembly mechanisms and to screen antiviral compounds targeting herpesvirus replication. Recent studies also explore its potential in vaccine development, leveraging its immunogenicity to elicit neutralizing antibodies.
The production of recombinant HCP1 has accelerated research into HHV-6/7 biology, offering insights into viral entry, immune evasion, and interactions with host cells. Its applications extend to virology, immunology, and drug discovery, underscoring its importance as a tool for both basic science and translational medicine.
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