| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EFNB1 |
| Uniprot No | P98172 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-232aa |
| 氨基酸序列 | LAKNLEPVSWSSLNPKFLSGKGLVIYPKIGDKLDIICPRAEAGRPYEYYK LYLVRPEQAAACSTVLDPNVLVTCNRPEQEIRFTIKFQEFSPNYMGLEFK KHHDYYITSTSNGSLEGLENREGGVCRTRTMKIIMKVGQDPNAVTPEQLT TSRPSKEADNTVKMATQAPGSRGSLGDSDGKHETVNQEEKSGPGASGGSS GDPDG |
| 预测分子量 | 23 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EFNB1重组蛋白的3篇参考文献示例(文献信息为模拟概括，非真实存在)：
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1. **标题**: "Structural insights into Ephrin-B1 signaling through recombinant protein crystallography"
**作者**: Smith A, et al.
**摘要**: 通过X射线晶体学解析了重组EFNB1胞外域与EphB2受体复合物的三维结构，揭示了其界面关键氨基酸残基，为靶向Eph-ephrin相互作用的药物设计提供依据。
2. **标题**: "Recombinant EFNB1-Fc fusion protein inhibits angiogenesis in tumor models"
**作者**: Chen L, et al.
**摘要**: 研究利用哺乳动物细胞表达系统制备EFNB1-Fc重组融合蛋白，证明其通过反向信号通路抑制体外血管内皮细胞迁移，并在小鼠肿瘤模型中显著减少血管生成和肿瘤生长。
3. **标题**: "Functional characterization of EFNB1 mutations using recombinant protein assays"
**作者**: Gupta R, et al.
**摘要**: 通过大肠杆菌表达纯化野生型和突变型EFNB1重组蛋白，结合细胞黏附实验，发现某些遗传病相关突变会破坏其与Eph受体的结合能力，导致信号传导异常。
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如需真实文献，建议在PubMed等数据库检索关键词：**EFNB1 recombinant protein, Ephrin-B1 expression, Eph-ephrin signaling**。
Ephrin-B1 (EFNB1) is a member of the ephrin protein family, which plays critical roles in cell-cell communication during development and tissue homeostasis. As a transmembrane ligand, EFNB1 binds to Eph receptors (primarily EphB subtypes), initiating bidirectional signaling pathways that regulate cell adhesion, migration, and tissue boundary formation. Unlike GPI-anchored ephrin-A proteins, EFNB1 contains a cytoplasmic domain enabling reverse signaling, influencing cytoskeletal dynamics and gene expression in ligand-expressing cells.
Recombinant EFNB1 proteins are engineered to mimic native protein functions for research and therapeutic applications. These proteins typically include the extracellular domain responsible for receptor binding, often fused to tags (e.g., Fc or His tags) for purification and detection. Produced in mammalian expression systems like HEK293 or CHO cells, they retain post-translational modifications essential for receptor interaction.
In biomedical research, recombinant EFNB1 is used to study axon guidance, angiogenesis, and cancer progression, where EFNB1-EphB interactions modulate tumor invasiveness and vascular remodeling. It also serves as a tool to investigate congenital disorders, as EFNB1 mutations cause craniofrontonasal syndrome, characterized by craniofacial and skeletal abnormalities. Therapeutic exploration includes targeting EFNB1 signaling in pathological angiogenesis or designing fusion proteins to modulate neural regeneration. Quality control involves verifying receptor-binding activity through ELISA or cell-based assays, ensuring biological relevance in experimental models.
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