| 纯度 | >90%SDS-PAGE. |
| 种属 | Hordeum |
| 靶点 | EPB2 |
| Uniprot No | P25250 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 134-373aa |
| 氨基酸序列 | LPPSVDWRQKGAVTGVKDQGKCGSCWAFSTVVSVEGINAIRTGSLVSLSEQELIDCDTADNDGCQGGLMDNAFEYIKNNGGLITEAAYPYRAARGTCNVARAAQNSPVVVHIDGHQDVPANSEEDLARAVANQPVSVAVEASGKAFMFYSEGVFTGECGTELDHGVAVVGYGVAEDGKAYWTVKNSWGPSWGEQGYIRVEKDSGASGGLCGIAMEASYPVKTYSKPKPTPRRALGARESL |
| 预测分子量 | 41.3 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EPB42(Erythrocyte Membrane Protein Band 4.2)重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*"Expression and functional characterization of recombinant human erythrocyte membrane protein band 4.2"*
**作者**：Korsgren C, Cohen CM
**摘要**：该研究成功克隆并表达了人源EPB42重组蛋白，证明其在红细胞膜稳定性中的作用，并通过体外实验验证其与血影蛋白(spectrin)的相互作用，为遗传性溶血性贫血的机制研究提供了依据。
2. **文献名称**：*"Defective binding of erythrocyte membrane protein band 4.2 in hereditary spherocytosis"*
**作者**：Rybicki AC, et al.
**摘要**：通过重组EPB42蛋白实验，发现某些遗传性球形红细胞增多症患者的EPB42存在突变，导致其与膜锚定蛋白(ankyrin)结合能力下降，揭示了该疾病中红细胞膜脆性增加的分子机制。
3. **文献名称**：*"Recombinant erythrocyte membrane protein 4.2: a potential diagnostic marker for hemolytic disorders"*
**作者**：Suzuki K, et al.
**摘要**：研究开发了高纯度EPB42重组蛋白，并证明其可用于检测患者血清中的自身抗体，为溶血性贫血的免疫学诊断提供了新的生物标志物工具。
注：EPB42相关重组蛋白研究相对较少，上述文献为示例性质，实际检索时建议通过PubMed或Google Scholar以关键词“EPB42 recombinant protein”或“Erythrocyte Membrane Protein Band 4.2”获取最新研究。
**Background of EPB2 Recombinant Protein**
Ephrin type-B receptor 2 (EPHB2), a member of the Eph receptor tyrosine kinase family, plays critical roles in cell-cell communication, tissue patterning, and developmental processes. These receptors and their ephrin ligands mediate bidirectional signaling, regulating cell adhesion, migration, and spatial organization in diverse biological systems, including the nervous and vascular systems. EPHB2 is particularly implicated in axon guidance, synaptic plasticity, and angiogenesis. Dysregulation of EPHB2 signaling has been linked to pathological conditions such as cancer metastasis, neurodegenerative disorders, and cardiovascular diseases.
Recombinant EPHB2 protein is engineered using molecular cloning techniques, often expressed in mammalian or insect cell systems to ensure proper post-translational modifications (e.g., glycosylation) and functional fidelity. The protein typically includes extracellular domains responsible for ligand binding and receptor dimerization, enabling studies on ligand-receptor interactions and downstream signaling mechanisms. Purification methods, such as affinity chromatography, yield high-purity protein suitable for structural, biochemical, and cellular assays.
Research applications of recombinant EPHB2 span *in vitro* and *in vivo* models. It is used to investigate Eph-ephrin signaling pathways, screen therapeutic agents targeting receptor-ligand interfaces, and explore mechanisms in tumorigenesis or neural repair. Its role in modulating cell adhesion and migration also makes it relevant for studying metastasis and tissue regeneration. Additionally, recombinant EPHB2 serves as a tool for antibody development and diagnostic biomarker research.
The production of functional EPHB2 recombinant protein underscores its importance in bridging basic research and therapeutic innovation, offering insights into developmental biology and disease mechanisms while holding potential for targeted therapies.
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