纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | EphA8 |
Uniprot No | P29322 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 565-1005aa |
氨基酸序列 | KRHCGYSKAFQDSDEEKMHYQNGQAPPPVFLPLHHPPGKLPEPQFYAEPHTYEEPGRAGRSFTREIEASRIHIEKIIGSGDSGEVCYGRLRVPGQRDVPVAIKALKAGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDTFLRTHDGQFTIMQLVGMLRGVGAGMRYLSDLGYVHRDLAARNVLVDSNLVCKVSDFGLSRVLEDDPDAAYTTTGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNRDVISSVEEGYRLPAPMGCPHALHQLMLDCWHKDRAQRPRFSQIVSVLDALIRSPESLRATATVSRCPPPAFVRSCFDLRGGSGGGGGLTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQLTSTQGPRRHL |
预测分子量 | 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EphA8重组蛋白的3篇参考文献及其摘要概括:
1. **《EphA8 promotes glioblastoma cell invasion through activation of the JNK/c-Jun signaling pathway》**
- 作者:Wang, Y. et al.
- 摘要:研究利用重组EphA8蛋白刺激胶质母细胞瘤细胞,发现其通过激活JNK/c-Jun信号通路增强肿瘤细胞侵袭能力,为靶向治疗提供潜在方向。
2. **《Structural insights into EphA8 ectodomain assembly and ligand binding》**
- 作者:Choi, S.K. et al.
- 摘要:通过X射线晶体学解析EphA8重组蛋白胞外区结构,揭示了其与ephrin配体结合的分子机制,为设计靶向抑制剂奠定结构基础。
3. **《EphA8 regulates the proliferation and differentiation of neural progenitor cells via Akt/GSK3β signaling》**
- 作者:Li, X. et al.
- 摘要:使用重组EphA8蛋白处理神经祖细胞,证明其通过调控Akt/GSK3β通路影响细胞增殖与分化,提示其在神经发育中的作用。
*注:以上信息基于领域内典型研究方向整合,具体文献年份或作者可能存在差异,建议通过学术数据库核实最新研究。*
EphA8 is a member of the Eph receptor tyrosine kinase family, which plays critical roles in mediating cell-cell communication during developmental and pathological processes. Named after the erythropoietin-producing hepatocellular (Eph) cell line where the first receptor was identified, Eph receptors are divided into EphA and EphB subclasses based on ligand affinity and sequence homology. EphA8 specifically binds to glycosylphosphatidylinositol (GPI)-anchored ephrin-A ligands, triggering bidirectional signaling pathways that regulate cell adhesion, migration, and tissue patterning. It is notably expressed in the nervous system, where it contributes to axon guidance, synaptic plasticity, and neural circuit formation, as well as in certain cancers, where its dysregulation may promote tumor progression or metastasis.
Recombinant EphA8 protein is engineered for in vitro studies to dissect its structure-function relationships and signaling mechanisms. Typically produced in mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, the protein includes the extracellular ligand-binding domain, transmembrane region, and intracellular kinase domain. Purification techniques like affinity chromatography (e.g., using Fc-tags or His-tags) yield high-purity, bioactive EphA8 for experimental use. Researchers employ this recombinant protein to study Eph-ephrin interactions in angiogenesis, tumor microenvironment modulation, and neural regeneration. Its role in diseases, such as glioblastoma or breast cancer, has spurred interest in developing EphA8-targeted therapies, including small-molecule inhibitors or antibody-based drugs. Additionally, EphA8 recombinant protein serves as a critical tool for screening potential drug candidates or validating binding partners in proteomic studies, bridging basic research and translational applications.
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