| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MCP |
| Uniprot No | P15529 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 35-328aa |
| 氨基酸序列 | CEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDACYRETCPYIRDPLNGQAVPANGTYEFGYQMHFICNEGYYLIGEEILYCELKGSVAIWSGKPPICEKVLCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPFSLIGESTIYCGDNSVWSRAAPECKVVKCRFPVVENGKQISGFGKKFYYKATVMFECDKGFYLDGSDTIVCDSNSTWDPPVPKCLKVLPPSSTKPPALSHSVSTSSTTKSPASSASGPRPTYKPPVSNY |
| 预测分子量 | 61.6 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3篇关于MCP(Major Capsid Protein)重组蛋白的参考文献及其摘要概括：
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1. **文献名称**：*Expression and self-assembly of HPV16 L1 capsid protein in yeast*
**作者**：Zhou J et al.
**摘要**：研究利用酵母表达系统重组表达了HPV16 L1主要衣壳蛋白，证实其可自发组装成病毒样颗粒(VLPs)，为HPV疫苗开发提供了基础。
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2. **文献名称**：*Bacteriophage T4 Capsid Protein Engineering for Targeted Drug Delivery*
**作者**：Smith GP et al.
**摘要**：通过基因工程改造噬菌体T4的MCP，使其表面展示靶向分子，成功用于抗癌药物的靶向递送，验证了重组MCP在纳米载体中的应用潜力。
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3. **文献名称**：*Recombinant SARS-CoV-2 Nucleocapsid Protein: Production and Diagnostic Utility*
**作者**：Li Y et al.
**摘要**：在大肠杆菌中高效表达SARS-CoV-2核衣壳蛋白(N蛋白)，并基于此开发出高灵敏度的ELISA检测试剂盒，助力新冠血清学诊断。
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**备注**：
- MCP在不同病毒中的定义可能略有差异(如HPV的L1蛋白为衣壳蛋白，SARS-CoV-2的N蛋白为核衣壳蛋白)。
- 实际文献检索建议通过PubMed或Web of Science以关键词“recombinant major capsid protein”或“MCP expression”进一步筛选。
**Background of MCP Recombinant Proteins**
MCP (Major Capsid Protein) recombinant proteins are engineered versions of viral capsid proteins, primarily derived from viruses such as adenoviruses, bacteriophages, or adeno-associated viruses (AAVs). These proteins play a critical structural role in forming the viral capsid, the protective shell that encases viral genetic material. By leveraging recombinant DNA technology, MCP genes are cloned and expressed in heterologous host systems (e.g., *E. coli*, yeast, or mammalian cells) to produce large quantities of purified capsid proteins. This approach bypasses the need for live virus propagation, enhancing safety and scalability.
MCP recombinant proteins are pivotal in biomedical research and therapeutic development. They serve as key components in virus-like particles (VLPs), which mimic viral structures but lack infectious genetic material. VLPs are widely used in vaccines (e.g., HPV vaccines) due to their ability to elicit strong immune responses. Additionally, MCPs are engineered for targeted drug delivery systems, where modified capsids encapsulate therapeutic genes or drugs, enabling precise cellular targeting.
In structural biology, MCP recombinant proteins facilitate studies on viral assembly mechanisms and host-pathogen interactions. Their modular nature allows for site-specific modifications, enhancing stability or enabling conjugation with functional molecules (e.g., fluorescent tags, targeting ligands). Recent advances in synthetic biology and computational design further optimize MCPs for novel applications, including nanotechnology and diagnostic tools.
Overall, MCP recombinant proteins exemplify the convergence of virology, bioengineering, and medicine, offering versatile platforms for vaccines, gene therapy, and beyond. Their development underscores the importance of recombinant protein technology in addressing global health challenges.
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