| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EFNA5 |
| Uniprot No | P52803 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-203aa |
| 氨基酸序列 | QDPGSKAVADRYAVYWNSSNPRFQRGDYHIDVCINDYLDVFCPHYEDSVPEDKTERYVLYMVNFDGYSACDHTSKGFKRWECNRPHSPNGPLKFSEKFQLFTPFSLGFEFRPGREYFYISSAIPDNGRRSCLKLKVFVRPTNSCMKTIGVHDRVFDVNDKVENSLEPADDTVHESAEPSRGEN |
| 预测分子量 | 50.1 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EFNA5重组蛋白的3篇参考文献，按文献名称、作者和摘要内容简要概括：
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1. **文献名称**：*Recombinant Ephrin-A5 Fusion Proteins and Their Biological Activity*
**作者**：Smith A, et al.
**摘要**：该研究通过哺乳动物表达系统制备了EFNA5重组蛋白，验证其与EphA3受体的结合活性，并证明其能抑制肿瘤细胞迁移，为癌症治疗提供潜在工具。
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2. **文献名称**：*Expression and Purification of Functional Ephrin-A5 in E. coli*
**作者**：Chen L, et al.
**摘要**：开发了一种在大肠杆菌中高效表达可溶性EFNA5重组蛋白的方法，通过体外实验证实其诱导神经元生长锥塌陷的能力，支持其在神经发育研究中的应用。
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3. **文献名称**：*Structural Insights into Ephrin-A5 Signaling via Recombinant Protein Crystallography*
**作者**：Wang Y, et al.
**摘要**：利用重组EFNA5蛋白解析了其与EphB2受体复合物的晶体结构，揭示了相互作用的关键结构域，为靶向Eph-ephrin通路的药物设计提供依据。
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注：以上为示例文献，实际引用时需根据具体研究领域补充真实文献信息。
Ephrin-A5 (EFNA5) is a member of the ephrin family of cell-surface proteins that play pivotal roles in cell-cell communication and tissue patterning during development. As a glycosylphosphatidylinositol (GPI)-anchored ligand, it interacts with Eph receptor tyrosine kinases (EphA subclass), triggering bidirectional signaling pathways critical for axon guidance, angiogenesis, and tissue boundary formation. EFNA5 is particularly notable for its involvement in nervous system development, where it regulates neuronal connectivity and synaptic plasticity, as well as in pathological processes such as cancer metastasis and neurodegenerative disorders.
Recombinant EFNA5 protein is engineered using expression systems like mammalian cells (e.g., HEK293) or *E. coli* to ensure proper post-translational modifications or cost-effective production, respectively. This purified protein retains the functional Eph receptor-binding domain, enabling researchers to study EFNA5-mediated signaling *in vitro* or *in vivo*. Its applications span mechanistic studies of cell repulsion/adhesion behaviors, drug discovery targeting Eph/ephrin pathways, and tissue engineering approaches. In cancer research, recombinant EFNA5 helps investigate its dual role as both a tumor suppressor (via receptor activation) and a promoter of invasiveness in certain contexts. Recent studies also explore its potential in modulating immune responses and neural repair. The availability of recombinant EFNA5 has accelerated structural biology efforts, including crystallography studies to map interaction interfaces with Eph receptors, providing insights for therapeutic design.
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