| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Cap |
| Uniprot No | P35237 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-376aa |
| 氨基酸序列 | MDVLAEANGT FALNLLKTLG KDNSKNVFFS PMSMSCALAM VYMGAKGNTA AQMAQILSFN KSGGGGDIHQ GFQSLLTEVN KTGTQYLLRM ANRLFGEKSC DFLSSFRDSC QKFYQAEMEE LDFISAVEKS RKHINTWVAE KTEGKIAELL SPGSVDPLTR LVLVNAVYFR GNWDEQFDKE NTEERLFKVS KNEEKPVQMM FKQSTFKKTY IGEIFTQILV LPYVGKELNM IIMLPDETTD LRTVEKELTY EKFVEWTRLD MMDEEEVEVS LPRFKLEESY DMESVLRNLG MTDAFELGKA DFSGMSQTDL SLSKVVHKSF VEVNEEGTEA AAATAAIMMM RCARFVPRFC ADHPFLFFIQ HSKTNGILFC GRFSSP |
| 预测分子量 | 43 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. |
以下是关于重组Cap蛋白的3篇参考文献示例(注：部分信息为示例性描述，实际引用时请核实文献真实性)：
1. **《Prokaryotic expression and purification of PCV2 Cap protein for vaccine development》**
作者：Zhang L, et al.
摘要：研究利用大肠杆菌系统表达猪圆环病毒2型(PCV2)Cap重组蛋白，优化纯化工艺，证实其可形成病毒样颗粒(VLPs)，并展示出良好的免疫原性，为亚单位疫苗开发提供基础。
2. **《SARS-CoV-2 Nucleocapsid protein: Expression in insect cells and serodiagnostic potential》**
作者：Chen X, et al.
摘要：通过杆状病毒-昆虫细胞系统高效表达SARS-CoV-2核衣壳(Cap)蛋白，建立基于该重组蛋白的ELISA检测方法，验证其在COVID-19血清学诊断中的高灵敏度和特异性。
3. **《Structural analysis of FMDV capsid protein using cryo-EM》**
作者：Wang Y, et al.
摘要：通过冷冻电镜解析口蹄疫病毒(FMDV)重组Cap蛋白的原子结构，揭示其与中和抗体的结合表位，为新型多表位疫苗设计提供结构生物学依据。
注：以上文献标题及内容为示例性质，实际研究请参考PubMed、Web of Science等数据库的权威论文。
**Background of Cap Recombinant Proteins**
Cap recombinant proteins, often derived from viral capsid proteins, play a critical role in biomedical research and therapeutic development. Capsid proteins are structural components of viruses, forming protective shells (capsids) that encapsulate viral genetic material. Recombinant versions are engineered using genetic cloning techniques, enabling large-scale production in heterologous systems like *E. coli*, yeast, or mammalian cells. These proteins retain key structural and functional features of native capsids but are non-infectious due to the absence of viral genomes.
A prominent example is the SARS-CoV-2 Spike (S) protein, a cap-related recombinant protein used in COVID-19 vaccine development. The S protein mediates viral entry by binding to host receptors, making it a prime target for vaccines and therapeutics. Recombinant S proteins are designed to mimic native conformations, eliciting neutralizing antibodies without exposing individuals to live viruses. Similar strategies apply to other viruses, including influenza, HIV, and adeno-associated viruses (AAVs).
In gene therapy, recombinant capsid proteins from AAVs are engineered to improve tissue targeting and evade pre-existing immunity. Modifications in capsid sequences (e.g., directed evolution or rational design) enhance delivery efficiency and safety. Beyond vaccines and gene therapy, cap recombinant proteins are used in diagnostic assays, antiviral drug screening, and structural studies to decipher viral entry mechanisms.
Challenges include maintaining proper protein folding, post-translational modifications (e.g., glycosylation), and stability during production. Advances in expression systems, purification techniques, and computational modeling continue to address these limitations, expanding applications in virology and precision medicine. Overall, cap recombinant proteins represent versatile tools for understanding viral pathogenesis and developing targeted interventions.
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