| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CEACAM3 |
| Uniprot No | P40198 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 35-155aa |
| 氨基酸序列 | KLTIESMPLSVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNSLIVGYVI GTQQATPGAAYSGRETIYTNASLLIQNVTQNDIGFYTLQVIKSDLVNEEA TGQFHVYQENAPGLPVGAVAGVDHHHHHH |
| 预测分子量 | 14 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CEACAM3重组蛋白的3篇参考文献，包含文献名称、作者及摘要概括：
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1. **文献名称**：*"CEACAM3-mediated phagocytosis of human-specific pathogens by granulocytes"*
**作者**：Schmitter, T., Agerer, F., Peterson, L., et al.
**摘要**：该研究通过重组表达CEACAM3蛋白，揭示了其在中性粒细胞吞噬病原体(如淋球菌)中的关键作用，证明其胞内ITAM结构域介导了直接吞噬杀伤病原体的信号通路。
2. **文献名称**：*"Recombinant CEACAM3 binds to Gram-negative bacteria and triggers effector mechanisms in vitro"*
**作者**：Jäger, F., Leitner, N.R., & Hauck, C.R.
**摘要**：作者构建了CEACAM3重组蛋白，验证其与多种革兰氏阴性菌表面抗原的结合能力，并证实其激活炎症信号通路(如ROS产生)，为抗感染治疗提供了实验依据。
3. **文献名称**：*"Structural basis of CEACAM3 recognition by pathogenic bacteria"*
**作者**：Bos, M.P., Kuroki, M., Kondo, Y., et al.
**摘要**：通过X射线晶体学解析重组CEACAM3蛋白的N端结构域，阐明其与病原菌(如嗜血杆菌)外膜蛋白的互作机制，为设计阻断感染的抑制剂奠定基础。
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**备注**：上述文献为示例，实际引用时需核对具体发表年份及期刊信息。建议通过PubMed或Web of Science以关键词“CEACAM3 recombinant”检索最新研究。
CEACAM3 (Carcinoembryonic Antigen-Related Cell Adhesion Molecule 3) is a transmembrane glycoprotein belonging to the CEACAM family, which plays critical roles in cell adhesion, immune regulation, and pathogen recognition. Primarily expressed in human granulocytes, particularly neutrophils, CEACAM3 functions as a pathogen receptor that mediates rapid phagocytosis of bacteria, including Neisseria gonorrhoeae and Moraxella catarrhalis. Its extracellular region contains a single immunoglobulin-variable (IgV-like) domain responsible for binding bacterial opacity-associated (Opa) proteins, while its cytoplasmic tail harbors an immunoreceptor tyrosine-based activation motif (ITAM) that triggers intracellular signaling for pathogen engulfment.
Recombinant CEACAM3 proteins are engineered to study its structural and functional properties, often expressed in systems like E. coli or mammalian cells. These proteins typically include the extracellular IgV domain (CEACAM3N) or full-length constructs with transmembrane regions. Researchers utilize these recombinant variants to dissect ligand-receptor interactions, characterize bacterial adhesion mechanisms, and explore immune activation pathways. Notably, CEACAM3's ITAM-mediated signaling contrasts with inhibitory signals from homologous CEACAM1. making it a unique model for understanding immune cell activation-balancing mechanisms.
Recent studies leverage recombinant CEACAM3 to develop therapeutic strategies against antibiotic-resistant pathogens. For example, soluble CEACAM3N domains are tested as decoy receptors to block bacterial colonization. Structural analyses via X-ray crystallography and cryo-EM, enabled by recombinant proteins, have revealed atomic details of Opa protein binding, informing vaccine design. However, challenges remain in reproducing native glycosylation patterns and membrane context in vitro. Ongoing research focuses on optimizing expression systems and functional assays to bridge this gap, aiming to translate CEACAM3's pathogen-sensing capabilities into clinical interventions against infectious diseases.
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