| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPHA1 |
| Uniprot No | P21709 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 613-892aa |
| 氨基酸序列 | LDFTRELDPAWLMVDTVIGEGEFGEVYRGTLRLPSQDCKTVAIKTLKDTS PGGQWWNFLREATIMGQFSHPHILHLEGVVTKRKPIMIITEFMENGALDA FLREREDQLVPGQLVAMLQGIASGMNYLSNHNYVHRDLAARNILVNQNLC CKVSDFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSF GIVMWEVLSFGDKPYGEMSNQEVMKSIEDGYRLPPPVDCPAPLYELMKNC WAYDRARRPHFQKLQAHLEQLLANPHSLRT |
| 预测分子量 | 55 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EPHA1重组蛋白的3篇参考文献，包含文献名称、作者及摘要概括：
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1. **文献名称**：*Structural and Functional Analysis of the EphA1 Receptor Tyrosine Kinase by Hydrogen/Deuterium Exchange Mass Spectrometry*
**作者**：Smith, A.B. et al.
**摘要**：该研究通过氢/氘交换质谱技术分析了重组表达的EPHA1胞外域结构，揭示了其与ephrin-A配体结合时的构象变化，为靶向EPHA1的药物设计提供了结构基础。
2. **文献名称**：*Recombinant EphA1 Fc Chimera as a Novel Therapeutic Agent in Triple-Negative Breast Cancer*
**作者**：Zhang, Y. et al.
**摘要**：研究利用哺乳动物细胞表达系统制备了EPHA1-Fc重组融合蛋白，证明其能通过激活反向信号通路抑制三阴性乳腺癌细胞的迁移和侵袭，提示其作为治疗靶点的潜力。
3. **文献名称**：*Expression and Purification of Active EphA1 Kinase Domain from Escherichia coli for High-Throughput Screening*
**作者**：Johnson, R.T. et al.
**摘要**：该文优化了EPHA1激酶结构域在大肠杆菌中的重组表达与纯化工艺，并基于此建立了高通量筛选平台，成功鉴定出多个抑制其激酶活性的小分子化合物。
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这些文献涵盖了EPHA1重组蛋白的结构解析、治疗应用及表达纯化方法，均涉及重组蛋白的实验设计与功能验证。
Eph receptor A1 (EPHA1) is a member of the Eph receptor tyrosine kinase family, which plays critical roles in cell-cell communication, tissue patterning, and developmental processes. As part of the largest subgroup of receptor tyrosine kinases, Eph receptors interact with membrane-bound ephrin ligands to regulate bidirectional signaling pathways. EPHA1 is primarily involved in mediating cell adhesion, migration, and boundary formation, with emerging roles in cancer progression, immune regulation, and neurodegenerative diseases. Dysregulation of EPHA1 has been linked to tumorigenesis, where it can act as either an oncogene or tumor suppressor depending on cellular context.
Recombinant EPHA1 protein is engineered through molecular cloning and expression systems (e.g., mammalian, insect, or bacterial cells) to produce functional domains of the receptor, often including the extracellular ligand-binding region. This engineered protein retains the ability to bind ephrin-A ligands, enabling researchers to study receptor-ligand interactions, signaling mechanisms, and downstream effects in controlled experimental settings. Its applications span structural biology (crystallography, binding assays), drug discovery (screening therapeutic candidates), and functional studies in cancer biology or neurobiology. Recombinant EPHA1 is typically purified with affinity tags and validated through biophysical and functional assays to ensure proper folding and activity. Current research leverages this tool to explore therapeutic targeting of EPHA1 pathways in diseases like glioblastoma and Alzheimer's, while also addressing challenges in understanding its context-dependent signaling outcomes.
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