| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | preA |
| Uniprot No | P25889 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-411aa |
| 氨基酸序列 | MLTKDLSITFCGVKFPNPFCLSSSPVGNCYEMCAKAYDTGWGGVVFKTIGFFIANEVSPRFDHLVKEDTGFIGFKNMEQIAEHPLEENLAALRRLKEDYPDKVLIASIMGENEQQWEELARLVQEAGADMIECNFSCPQMTSHAMGSDVGQSPELVEKYCRAVKRGSTLPMLAKMTPNIGDMCEVALAAKRGGADGIAAINTVKSITNIDLNQKIGMPIVNGKSSISGYSGKAVKPIALRFIQQMRTHPELRDFPISGIGGIETWEDAAEFLLLGAATLQVTTGIMQYGYRIVEDMASGLSHYLADQGFDSLQEMVGLANNNIVPAEDLDRSYIVYPRINLDKCVGCGRCYISCYDGGHQAMEWSEKTRTPHCNTEKCVGCLLCGHVCPVGCIELGEVKFKKGEKEHPVTL |
| 预测分子量 | 52.5 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preA重组蛋白的3篇示例参考文献(内容为示例，非真实文献)：
1. **《Optimization of Recombinant PreA Protein Expression in E. coli》**
- 作者：Zhang L, et al.
- 摘要：研究通过密码子优化和诱导条件调控，提高preA重组蛋白在大肠杆菌中的可溶性表达，并通过亲和层析纯化获得高纯度蛋白，为后续功能研究奠定基础。
2. **《Structural and Functional Analysis of PreA in Neurodegenerative Disease》**
- 作者：Smith J, et al.
- 摘要：解析preA重组蛋白的晶体结构，发现其与β-淀粉样蛋白聚集的相关性，提示其在阿尔茨海默病病理中的潜在作用机制。
3. **《PreA-Based Vaccine Development Against Bacterial Infections》**
- 作者：Wang Y, et al.
- 摘要：利用重组preA蛋白作为抗原，在小鼠模型中诱导强效免疫应答，证明其在革兰氏阴性菌感染预防中的潜在应用价值。
(注：若需真实文献，建议提供更明确的“preA”定义或相关研究背景。)
**Background of Recombinant Proteins in Preclinical and Research Applications**
Recombinant proteins, engineered through genetic recombination technology, are pivotal in modern biotechnology and biomedical research. The concept emerged in the 1970s following breakthroughs in molecular cloning and DNA manipulation, enabling scientists to insert genes encoding specific proteins into host organisms (e.g., bacteria, yeast, or mammalian cells). These systems then express the desired protein, which is harvested and purified for diverse applications.
In preclinical (preA) stages, recombinant proteins serve as critical tools for drug discovery, disease modeling, and therapeutic development. They are used to study protein function, validate drug targets, and screen potential therapeutics. For instance, recombinant cytokines, growth factors, or antibodies are employed in *in vitro* and *in vivo* assays to assess efficacy, toxicity, and mechanism of action. Their high purity and specificity ensure reproducibility, a cornerstone of robust preclinical research.
The rise of personalized medicine and biologics has further amplified their importance. Recombinant proteins are integral to developing monoclonal antibodies, enzyme replacements, and vaccines, including recent advancements in mRNA-based platforms. Additionally, they facilitate structural biology studies (e.g., X-ray crystallography) to elucidate drug-protein interactions.
Challenges remain, such as optimizing expression systems for complex proteins, ensuring proper post-translational modifications, and scaling production cost-effectively. Innovations in cell-free systems, CRISPR engineering, and AI-driven protein design are addressing these hurdles, accelerating translational research.
Overall, recombinant proteins in preA phases bridge basic science and clinical application, underpinning advancements in therapeutics and our understanding of human biology. Their continued evolution promises to reshape drug development and precision medicine.
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