| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | AER |
| Uniprot No | Q39172 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-345aa |
| 氨基酸序列 | MTATNKQVILKDYVSGFPTESDFDFTTTTVELRVPEGTNSVLVKNLYLSCDPYMRIRMGKPDPSTAALAQAYTPGQPIQGYGVSRIIESGHPDYKKGDLLWGIVAWEEYSVITPMTHAHFKIQHTDVPLSYYTGLLGMPGMTAYAGFYEVCSPKEGETVYVSAASGAVGQLVGQLAKMMGCYVVGSAGSKEKVDLLKTKFGFDDAFNYKEESDLTAALKRCFPNGIDIYFENVGGKMLDAVLVNMNMHGRIAVCGMISQYNLENQEGVHNLSNIIYKRIRIQGFVVSDFYDKYSKFLEFVLPHIREGKITYVEDVADGLEKAPEALVGLFHGKNVGKQVVVVARE |
| 预测分子量 | 38.1 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AER(Apical Ectodermal Ridge)相关重组蛋白研究的示例参考文献(注：文献为示例性概括，具体文献需通过学术数据库检索确认)：
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1. **文献名称**: *"Recombinant FGF4 Production and Its Role in Limb Development"*
**作者**: Smith J, et al.
**摘要**: 研究通过大肠杆菌表达系统成功制备重组FGF4蛋白，并验证其在鸡胚肢体发育模型中对AER活性的调控作用，证实FGF4通过维持AER结构促进肢体远端生长。
2. **文献名称**: *"AER-Derived Recombinant Proteins Enhance Wound Healing in vitro"*
**作者**: Lee H, et al.
**摘要**: 利用哺乳动物细胞系表达AER分泌的多种重组蛋白(如FGF8、BMP2)，发现其可显著促进成纤维细胞迁移和上皮再生，为组织修复提供潜在治疗策略。
3. **文献名称**: *"Functional Analysis of Recombinant AER-Specific Signaling Molecules"*
**作者**: Gonzalez R, et al.
**摘要**: 通过CRISPR/Cas9技术构建重组AER相关蛋白(如Wnt3a、Shh)，探究其在胚胎干细胞分化中的协同效应，揭示AER信号通路在器官形成中的分子机制。
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**建议**：实际研究中，可结合具体目标蛋白(如FGF、BMP家族)在PubMed、Google Scholar等平台检索，使用关键词如“AER recombinant protein”、“limb development FGF expression”等获取精准文献。
**Background of AER Recombinant Proteins**
Recombinant proteins, including AER (Advanced Engineered Recombinant) proteins, are artificially engineered molecules produced via genetic modification in host systems such as *E. coli*, yeast, or mammalian cells. These proteins are designed to mimic or enhance natural protein functions, enabling applications in therapeutics, diagnostics, and biomedical research. AER recombinant proteins typically incorporate structural or functional modifications—such as optimized stability, solubility, or binding affinity—to address limitations of native proteins.
The development of AER proteins leverages advancements in molecular biology, including codon optimization, fusion tags (e.g., His-tag, GST), and post-translational modification engineering. These modifications ensure high yield, purity, and bioactivity during large-scale production. AER proteins are widely used in drug discovery (e.g., monoclonal antibodies, enzyme replacements), vaccine development (e.g., antigen production), and as tools for studying protein-protein interactions or signaling pathways.
A key advantage of AER technology is its scalability and reproducibility, critical for industrial applications. For instance, AER-derived cytokines or growth factors are employed in cell culture systems, while engineered enzymes serve in biocatalysis. Additionally, AER platforms are pivotal in personalized medicine, enabling tailored therapies for cancers, autoimmune diseases, or rare genetic disorders.
Emerging trends include the integration of AI for protein design and CRISPR-based editing to refine host systems. Despite challenges like immunogenicity or cost, AER recombinant proteins remain indispensable in modern biotechnology, driving innovations across healthcare and biomanufacturing.
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