| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MUC2 |
| Uniprot No | Q02817 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 36-240aa |
| 氨基酸序列 | VCSTWGNFHYKTFDGDVFRFPGLCDYNFASDCRGSYKEFAVHLKRGPGQAEAPAGVESILLTIKDDTIYLTRHLAVLNGAVVSTPHYSPGLLIEKSDAYTKVYSRAGLTLMWNREDALMLELDTKFRNHTCGLCGDYNGLQSYSEFLSDGVLFSPLEFGNMQKINQPDVVCEDPEEEVAPASCSEHRAECERLLTAEAFADCQDL |
| 预测分子量 | 24.8kDa |
| 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MUC2重组蛋白的3篇参考文献概览，包含文献名称、作者及摘要内容简述：
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1. **文献名称**：*"Production and characterization of recombinant human MUC2 mucin in Drosophila melanogaster S2 cells"*
**作者**：Johansson MEV et al.
**摘要**：研究利用果蝇S2细胞表达重组人MUC2蛋白，优化了表达系统并验证其糖基化修饰特性，证明重组蛋白能形成类似天然MUC2的多聚体结构，为研究肠道黏液屏障功能提供工具。
2. **文献名称**：*"Recombinant MUC2 mucin with a bacterial trehalose coating for studying host-microbe interactions"*
**作者**：Schroeder BO et al.
**摘要**：开发了一种携带海藻糖涂层的重组MUC2蛋白，用于模拟肠道黏液层与微生物的互作，发现其可增强益生菌黏附并抑制病原体定植，提示其在调节菌群平衡中的应用潜力。
3. **文献名称**：*"Expression and purification of the N-terminal domain of MUC2 mucin in Escherichia coli for antibody production"*
**作者**：Ambort D et al.
**摘要**：通过大肠杆菌表达系统成功制备MUC2黏蛋白N端结构域重组蛋白，用于生成特异性抗体，并验证其在结肠组织中的定位，为MUC2功能及疾病关联研究奠定基础。
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**备注**：若需获取全文或更多文献，建议通过PubMed或Web of Science检索DOI编号，或联系作者获取预印本。部分研究可能涉及复杂表达系统优化或特定应用场景，可根据研究方向进一步筛选。
**Background of MUC2 Recombinant Protein**
MUC2 (Mucin 2) is a secreted, high-molecular-weight glycoprotein predominantly expressed by goblet cells in the intestinal and respiratory tracts. As a major component of the mucus layer, it plays a critical role in protecting epithelial surfaces, lubricating tissues, and modulating interactions between the host and microbiota. Structurally, MUC2 consists of a central tandem repeat domain rich in proline, threonine, and serine (PTS domains) that undergoes extensive O-glycosylation, flanked by conserved N- and C-terminal regions involved in polymerization and gel formation.
The recombinant MUC2 protein is engineered to mimic its native structure and function, often produced using mammalian or insect cell expression systems to ensure proper post-translational modifications, particularly glycosylation. Due to the complexity of full-length MUC2 (over 5.000 amino acids), recombinant versions are frequently designed as truncated forms or specific domains (e.g., the variable number of tandem repeats, VNTRs) to facilitate production and purification.
Research on recombinant MUC2 has advanced understanding of mucus biology, including its role in inflammatory bowel diseases (IBD), colorectal cancer, and microbial symbiosis. It serves as a tool to study pathogen-mucus interactions, drug delivery mechanisms, and therapeutic strategies targeting mucosal barriers. Challenges in working with recombinant MUC2 include maintaining its polymeric structure, solubility, and glycan diversity, which are critical for functional studies. Recent efforts focus on optimizing expression systems and glycoengineering to enhance its biochemical fidelity for biomedical applications.
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