纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | EFNA1 |
Uniprot No | P20827 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 19-182aa |
氨基酸序列 | DR HTVFWNSSNP KFRNEDYTIH VQLNDYVDII CPHYEDHSVA DAAMEQYILY LVEHEEYQLC QPQSKDQVRW QCNRPSAKHG PEKLSEKFQR FTPFTLGKEF KEGHSYYYIS KPIHQHEDRC LRLKVTVSGK ITHSPQAHDN PQEKRLAADD PEVRVLHSIG HS |
预测分子量 | 46 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EFNA1重组蛋白的3篇代表性文献(虚构示例,供参考格式):
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1. **文献名称**: *"Recombinant Ephrin-A1 inhibits tumor angiogenesis through EphA2 receptor signaling"*
**作者**: Smith J et al.
**摘要**: 研究利用重组EFNA1蛋白与EphA2受体结合,通过体外和小鼠模型实验证明其抑制血管内皮细胞迁移和肿瘤血管生成的作用,为抗肿瘤治疗提供新策略。
2. **文献名称**: *"Structural characterization of human Ephrin-A1 and its binding dynamics with Eph receptors"*
**作者**: Lee S et al.
**摘要**: 通过X射线晶体学解析重组EFNA1蛋白结构,揭示其与EphA家族受体的结合界面特征,阐明配体-受体特异性相互作用的分子机制。
3. **文献名称**: *"Recombinant EFNA1 modulates inflammatory response in macrophage via reverse signaling"*
**作者**: Chen L et al.
**摘要**: 发现重组EFNA1蛋白可通过激活巨噬细胞内的逆向信号通路,下调促炎因子TNF-α和IL-6的表达,提示其在炎症性疾病中的潜在应用。
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(注:以上文献为模拟内容,实际研究中需通过PubMed或Web of Science检索真实文献。)
Ephrin-A1 (EFNA1) is a member of the ephrin family of cell-surface proteins that bind to Eph receptor tyrosine kinases, mediating critical cell-cell communication processes. As a key ligand for Eph receptors, EFNA1 plays pivotal roles in developmental biology, including axon guidance, vascular patterning, and tissue boundary formation. Structurally, it is a glycosylphosphatidylinositol (GPI)-anchored protein containing a conserved receptor-binding domain and a variable N-terminal region. Dysregulation of EFNA1-Eph signaling is implicated in cancer progression, angiogenesis, and inflammatory diseases, making it a therapeutic target.
Recombinant EFNA1 protein is engineered using expression systems (e.g., mammalian cells) to ensure proper post-translational modifications and functional activity. It typically includes the extracellular domain (amino acids 1-182 in humans) to retain receptor-binding capability. Researchers utilize recombinant EFNA1 to study Eph receptor activation, downstream signaling pathways (e.g., MAPK, PI3K/AKT), and its dual role in both promoting and suppressing tumor growth depending on cellular context. In cancer biology, EFNA1 exhibits paradoxical effects: it can inhibit angiogenesis by destabilizing endothelial cell networks or enhance metastatic potential through epithelial-mesenchymal transition (EMT).
Additionally, EFNA1 recombinant protein is employed in drug discovery, particularly for screening inhibitors or agonists of Ephrin-Eph interactions. Its applications extend to neurology, where it aids in modeling synaptic plasticity and neural repair mechanisms. Recent studies also explore its immunomodulatory functions in autoimmune disorders. Despite its complexity, recombinant EFNA1 remains a vital tool for deciphering cell signaling crosstalk and developing targeted therapies for cancer and neurological diseases.
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