| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CP |
| Uniprot No | P00450 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1065aa |
| 氨基酸序列 | MKILILGIFLFLCSTPAWAKEKHYYIGIIETTWDYASDHGEKKLISVDTEHSNIYLQNGPDRIGRLYKKALYLQYTDETFRTTIEKPVWLGFLGPIIKAETGDKVYVHLKNLASRPYTFHSHGITYYKEHEGAIYPDNTTDFQRADDKVYPGEQYTYMLLATEEQSPGEGDGNCVTRIYHSHIDAPKDIASGLIGPLIICKKDSLDKEKEKHIDREFVVMFSVVDENFSWYLEDNIKTYCSEPEKVDKDNEDFQESNRMYSVNGYTFGSLPGLSMCAEDRVKWYLFGMGNEVDVHAAFFHGQALTNKNYRIDTINLFPATLFDAYMVAQNPGEWMLSCQNLNHLKAGLQAFFQVQECNKSSSKDNIRGKHVRHYYIAAEEIIWNYAPSGIDIFTKENLTAPGSDSAVFFEQGTTRIGGSYKKLVYREYTDASFTNRKERGPEEEHLGILGPVIWAEVGDTIRVTFHNKGAYPLSIEPIGVRFNKNNEGTYYSPNYNPQSRSVPPSASHVAPTETFTYEWTVPKEVGPTNADPVCLAKMYYSAVEPTKDIFTGLIGPMKICKKGSLHANGRQKDVDKEFYLFPTVFDENESLLLEDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLTMCKGDSVVWYLFSAGNEADVHGIYFSGNTYLWRGERRDTANLFPQTSLTLHMWPDTEGTFNVECLTTDHYTGGMKQKYTVNQCRRQSEDSTFYLGERTYYIAAVEVEWDYSPQREWEKELHHLQEQNVSNAFLDKGEFYIGSKYKKVVYRQYTDSTFRVPVERKAEEEHLGILGPQLHADVGDKVKIIFKNMATRPYSIHAHGVQTESSTVTPTLPGETLTYVWKIPERSGAGTEDSACIPWAYYSTVDQVKDLYSGLIGPLIVCRRPYLKVFNPRRKLEFALLFLVFDENESWYLDDNIKTYSDHPEKVNKDDEEFIESNKMHAINGRMFGNLQGLTMHVGDEVNWYLMGMGNEIDLHTVHFHGHSFQYKHRGVYSSDVFDIFPGTYQTLEMFPRTPGIWLLHCHVTDHIHAGMETTYTVLQNEDTKSG |
| 预测分子量 | 122,2 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CP(衣壳蛋白)重组蛋白的3篇模拟参考文献示例，供参考：
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1. **文献名称**：*Expression and Purification of Recombinant Capsid Protein of Tomato Yellow Leaf Curl Virus in E. coli*
**作者**：Zhang, L., et al.
**摘要**：本研究成功在大肠杆菌中表达了番茄黄化曲叶病毒(TYLCV)的衣壳蛋白(CP)，并通过亲和层析纯化获得高纯度重组蛋白。实验证实该蛋白可与感染植株的抗体特异性结合，为血清学检测提供了可靠抗原。
2. **文献名称**：*Assembly of Virus-like Particles Using Recombinant Hepatitis B Virus Core Protein*
**作者**：Kim, S., & Park, J.H.
**摘要**：作者利用昆虫细胞表达系统制备乙肝病毒核心抗原(HBcAg)重组蛋白，并证明其可自组装成病毒样颗粒(VLPs)。该VLPs在小鼠模型中诱导强烈的免疫应答，支持其在亚单位疫苗开发中的应用潜力。
3. **文献名称**：*Structural Analysis of Norovirus Capsid Protein by X-ray Crystallography*
**作者**：Jones, T.A., et al.
**摘要**：本研究解析了诺如病毒CP重组蛋白的晶体结构(分辨率2.8Å)，揭示了其表面受体结合域的关键氨基酸位点，为抗病毒药物设计提供了结构基础。
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**备注**：以上文献信息为模拟示例，实际引用时请通过学术数据库(如PubMed、Web of Science)核实真实文献。若需特定病毒或应用的文献，建议补充关键词进一步筛选。
**Background of CP Recombinant Proteins**
CP (Capsid Protein) recombinant proteins are engineered versions of viral structural proteins, primarily derived from the capsid components of viruses. These proteins play a critical role in viral assembly, host cell recognition, and immune evasion. With advancements in genetic engineering, CP proteins are produced recombinantly by inserting their encoding genes into expression systems (e.g., *E. coli*, yeast, or mammalian cells*), enabling large-scale, pathogen-free production.
CP recombinant proteins are widely studied for vaccine development, as they often elicit immune responses without the risk of live viral infection. For example, hepatitis B virus (HBV) surface antigen (HBsAg), a capsid-like particle, is a cornerstone of HBV vaccines. Similarly, CPs from plant viruses (e.g., *Tobacco Mosaic Virus*) are explored as biocompatible nanocarriers for drug delivery or antigen display due to their self-assembling properties.
In research, CPs serve as tools to study virus-host interactions, particle assembly mechanisms, and immune recognition. Their modularity allows functional modifications, such as embedding epitopes for diagnostic kits or attaching therapeutic molecules. Challenges include ensuring proper folding, stability, and post-translational modifications in heterologous systems.
Overall, CP recombinant proteins bridge virology, biotechnology, and medicine, offering versatile platforms for vaccines, therapeutics, and nanotechnology applications. Continued optimization of expression systems and structural engineering is expanding their potential in addressing emerging health challenges.
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