纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | EPHA2 |
Uniprot No | P29317 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 24-534aa |
氨基酸序列 | AQGKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNIMNDMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPPGGEEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTLPSPEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGREDIVYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGVSGLVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGDSNSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGN |
预测分子量 | 61.2 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EPHA2重组蛋白的3篇参考文献示例(内容为虚构,仅作格式参考):
1. **文献名称**:*Structural and functional analysis of the EphA2 receptor tyrosine kinase*
**作者**:Nikolova, Z., Binns, K.L., & Himanen, J.P.
**摘要**:该研究通过重组表达并纯化人源EPHA2的胞外结构域,利用X射线晶体学解析其三维结构,揭示了配体结合的关键表位,并证明其激酶活性依赖特定的磷酸化位点。
2. **文献名称**:*EphA2 recombinant protein inhibits tumor angiogenesis by blocking VEGF signaling*
**作者**:Cheng, X., et al.
**摘要**:通过大肠杆菌系统表达EPHA2重组蛋白,发现其可通过竞争性结合血管内皮生长因子(VEGF),抑制肿瘤微环境中的血管生成,为靶向治疗提供实验依据。
3. **文献名称**:*Development of a high-throughput assay for screening EphA2 kinase inhibitors using recombinant protein*
**作者**:Lee, S.M., & Park, H.
**摘要**:研究构建了EPHA2激酶结构域的重组蛋白,并建立基于荧光共振能量转移(FRET)的高通量筛选平台,成功鉴定出多个小分子抑制剂,为抗癌药物开发奠定基础。
如需真实文献,建议通过PubMed或Google Scholar检索关键词“EPHA2 recombinant protein expression”或“EPHA2 structural study”。
Eph receptor A2 (EPHA2) is a member of the Eph receptor tyrosine kinase family, which plays critical roles in cell-cell communication, tissue patterning, and disease progression. Structurally, EPHA2 consists of an extracellular ligand-binding domain, a transmembrane region, and an intracellular kinase domain. It interacts with membrane-bound ephrin-A ligands to initiate bidirectional signaling pathways that regulate cell adhesion, migration, and proliferation. Unlike most Eph receptors, EPHA2 exhibits unique signaling behaviors, including ligand-independent activation in pathological conditions such as cancer. Its dual role in both tumor suppression and promotion—depending on ligand engagement and cellular context—has made it a compelling yet complex therapeutic target.
Recombinant EPHA2 proteins are engineered to study its structure-function relationships, signaling mechanisms, and therapeutic modulation. These proteins are typically produced in mammalian or insect expression systems to preserve post-translational modifications and ligand-binding capacity. Common variants include extracellular domains for binding studies, kinase domains for enzymatic activity assays, and full-length receptors for cell-based experiments. Researchers utilize recombinant EPHA2 to investigate its crosstalk with oncogenic pathways (e.g., RAS/MAPK), angiogenesis, and epithelial-mesenchymal transition. In cancer biology, EPHA2 overexpression correlates with metastasis and drug resistance, driving interest in developing inhibitory antibodies or small molecules. Additionally, its involvement in vascular and neurological disorders highlights broad biomedical relevance. The production of active, purified EPHA2 protein remains essential for structural studies (e.g., crystallography) and high-throughput drug screening platforms aiming to exploit its context-dependent signaling for precision therapies.
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