| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EphB6 |
| Uniprot No | O15197 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 617-1021aa |
| 氨基酸序列 | VVFQRKRRGTGYTEQLQQYSSPGLGVKYYIDPSTYEDPCQAIRELAREVDPAYIKIEEVIGTGSFGEVRQGRLQPRGRREQTVAIQALWAGGAESLQMTFLGRAAVLGQFQHPNILRLEGVVTKSRPLMVLTEFMELGPLDSFLRQREGQFSSLQLVAMQRGVAAAMQYLSSFAFVHRSLSAHSVLVNSHLVCKVARLGHSPQGPSCLLRWAAPEVIAHGKHTTSSDVWSFGILMWEVMSYGERPYWDMSEQEVLNAIEQEFRLPPPPGCPPGLHLLMLDTWQKDRARRPHFDQLVAAFDKMIRKPDTLQAGGDPGERPSQALLTPVALDFPCLDSPQAWLSAIGLECYQDNFSKFGLCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQLLQQHLRQQGSVEV |
| 预测分子量 | 70 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EphB6重组蛋白的3篇参考文献示例(注：文献信息为模拟示例，实际文献需通过学术数据库验证)：
---
1. **文献名称**: "Recombinant EphB6 regulates T-cell signaling through ligand-independent mechanisms"
**作者**: Yu G, et al.
**摘要**: 本研究利用哺乳动物表达系统成功表达并纯化EphB6重组蛋白，发现其在T细胞中通过非依赖配体的方式抑制ERK/MAPK信号通路，揭示了EphB6在免疫调节中的潜在作用。
2. **文献名称**: "Structural and functional characterization of the EphB6 kinase domain"
**作者**: Li X, et al.
**摘要**: 通过X射线晶体学解析EphB6重组蛋白激酶结构域的三维结构，发现其因关键氨基酸缺失导致激酶活性丧失，并证实其通过非催化机制参与细胞粘附和迁移调控。
3. **文献名称**: "EphB6 suppresses metastasis in breast cancer via interaction with EGFR"
**作者**: Miao H, et al.
**摘要**: 利用重组EphB6蛋白进行体外实验，证明其与表皮生长因子受体(EGFR)直接结合，负向调控EGFR下游信号传导，抑制乳腺癌细胞的侵袭和转移能力。
---
**备注**：以上文献信息为示例，建议通过PubMed、Google Scholar等平台检索最新研究，关键词包括“EphB6 recombinant protein”、“EphB6 expression/purification”、“EphB6 signaling”。
EphB6 is a member of the Eph receptor tyrosine kinase family, which plays critical roles in cell-cell communication, tissue patterning, and developmental processes. Unlike most Eph receptors, EphB6 is unique due to its lack of intrinsic kinase activity, a result of amino acid substitutions in its kinase domain. This "kinase-dead" characteristic shifts its functional focus to kinase-independent signaling mechanisms, often involving interactions with other Eph receptors or downstream adaptor proteins. Structurally, EphB6 consists of an extracellular domain that binds ephrin-B ligands, a transmembrane region, and a cytoplasmic domain responsible for signal transduction. It is predominantly expressed in the nervous system, immune cells, and certain epithelial tissues.
Research has linked EphB6 to diverse physiological and pathological processes, including cancer progression, neuronal development, and immune regulation. In cancer, EphB6 exhibits dual roles—acting as a tumor suppressor in some contexts (e.g., inhibiting metastasis in breast cancer) while promoting tumorigenesis in others (e.g., enhancing survival in T-cell leukemia). Its involvement in immune regulation includes modulating T-cell activation and cytokine secretion. In the nervous system, EphB6 contributes to axon guidance and synaptic plasticity through interactions with ephrin-B ligands.
Recombinant EphB6 protein, typically produced in mammalian or insect expression systems, retains post-translational modifications essential for ligand binding and functional studies. It serves as a vital tool for investigating EphB6-ephrin-B interactions, receptor clustering, and downstream signaling pathways in vitro. Researchers utilize it to study mechanisms underlying cell adhesion, migration, and apoptosis, as well as to screen therapeutic agents targeting Eph-related diseases. Structural studies using recombinant EphB6 have also clarified its ligand-binding specificity and conformational changes during activation. Despite its kinase inactivity, EphB6’s ability to form heterocomplexes with active Eph receptors underscores its role as a regulatory node in Eph signaling networks, making it a compelling subject for both basic and translational research.
×
