| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EFNB3 |
| Uniprot No | Q15768 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-226aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMLSLEP VYWNSANKRF QAEGGYVLYP QIGDRLDLLC PRARPPGPHS SPNYEFYKLY LVGGAQGRRC EAPPAPNLLL TCDRPDLDLR FTIKFQEYSP NLWGHEFRSH HDYYIIATSD GTREGLESLQ GGVCLTRGMK VLLRVGQSPR GGAVPRKPVS EMPMERDRGA AHSLEPGKEN LPGDPTSNAT SRGAEGPLPP PSMP |
| 预测分子量 | 25 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EFNB3重组蛋白的示例参考文献(注：以下内容为模拟虚构，建议通过学术数据库获取真实文献)：
---
1. **标题**: *"Recombinant EFNB3 protein promotes axon guidance via Eph receptor signaling"*
**作者**: Zhang L, et al.
**摘要**: 本研究通过大肠杆菌系统成功表达并纯化了EFNB3重组蛋白，验证了其与EphA4受体的特异性结合能力。体外实验表明，EFNB3重组蛋白可诱导神经元生长锥塌陷，提示其在轴突导向中的关键作用。
2. **标题**: *"Structural and functional characterization of human EFNB3 extracellular domain"*
**作者**: Kim S, Park JH.
**摘要**: 作者利用哺乳动物表达系统制备了EFNB3胞外域重组蛋白，通过X射线晶体学解析其三维结构，并证实其通过β-折叠片层介导受体二聚化，为靶向Ephrin信号通路的药物设计提供依据。
3. **标题**: *"EFNB3 recombinant protein suppresses breast cancer cell invasion in vitro"*
**作者**: Chen R, et al.
**摘要**: 研究显示，通过昆虫细胞表达系统获得的EFNB3重组蛋白可显著抑制乳腺癌细胞迁移和侵袭，其机制可能与下调基质金属蛋白酶(MMP-9)表达及阻断上皮-间质转化(EMT)相关。
---
**建议**：如需真实文献，请使用PubMed、Web of Science等平台，以关键词“EFNB3 recombinant protein”或“Ephrin-B3 recombinant”检索最新研究。
Ephrin-B3 (EFNB3) is a member of the ephrin protein family, which plays critical roles in cell-cell communication, tissue patterning, and developmental processes. As a transmembrane ligand, EFNB3 interacts with Eph receptors, a subclass of receptor tyrosine kinases, to mediate bidirectional signaling. This interaction regulates diverse biological functions, including axon guidance, angiogenesis, and cell adhesion. EFNB3 is particularly notable for its involvement in nervous system development, where it contributes to neural crest cell migration, synaptic plasticity, and boundary formation in the brain. Dysregulation of EFNB3 has been implicated in pathological conditions such as cancer metastasis, neurological disorders, and vascular abnormalities.
Recombinant EFNB3 protein is engineered to study its structure, signaling mechanisms, and therapeutic potential. Produced via heterologous expression systems (e.g., mammalian cells or *E. coli*), the recombinant form typically retains functional domains, including the receptor-binding ephrin domain and conserved tyrosine residues. Researchers often use soluble variants (e.g., EFNB3-Fc fusion proteins) to investigate receptor-ligand interactions without membrane anchoring. These tools enable *in vitro* assays (e.g., cell migration or neurite outgrowth studies) and *in vivo* models to explore EFNB3's role in tissue repair or disease progression.
Current studies focus on EFNB3's dual role in cancer—promoting tumor suppression via receptor binding or facilitating invasiveness through alternative pathways. Its recombinant form also serves as a potential therapeutic agent for nerve regeneration or angiogenesis modulation. However, challenges remain in optimizing protein stability, avoiding off-target effects, and deciphering context-dependent signaling outcomes. Advances in structural biology and protein engineering continue to refine EFNB3 recombinant tools, enhancing their utility in both basic research and translational applications.
×
