| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CEA |
| Uniprot No | P06731 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 35-685aa |
| 氨基酸序列 | KLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNIIQNDTGFYTLHVIKSDLVNEEATGQFRVYPELPKPSISSNNSKPVEDKDAVAFTCEPETQDATYLWWVNNQSLPVSPRLQLSNGNRTLTLFNVTRNDTASYKCETQNPVSARRSDSVILNVLYGPDAPTISPLNTSYRSGENLNLSCHAASNPPAQYSWFVNGTFQQSTQELFIPNITVNNSGSYTCQAHNSDTGLNRTTVTTITVYAEPPKPFITSNNSNPVEDEDAVALTCEPEIQNTTYLWWVNNQSLPVSPRLQLSNDNRTLTLLSVTRNDVGPYECGIQNKLSVDHSDPVILNVLYGPDDPTISPSYTYYRPGVNLSLSCHAASNPPAQYSWLIDGNIQQHTQELFISNITEKNSGLYTCQANNSASGHSRTTVKTITVSAELPKPSISSNNSKPVEDKDAVAFTCEPEAQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLFNVTRNDARAYVCGIQNSVSANRSDPVTLDVLYGPDTPIISPPDSSYLSGANLNLSCHSASNPSPQYSWRINGIPQQHTQVLFIAKITPNNNGTYACFVSNLATGRNNSIVKSITVSASGTSPGLSA |
| 预测分子量 | 74.1 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. |
以下为3-4条关于CEA(癌胚抗原)重组蛋白的模拟参考文献示例(内容为虚构，供参考)：
1. **文献名称**：*Expression and Purification of Recombinant CEA in E. coli for Immunoassay Development*
**作者**：Smith J. et al.
**摘要**：本研究报道了通过大肠杆菌表达系统高效表达重组CEA蛋白，并优化纯化流程，验证其与临床抗体的结合活性，为癌症诊断试剂盒开发提供基础。
2. **文献名称**：*Structural Analysis of CEA Glycoprotein Using Recombinant Variants*
**作者**：Chen L. et al.
**摘要**：通过基因重组技术构建不同结构域的CEA蛋白变体，解析其糖基化修饰对肿瘤细胞黏附功能的影响，揭示CEA在癌症转移中的潜在机制。
3. **文献名称**：*Recombinant CEA as a Target for CAR-T Cell Therapy in Colorectal Cancer*
**作者**：Wang Y. et al.
**摘要**：利用重组CEA蛋白筛选高亲和力抗体，构建靶向CEA的CAR-T细胞，体外实验显示其对表达CEA的结肠癌细胞具有特异性杀伤效果。
4. **文献名称**：*Development of a CEA-based Recombinant Protein Vaccine for Immunotherapy*
**作者**：Johnson R. et al.
**摘要**：设计重组CEA与佐剂融合蛋白疫苗，动物实验表明其可诱导强烈的T细胞免疫应答，抑制小鼠模型中肿瘤生长，具有临床转化潜力。
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注：以上文献为模拟生成，实际引用需查询PubMed、Web of Science等数据库获取真实研究。
Carcinoembryonic antigen (CEA), also known as CEACAM5. is a glycosylated cell surface protein belonging to the immunoglobulin superfamily. First identified in 1965 as a tumor-associated antigen in colorectal cancer, CEA is overexpressed in many epithelial cancers, including gastrointestinal, lung, breast, and pancreatic malignancies. While its physiological role remains incompletely understood, CEA is implicated in cell adhesion, immune modulation, and intracellular signaling. Healthy adults typically exhibit low serum CEA levels (<5 ng/mL), but concentrations rise significantly in malignancies, making it a widely used clinical biomarker for cancer monitoring.
Recombinant CEA protein is engineered through genetic modification, where the CEA-coding sequence is inserted into expression vectors (e.g., bacterial, mammalian, or insect cell systems) for large-scale production. This technology enables precise control over protein structure and post-translational modifications, particularly glycosylation patterns critical for maintaining antigenic properties. Mammalian expression systems like CHO cells are often preferred to replicate human-like glycosylation.
The recombinant protein serves multiple research and clinical applications. It is essential for developing diagnostic immunoassays (ELISA, lateral flow tests) to quantify CEA in patient samples. In therapeutics, recombinant CEA underpins vaccine development and targeted therapies, including antibody-drug conjugates and CAR-T cell platforms. Recent studies also explore its role in tumor microenvironment modulation and as a carrier for drug delivery systems.
Quality considerations for recombinant CEA include batch-to-bbatch consistency, endotoxin levels, and validation of biological activity through binding assays with anti-CEA antibodies. Ongoing research focuses on optimizing expression systems to enhance yield while preserving functional epitopes, addressing challenges in structural complexity and heterogeneity inherent to glycoproteins.
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