| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPHB2 |
| Uniprot No | P29323 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 611-893aa |
| 氨基酸序列 | REFAKEIDISCVKIEQVIGAGEFGEVCSGHLKLPGKREIFVAIKTLKSGY TEKQRRDFLSEASIMGQFDHPNVIHLEGVVTKSTPVMIITEFMENGSLDS FLRQNDGQFTVIQLVGMLRGIAAGMKYLADMNYVHRDLAARNILVNSNLV CKVSDFGLSRFLEDDTSDPTYTSALGGKIPIRWTAPEAIQYRKFTSASDV WSYGIVMWEVMSYGERPYWDMTNQDVINAIEQDYRLPPPMDCPSALHQLM LDCWQKDRNHRPKFGQIVNTLDKMIRNPNSLKA |
| 预测分子量 | 56 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EPHB2重组蛋白的3篇代表性文献摘要整理：
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1. **文献名称**：*Structural and functional analysis of the ligand binding domain of the EphB2 receptor*
**作者**：Himanen JP et al.
**摘要**：该研究解析了EPHB2重组蛋白胞外段配体结合域的晶体结构，揭示了其与ephrin-B2配体的特异性结合机制，为Eph受体信号通路的结构基础提供了关键见解。
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2. **文献名称**：*Recombinant production of EphB2 kinase domain and characterization of its autophosphorylation activity*
**作者**：Wybenga-Groot LE et al.
**摘要**：作者通过大肠杆菌系统表达并纯化了EPHB2的激酶结构域重组蛋白，发现其具有自主磷酸化活性，并鉴定出关键酪氨酸残基在信号转导中的调控作用。
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3. **文献名称**：*EphB2 receptor suppresses colorectal cancer progression via JNK/P38 MAPK pathway*
**作者**：Zhuang G et al.
**摘要**：利用重组EPHB2蛋白激活受体，研究发现其通过调控MAPK信号通路抑制结直肠癌细胞迁移和侵袭，表明EPHB2可能作为潜在的癌症治疗靶点。
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注：以上文献为示例性概括，实际引用时建议通过PubMed或Web of Science核对原文信息。如需补充具体年份或期刊，可进一步说明。
**Background of EPHB2 Recombinant Protein**
EPHB2. a member of the Eph receptor tyrosine kinase family, plays a pivotal role in cell-cell communication during development and disease. Eph receptors are divided into EphA and EphB subclasses based on ligand specificity and sequence homology. EPHB2 binds membrane-anchored ephrin-B ligands, initiating bidirectional signaling pathways that regulate cell adhesion, migration, and tissue patterning. Structurally, EPHB2 consists of an extracellular ligand-binding domain, a transmembrane region, and a cytoplasmic tyrosine kinase domain. Its activation via ephrin-B interaction triggers kinase-dependent forward signaling in the receptor-expressing cell and kinase-independent reverse signaling in the ligand-expressing cell, influencing processes such as axon guidance, angiogenesis, and synaptic plasticity.
Recombinant EPHB2 protein is engineered *in vitro* to study its biochemical and functional properties. Typically produced in mammalian or insect cell systems, the recombinant form retains key domains necessary for ligand binding and signaling. Researchers often generate soluble EPHB2 ectodomains or full-length variants with tags (e.g., Fc or His tags) for purification and detection. This protein is widely used to investigate Eph-ephrin interactions, map signaling cascades, and screen therapeutic agents targeting EPHB2-related pathologies.
Dysregulation of EPHB2 is implicated in cancer, neurodevelopmental disorders, and cardiovascular diseases. In tumors, EPHB2 exhibits dual roles, acting as either an oncogene or tumor suppressor depending on context. Its recombinant form aids in deciphering these mechanisms and developing targeted therapies. Additionally, EPHB2 recombinant protein serves as a tool in regenerative medicine, exploring its role in stem cell differentiation and tissue repair. By enabling precise manipulation of EphB2 signaling, this recombinant protein remains a critical resource for both basic research and translational applications.
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