| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | 5a |
| Uniprot No | P47898 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-357aa |
| 氨基酸序列 | MDLPVNLTSFSLSTPSPLETNHSLGKDDLRPSSPLLSVFGVLILTLLGFLVAATFAWNLLVLATILRVRTFHRVPHNLVASMAVSDVLVAALVMPLSLVHELSGRRWQLGRRLCQLWIACDVLCCTASIWNVTAIALDRYWSITRHMEYTLRTRKCVSNVMIALTWALSAVISLAPLLFGWGETYSEGSEECQVSREPSYAVFSTVGAFYLPLCVVLFVYWKIYKAAKFRVGSRKTNSVSPISEAVEVKDSAKQPQMVFTVRHATVTFQPEGDTWREQKEQRAALMVGILIGVFVLCWIPFFLTELISPLCSCDIPAIWKSIFLWLGYSNSFFNPLIYTAFNKNYNSAFKNFFSRQH |
| 预测分子量 | 40,2 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5a重组蛋白的3条参考文献示例(内容基于假设性研究，仅供参考)：
---
1. **文献名称**：Structural Characterization of SARS-CoV-2 ORF5a Protein Expressed in E. coli
**作者**：Smith J. et al.
**摘要**：本研究利用大肠杆菌系统成功表达并纯化了SARS-CoV-2 ORF5a重组蛋白，通过X射线晶体学解析了其三维结构，揭示了该蛋白与宿主细胞膜相互作用的潜在机制。
---
2. **文献名称**：Functional Analysis of Recombinant 5a Protein in Viral Pathogenesis
**作者**：Zhang L. et al.
**摘要**：通过体外实验验证了重组5a蛋白在调控宿主免疫反应中的功能，发现其能抑制干扰素信号通路，为开发靶向抗病毒药物提供了理论依据。
---
3. **文献名称**：High-Yield Production of Recombinant 5a Protein Using Mammalian Expression Systems
**作者**：Kim S. et al.
**摘要**：优化哺乳动物细胞表达系统，显著提高了重组5a蛋白的产量和稳定性，并证实其在诊断试剂开发中的高抗原性和特异性。
---
注：以上文献为示例性质，实际研究中请参考真实发表的学术论文。建议通过PubMed、Google Scholar等平台检索关键词如“recombinant 5a protein”或“ORF5a expression”获取具体文献。
**Background of 5a Recombinant Protein**
Recombinant proteins, engineered through genetic modification, are pivotal tools in biomedical research and therapeutic development. The 5a recombinant protein, a specific variant of a target protein, is typically designed to enhance stability, solubility, or functional properties compared to its native or earlier versions. Its development aligns with advances in molecular cloning, codon optimization, and expression system engineering, which collectively address challenges like low yield, misfolding, or post-translational modification deficiencies observed in traditional protein production.
The 5a variant often emerges from iterative optimization processes. For instance, in viral protein research (e.g., SARS-CoV-2 spike protein), modifications such as proline-stabilization or truncation of hydrophobic regions may be introduced to improve structural integrity and antigenic performance. Such adaptations make 5a recombinant proteins valuable in vaccine development, serological assays, and receptor-binding studies.
Expression systems for 5a recombinant proteins vary depending on the application. Mammalian systems (e.g., HEK293 or CHO cells) are preferred for producing glycosylated proteins that mimic natural conformations, while prokaryotic systems (e.g., *E. coli*) offer cost-effective solutions for non-glycosylated proteins. Post-purification, techniques like SDS-PAGE, Western blotting, and surface plasmon resonance (SPR) validate purity, specificity, and functional activity.
In therapeutics, 5a recombinant proteins may serve as biologics (e.g., monoclonal antibodies, cytokines) or diagnostic antigens. Their role in structural biology—enabling X-ray crystallography or cryo-EM studies—has also accelerated drug discovery. Despite challenges in scalability and immunogenicity risks, ongoing innovations in synthetic biology and AI-driven protein design continue to refine the utility of 5a recombinant proteins across science and medicine.
×
