| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | YJEFN3 |
| Uniprot No | A6XGL0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-299aa |
| 氨基酸序列 | MSSAAGPDPSEAPEERHFLRALELQPPLADMGRAELSSNATTSLVQRRKQAWGRQSWLEQIWNAGPVCQSTAEAAALERELLEDYRFGRQQLVELCGHASAVAVTKAFPLPALSRKQRTVLVVCGPEQNGAVGLVCARHLRVFEYEPTIFYPTRSLDLLHRDLTTQCEKMDIPFLSYLPTEVQLINEAYGLVVDAVLGPGVEPGEVGGPCTRALATLKLLSIPLVSLDIPSGWDAETGSDSEDGLRPDVLVSLAAPKRCAGRFSGRHHFVAGRFVPDDVRRKFALRLPGYTGTDCVAAL |
| 预测分子量 | 32.6 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. |
以下是基于常见重组蛋白研究模拟的示例文献(请注意，这些为虚构内容，实际文献需通过学术数据库检索)：
1. **文献名称**：Structural and Functional Characterization of Recombinant YJEFN3 Protein
**作者**：Zhang L, et al.
**摘要**：本研究通过大肠杆菌系统表达并纯化了YJEFN3重组蛋白，利用X射线晶体学解析其三维结构，揭示了FN3结构域的关键功能位点，为靶向药物设计提供依据。
2. **文献名称**：YJEFN3 Recombinant Protein Enhances Neurite Outgrowth in vitro
**作者**：Kim S, et al.
**摘要**：研究发现，YJEFN3重组蛋白通过激活PI3K/Akt信号通路促进神经元突触生长，提示其在神经修复治疗中的潜在应用价值。
3. **文献名称**：High-Yield Production of YJEFN3 via Yeast Expression System
**作者**：Wang Y, et al.
**摘要**：采用毕赤酵母表达系统优化YJEFN3的分泌表达，实现高产量(>200 mg/L)和低内毒素水平，为规模化制备奠定基础。
4. **文献名称**：YJEFN3 as a Biomarker in Colorectal Cancer Progression
**作者**：Garcia R, et al.
**摘要**：通过ELISA检测发现，YJEFN3在结直肠癌患者血清中显著高表达，且与肿瘤转移呈正相关，或可作为新型诊断标志物。
**注意事项**：
- 以上为模拟文献，实际研究中请通过PubMed、Web of Science等平台检索真实文献(关键词：YJEFN3 recombinant protein)。
- 若名称存在拼写误差(如实际为YJE1、FN3融合蛋白等)，建议结合基因编号(如UniProt ID)精准检索。
**Background of YJEFN3 Recombinant Protein**
The YJEFN3 recombinant protein is a engineered fusion protein designed for biomedical research and therapeutic development. Its name derives from the combination of functional domains: "YJE" likely references a catalytic or receptor-binding module, while "FN3" denotes the fibronectin type III (FN3) domain, a stable β-sandwich structural motif commonly found in cell adhesion proteins and extracellular matrix interactions. The FN3 domain is often utilized as a scaffold for protein engineering due to its stability, solubility, and versatility in binding epitopes.
YJEFN3 is typically produced via recombinant DNA technology, expressed in prokaryotic (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian cells) to ensure proper folding and post-translational modifications. Its design aims to harness the targeting specificity of the YJE component—potentially derived from antibodies, cytokines, or signaling proteins—and the structural robustness of FN3. This combination enhances pharmacokinetic properties, such as serum half-life and tissue penetration, making it suitable for applications in diagnostics, targeted drug delivery, or as a therapeutic biologic.
Research involving YJEFN3 often focuses on its interaction with cellular receptors or pathogenic targets, leveraging its dual-domain architecture to modulate signaling pathways or neutralize disease-associated molecules. For instance, in oncology, similar recombinant proteins are explored to block tumor growth factors or immune checkpoints. In infectious diseases, they may serve as decoy receptors to inhibit viral entry.
The development of YJEFN3 aligns with advancements in protein engineering, emphasizing modularity and multifunctionality. Its characterization typically involves biophysical assays (e.g., SPR, ELISA) to validate binding affinity, alongside functional studies in cellular or animal models to assess efficacy and safety. As with many recombinant proteins, scalability, immunogenicity, and cost-effective production remain critical considerations for translational success.
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