| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HCV-NS5a |
| Uniprot No | Q15004 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-111aa |
| 氨基酸序列 | MVRTKADSVPGTYRKVVAARAPRKVLGSSTSATNSTSVSSRKAENKYAGGNPVCVRPTPKWQKGIGEFFRLSPKDSEKENQIPEEAGSSGLGKAKRKACPLQPDHTNDEKE |
| 预测分子量 | 39.0kDa |
| 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-NS5a重组蛋白的代表性文献摘要(虚构示例，仅供格式参考)：
1. **文献名称**：*Structural characterization of HCV NS5A recombinant protein and its role in viral replication*
**作者**：Smith J, et al.
**摘要**：本研究通过大肠杆菌表达系统纯化HCV NS5A重组蛋白，利用X射线晶体学解析其三维结构，揭示NS5A蛋白的磷酸化位点及与宿主因子VAP-A的相互作用，阐明其在病毒复制复合体形成中的关键作用。
2. **文献名称**：*HCV NS5A recombinant protein enhances RNA binding and modulates interferon resistance*
**作者**：Lee S, et al.
**摘要**：通过体外实验证实重组NS5A蛋白直接结合病毒RNA，并通过抑制宿主IRF3信号通路削弱干扰素应答，为解释HCV临床耐药性提供分子机制依据。
3. **文献名称**：*Development of a high-throughput assay for NS5A inhibitors using recombinant protein*
**作者**：Wang L, et al.
**摘要**：构建基于荧光共振能量转移(FRET)的NS5A重组蛋白筛选平台，用于快速检测小分子抑制剂对NS5A二聚化的阻断效果，推动抗病毒药物研发。
(注：以上为模拟内容，实际文献需通过PubMed等数据库检索，关键词："HCV NS5A recombinant")
HCV-NS5a is a non-structural protein encoded by the hepatitis C virus (HCV), a major causative agent of chronic hepatitis, cirrhosis, and hepatocellular carcinoma. NS5a plays a critical role in viral RNA replication, assembly, and modulation of host cell pathways. It lacks enzymatic activity but serves as a multifunctional scaffold, interacting with viral RNA, other HCV proteins (like NS5b polymerase), and host factors to form the membranous web—a replication platform. NS5a exists in two phosphorylation states (basal and hyperphosphorylated), regulating the transition between replication and virion assembly. Its structure includes three domains: D1 (essential for replication), D2 (involved in interactions), and D3 (linked to particle production).
Recombinant NS5a proteins are generated via heterologous expression systems (e.g., *E. coli* or mammalian cells) for structural and functional studies. These proteins enable researchers to explore NS5a's role in the HCV lifecycle, its interaction with antivirals, and host immune evasion mechanisms. NS5a is a key drug target; direct-acting antivirals (DAAs) such as daclatasvir block its function, achieving high cure rates. However, NS5a's intrinsic disorder and conformational flexibility pose challenges in structural characterization. Recombinant versions have been instrumental in mapping drug-binding sites, understanding resistance mutations, and developing diagnostic tools. Studies using NS5a also highlight its interference with host interferon signaling, lipid metabolism, and apoptosis pathways, underscoring its dual role in viral persistence and pathogenesis. Despite therapeutic advances, research on NS5a continues to address unresolved questions about HCV's biology and resistance mechanisms.
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