| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HCV-Core |
| Uniprot No | Q8TC12 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-318aa |
| 氨基酸序列 | PQIRKMLSSGVCTSTVQLPGKVVVVTGANTGIGKETAKELAQRGARVYLACRDVEKGELVAKEIQTTTGNQQVLVRKLDLSDTKSIRAFAKGFLAEEKHLHVLINNAGVMMCPYSKTADGFEMHIGVNHLGHFLLTHLLLEKLKESAPSRIVNVSSLAHHLGRIHFHNLQGEKFYNAGLAYCHSKLANILFTQELARRLKGSGVTTYSVHPGTVQSELVRHSSFMRWMWWLFSFFIKTPQQGAQTSLHCALTEGLEILSGNHFSDCHVAWVSAQARNETIARRLWDVSCDLLGLPID |
| 预测分子量 | 49.0kDa |
| 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3篇关于HCV-Core重组蛋白的代表性文献示例(注：文献信息为模拟示例，非真实存在)：
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1. **文献名称**：Expression and Purification of Recombinant HCV Core Protein for Serological Diagnosis
**作者**：Smith A, et al.
**摘要**：本研究成功在大肠杆菌中表达并纯化HCV-Core重组蛋白，验证其抗原性可用于ELISA检测，显著提高HCV抗体检测的特异性和敏感性，为临床诊断提供可靠工具。
2. **文献名称**：Structural Characterization of HCV Core Protein and Its Interaction with Host Lipids
**作者**：Zhang L, et al.
**摘要**：通过X射线晶体学解析HCV-Core重组蛋白结构，发现其N端结构域与宿主细胞脂滴结合的关键位点，揭示病毒组装机制，为抗病毒药物设计提供靶点。
3. **文献名称**：HCV Core Recombinant Protein Induces Immune Response in Mouse Models
**作者**：Tanaka K, et al.
**摘要**：在小鼠模型中评估HCV-Core重组蛋白的免疫原性，证实其可激活特异性T细胞和抗体反应，提示其在HCV疫苗开发中的潜在应用价值。
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如需真实文献，建议检索PubMed或Google Scholar，关键词："HCV Core recombinant protein"+"expression/diagnostic/vaccine"。
The hepatitis C virus (HCV) core protein is a structural component of the HCV virion, encoded by the highly conserved 5' end of the viral genome. As the first protein synthesized during viral replication, it plays a critical role in viral assembly and host interactions. The mature core protein consists of approximately 191 amino acids (∼21 kDa) and contains three conserved domains: a hydrophilic N-terminal domain involved in RNA binding, a C-terminal hydrophobic signal sequence for membrane anchoring, and a central intrinsically disordered region mediating protein-protein interactions.
Recombinant HCV core protein is typically produced using heterologous expression systems (e.g., E. coli, yeast, or mammalian cells) for research and diagnostic applications. Its production has enabled significant advances in understanding HCV biology, particularly its roles in immune evasion, lipid metabolism modulation, and potential oncogenic properties through interactions with host cell pathways. The protein's antigenic properties make it valuable for developing serological assays to detect HCV-specific antibodies in patient samples.
Structural studies using recombinant core protein have revealed its ability to form nucleocapsid-like particles and interact with viral RNA. However, challenges remain in maintaining proper conformation during recombinant production due to the protein's inherent hydrophobicity and tendency to aggregate. Researchers often employ solubility tags (e.g., GST, His-tag) or alternative expression strategies to overcome these limitations.
Current applications extend to vaccine development, as the core protein contains conserved T-cell epitopes that may elicit cross-genotypic immune responses. Its role in diagnostic test development remains crucial, particularly in differentiating acute and chronic infections. Ongoing research continues to explore core protein's interactions with host factors like lipid droplets and its potential as a therapeutic target, despite not being directly inhibited by current direct-acting antivirals.
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