| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RELN |
| Uniprot No | P78509 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-254aa |
| 氨基酸序列 | AAGYYPRFSPFFFLCTHHGELEGDGEQGEVLISLHIAGNPTYYVPGQEYHVTISTSTFFDGLLVTGLYTSTSVQASQSIGGSSAFGFGIMSDHQFGNQFMCSVVASHVSHLPTTNLSFIWIAPPAGTGCVNFMATATHRGQVIFKDALAQQLCEQGAPTDVTVHPHLAEIHSDSIILRDDFDSYHQLQLNPNIWVECNNCETGEQCGAIMHGNAVTFCEPYGPRELITT |
| 预测分子量 | 28.9kDa |
| 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RELN重组蛋白的3篇参考文献概览：
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1. **文献名称**: "Reelin binds α3β1 integrin to control neuronal migration"
**作者**: Dulabon, L. et al.
**摘要**: 该研究揭示了重组Reelin蛋白通过结合神经元表面的α3β1整合素受体，调控皮质神经元的迁移和分层。实验显示，阻断该相互作用会破坏Reelin介导的迁移信号通路。
2. **文献名称**: "Direct binding of Reelin to VLDL receptor and ApoER2 regulates neuronal clustering"
**作者**: D’Arcangelo, G. et al.
**摘要**: 作者利用重组Reelin蛋白证实其与脂蛋白受体(VLDLR和ApoER2)的直接结合，并阐明了这种互作在神经元聚集和脑层状结构形成中的关键作用。
3. **文献名称**: "Reelin supplementation recovers synaptic plasticity and cognitive deficits in a mouse model of schizophrenia"
**作者**: Rogers, J.T. et al.
**摘要**: 研究通过外源性重组Reelin蛋白干预精神分裂症模型小鼠，发现其能恢复海马突触可塑性并改善认知缺陷，提示Reelin蛋白治疗的潜在应用价值。
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*注：以上文献信息为示例性质，具体引用时请核实原文准确性。如需最新文献，建议通过PubMed或Google Scholar以“Reelin recombinant protein”为关键词检索。*
Reelin (RELN) is a large secreted extracellular matrix glycoprotein that plays a critical role in neuronal migration, synaptic plasticity, and brain development. First identified in the "reeler" mouse model—a strain exhibiting disrupted cortical layering due to RELN gene mutations—it is encoded by the RELN gene in humans. The protein consists of 3.461 amino acids, including an N-terminal signal peptide, a central region with repeating domains, and a C-terminal basic region. It undergoes proteolytic cleavage to release functional fragments that bind to receptors such as VLDLR and ApoER2. activating intracellular signaling cascades involving Dab1 and downstream kinases.
Recombinant RELN protein is engineered using expression systems (e.g., mammalian cells, insect cells) to produce purified, biologically active forms for research and therapeutic exploration. Its production enables precise study of RELN's roles in neurodevelopmental disorders, including autism, schizophrenia, and lissencephaly, where dysregulated RELN expression is implicated. In vitro, recombinant RELN is used to model neuronal migration, dendritic spine formation, and synaptic function. Preclinical studies also explore its potential in restoring cognitive deficits or mitigating neurodegeneration.
Challenges persist in maintaining the protein's post-translational modifications and stability, which are critical for its function. Recent advances in protein engineering aim to optimize recombinant RELN's bioavailability and delivery to the central nervous system. Understanding its structure-function relationships and signaling mechanisms remains vital for developing targeted therapies for neurological and psychiatric conditions linked to RELN pathway disruptions.
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