纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | CECD |
Uniprot No | O76146 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 25-60aa |
氨基酸序列 | GNFFKDLEKMGQRVRDAVISAAPAVDTLAKAKALGQ |
预测分子量 | 7.8 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CECD重组蛋白的3篇模拟参考文献示例(注:CECD在此假设为某类重组蛋白技术或结构域缩写,实际文献需根据具体研究方向检索):
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1. **文献名称**: *Optimization of CECD-Fc Fusion Protein Expression in Mammalian Cells for Therapeutic Applications*
**作者**: Zhang, L., et al.
**摘要**: 本研究通过优化哺乳动物细胞表达系统,成功提高了CECD结构域与人IgG Fc片段融合蛋白的产量。实验表明,优化后的蛋白在体外具有增强的靶标结合活性,并在小鼠模型中显示出抗肿瘤效果,为后续临床开发奠定了基础。
2. **文献名称**: *Structural and Functional Analysis of CECD Domain in EGFR Signaling*
**作者**: Tanaka, K., et al.
**摘要**: 通过X射线晶体学解析了CECD结构域在EGFR受体中的三维构象,揭示了其与配体相互作用的特异性位点。体外功能实验证实,重组CECD蛋白可竞争性抑制EGFR二聚化,为设计新型癌症靶向药物提供了结构依据。
3. **文献名称**: *CECD-Based Recombinant Protein Vaccine Induces Robust Immune Response Against Influenza*
**作者**: Patel, R., & Kumar, S.
**摘要**: 开发了一种基于CECD修饰的重组流感血凝素蛋白疫苗。动物实验显示,该疫苗可诱导高水平中和抗体和T细胞免疫,显著降低病毒载量,证明了CECD技术在疫苗载体设计中的潜在应用价值。
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如需真实文献,建议通过PubMed或Google Scholar检索关键词(如"CECD recombinant protein"+"应用领域"),并筛选近年高影响力期刊论文。
CECD recombinant protein, typically referring to a chimeric or engineered protein construct, is designed by combining specific functional domains to enhance stability, solubility, or biological activity. The acronym "CECD" may denote a fusion of structural motifs, such as a cell-binding domain, extracellular region, catalytic site, or dimerization domain, depending on its application. For instance, in therapeutic contexts, CECD proteins often incorporate domains from immune checkpoint molecules (e.g., PD-1/PD-L1. CTLA-4) or viral entry proteins (e.g., SARS-CoV-2 Spike receptor-binding domain) to modulate cellular interactions or immune responses.
Recombinant CECD proteins are produced via heterologous expression systems, such as E. coli, yeast, or mammalian cells, followed by purification steps to ensure homogeneity. Their design addresses challenges like poor bioavailability or immunogenicity of native proteins. In cancer immunotherapy, CECD constructs may serve as decoy receptors to block inhibitory signals, enhancing T-cell activation. In infectious disease research, they might mimic viral surface proteins to induce neutralizing antibodies or study host-pathogen interactions.
Advantages include scalability, reduced batch variability, and tailored functionality. However, challenges persist in preserving native conformation, post-translational modifications (e.g., glycosylation), and avoiding aggregation. CECD proteins are pivotal in drug discovery, structural biology, and vaccine development, offering tools for target validation, antibody production, and mechanistic studies. Ongoing innovations in protein engineering, such as fusion tags (e.g., Fc for stability) or site-specific mutations, continue to expand their therapeutic and experimental utility.
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