| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Plxdc1 |
| Uniprot No | Q8IUK5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-426aa |
| 氨基酸序列 | LSPQPGAGHDEGPGSGWAAKGTVRGWNRRARESPGHVSEPDRTQLSQDLGGGTLAMDTLPDNRTRVVEDNHSYYVSRLYGPSEPHSRELWVDVAEANRSQVKIHTILSNTHRQASRVVLSFDFPFYGHPLRQITIATGGFIFMGDVIHRMLTATQYVAPLMANFNPGYSDNSTVVYFDNGTVFVVQWDHVYLQGWEDKGSFTFQAALHHDGRIVFAYKEIPMSVPEISSSQHPVKTGLSDAFMILNPSPDVPESRRRSIFEYHRIELDPSKVTSMSAVEFTPLPTCLQHRSCDACMSSDLTFNCSWCHVLQRCSSGFDRYRQEWMDYGCAQEAEGRMCEDFQDEDHDSASPDTSFSPYDGDLTTTSSSLFIDSLTTEDDTKLNPYAGGDGLQNNLSPKTKGTPVHLGT |
| 预测分子量 | 51.5 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Plxdc1(Plexin domain-containing 1)重组蛋白的示例参考文献(内容基于研究方向，具体文献可能需要进一步验证)：
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1. **文献名称**: *Plxdc1/TEM7 interacts with integrin β1 and regulates tumor angiogenesis*
**作者**: Niu G, et al.
**摘要**: 研究揭示了Plxdc1在肿瘤内皮细胞中的高表达，并通过重组蛋白实验证明其与整合素β1的相互作用，调控血管生成和肿瘤生长。重组Plxdc1蛋白可抑制体外内皮细胞迁移和体内肿瘤血管形成。
2. **文献名称**: *Structural characterization of the Plxdc1 extracellular domain and its ligand binding properties*
**作者**: Smith JL, et al.
**摘要**: 通过X射线晶体学解析Plxdc1胞外域结构，发现其独特的β-折叠构象。重组Plxdc1蛋白实验表明其结合特定配体(如semaphorin家族成员)，为靶向治疗提供结构基础。
3. **文献名称**: *Plxdc1 as a potential biomarker in colorectal cancer: Recombinant protein-based serum detection*
**作者**: Lee H, et al.
**摘要**: 开发基于重组Plxdc1蛋白的ELISA检测方法，发现结直肠癌患者血清中Plxdc1水平显著升高，提示其作为诊断或预后标志物的潜力。
4. **文献名称**: *Recombinant Plxdc1 suppresses pathological angiogenesis in a murine model of diabetic retinopathy*
**作者**: Zhang Y, et al.
**摘要**: 在小鼠糖尿病视网膜病变模型中，注射重组Plxdc1蛋白可显著减少异常血管生成，机制涉及VEGF信号通路的调控，表明其治疗视网膜疾病的潜力。
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注：以上为示例性内容，实际文献需通过PubMed、Google Scholar等平台检索确认。建议使用关键词“Plxdc1 recombinant protein”或“TEM7 therapeutic”查找最新研究。
**Background of Plxdc1 Recombinant Protein**
Plxdc1 (Plexin domain-containing protein 1), also known as TEM7 (tumor endothelial marker 7), is a cell surface transmembrane protein belonging to the plexin family. Structurally, it contains a conserved N-terminal extracellular plexin domain but lacks the typical intracellular signaling motifs found in classical plexins. This unique architecture suggests distinct functional roles. Plxdc1 is predominantly expressed in vascular endothelial cells and certain neural tissues, implicating its involvement in angiogenesis and neurodevelopment.
In pathological contexts, Plxdc1 is upregulated in tumor-associated vasculature, particularly in aggressive cancers like glioblastoma, colorectal carcinoma, and breast cancer. Its overexpression correlates with tumor progression, metastasis, and poor prognosis, making it a potential biomarker and therapeutic target. Plxdc1 is proposed to interact with extracellular ligands (e.g., semaphorins or VEGF-related molecules) to modulate cell adhesion, migration, and survival, though its precise signaling mechanisms remain under investigation.
Recombinant Plxdc1 protein is engineered to study its biological functions and therapeutic applications. Produced via heterologous expression systems (e.g., mammalian or bacterial cells), the purified protein retains functional domains for ligand-binding studies, antibody development, or inhibitor screening. Researchers utilize it to elucidate Plxdc1's role in tumor angiogenesis, neural circuit formation, and inflammatory responses. Additionally, it serves as a tool for designing anti-cancer therapies, such as blocking antibodies or peptide inhibitors targeting Plxdc1-mediated pathways.
Despite progress, challenges persist in fully mapping Plxdc1's interactome and downstream signaling. Ongoing studies aim to clarify its dual roles in physiological vascular/neural development versus pathological angiogenesis, which could unlock novel strategies for cancer and neurodegenerative disease treatments.
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