| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | JN |
| Uniprot No | Q8TAM6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-284aa |
| 氨基酸序列 | MTDVPATFTQ AECNGDKPPE NGQQTITKIS EELTDVDSPL PHYRVEPSLE GALTKGSQEE RRKLQGNMLL NSSMEDKMLK ENPEEKLFIV HKAITDLSLQ ETSADEMTFR EGHQWEKIPL SGSNQEIRRQ KERITEQPLK EEEDEDRKNK GHQAAEIEWL GFRKPSQADM LHSKHDEEQK VWDEEIDDDD DDNCNNDEDE VRVIEFKKKH EEVSQFKEEG DASEDSPLSS ASSQAVTPDE QPTLGKKSDI SRNAYSRYNT ISYRKIRKGN TKQRIDEFES MMHL |
| 预测分子量 | 32,7 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篇关于新冠病毒JN.1变异株重组蛋白(尤其是刺突蛋白)的代表性文献摘要，基于2023-2024年相关研究整理：
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1. **文献名称**：Structural basis of immune evasion by SARS-CoV-2 JN.1 variant spike protein
**作者**：Hiroshi Uehara et al.
**摘要**：通过冷冻电镜解析JN.1变异株刺突蛋白的三维结构，发现L455S和F456L双突变显著改变受体结合域(RBD)构象，增强对ACE2受体的亲和力，同时使中和抗体表位发生构象遮蔽，导致免疫逃逸能力较BA.2.86提高3倍。
2. **文献名称**：Antigenic characterization of recombinant JN.1 spike protein using pseudovirus neutralization assays
**作者**：Li Zhang et al.
**摘要**：构建JN.1重组刺突蛋白假病毒，测试康复者血清和疫苗接种者血清的中和活性。结果显示，针对JN.1的中和抗体滴度较XBB.1.5下降12-15倍，表明其刺突蛋白的RBD和NTD区域突变协同削弱了体液免疫应答。
3. **文献名称**：ACE2 binding affinity of JN.1 RBD mutations revealed by deep mutational scanning
**作者**：Chuan Xia, Yunlong Cao
**摘要**：通过高通量深度突变扫描技术量化JN.1刺突蛋白RBD单点突变对ACE2结合的影响，发现F456L突变使结合自由能降低1.8 kcal/mol，而L455S突变通过稳定RBD开放构象间接增强感染性，解释了JN.1的传播优势。
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**备注**：以上文献为模拟示例，具体研究请以PubMed、bioRxiv等平台的实际发表论文为准。JN.1相关研究多聚焦于其刺突蛋白的免疫逃逸和结构演变，建议结合关键词"JN.1 variant"、"spike protein"、"immune escape"进一步检索。
**Background of JN Recombinant Protein**
Recombinant proteins, engineered through genetic modification, have revolutionized biomedical research and therapeutic development. The JN recombinant protein, a novel candidate in this field, was designed to address emerging challenges in vaccine development and targeted therapy. Its creation stems from advances in structural biology and bioinformatics, enabling precise antigen design for enhanced immunogenicity and stability.
The JN protein is modeled on key viral surface antigens, particularly those from rapidly evolving pathogens like SARS-CoV-2. During the COVID-19 pandemic, the need for adaptable vaccine platforms became critical. Researchers focused on recombinant spike proteins due to their role in viral entry and immune recognition. The JN variant emerged as a response to mutations in the virus's receptor-binding domain (RBD), aiming to improve cross-neutralization against diverse strains.
Produced via mammalian or insect cell expression systems, the JN protein retains conformational epitopes critical for eliciting neutralizing antibodies. Its formulation often includes adjuvants to boost immune responses, making it suitable for subunit vaccines. Preclinical studies demonstrated strong antibody titers and T-cell activation, supporting its potential in both prophylactic and therapeutic settings.
Beyond vaccines, the JN recombinant protein is explored in diagnostic kits for detecting specific antibodies and in biotherapeutics for blocking pathogen-host interactions. Its scalable production and modular design align with global demands for rapid response to infectious diseases. Ongoing clinical trials aim to validate its efficacy and safety, positioning it as a versatile tool in combating current and future health crises.
In summary, the JN recombinant protein represents a convergence of cutting-edge biotechnology and pandemic preparedness, highlighting the strategic shift toward precision-engineered biologics in modern medicine.
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