| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MUC1 |
| Uniprot No | P15941 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1095-1140aa |
| 氨基酸序列 | LRPGSVVVQLTLAFREGTINVHDVETQFNQYKTEAASRYNLTISDVSG |
| 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3条关于MUC1重组蛋白的参考文献示例(注：文献信息为模拟示例，实际引用需核实原文)：
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1. **文献名称**：*Expression and Purification of Recombinant MUC1 Glycoprotein in Escherichia coli for Cancer Immunotherapy*
**作者**：Smith A, et al.
**摘要**：研究报道了一种在大肠杆菌系统中高效表达MUC1重组蛋白的方法，通过优化密码子和纯化策略获得高产量蛋白，并证明其在小鼠模型中可诱导特异性抗肿瘤免疫反应。
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2. **文献名称**：*Structural Characterization of Glycosylated MUC1 Tandem Repeat Domain Produced in Insect Cells*
**作者**：Lee B, et al.
**摘要**：利用杆状病毒-昆虫细胞表达系统成功制备了糖基化修饰的MUC1重组蛋白，通过质谱和X射线晶体学解析其结构，为研究MUC1在癌症中的异常糖基化机制提供工具。
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3. **文献名称**：*Recombinant MUC1 Protein as a Serological Biomarker for Early Detection of Breast Cancer*
**作者**：Wang C, et al.
**摘要**：开发基于重组MUC1蛋白的ELISA检测方法，验证其在乳腺癌患者血清中的诊断价值，结果显示高灵敏度和特异性，优于传统肿瘤标志物。
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**提示**：实际文献需通过PubMed、Web of Science或Google Scholar搜索关键词(如"MUC1 recombinant protein expression"或"MUC1 cancer biomarker")获取。建议优先选择近5年高被引论文或权威期刊(如*Nature Communications*、*Cancer Research*)。
**Background of MUC1 Recombinant Protein**
MUC1 (Mucin 1) is a transmembrane glycoprotein predominantly expressed on the apical surface of epithelial cells in various tissues, including the respiratory, gastrointestinal, and reproductive tracts. It plays a critical role in protecting mucosal surfaces by forming a physical barrier and participating in cell signaling. Structurally, MUC1 consists of a large extracellular domain with variable numbers of tandem repeats (VNTRs) rich in serine, threonine, and proline residues, which serve as sites for O-glycosylation. The protein also includes a transmembrane domain and a cytoplasmic tail involved in intracellular signaling pathways.
In cancer, MUC1 undergoes abnormal overexpression and hypo-glycosylation, exposing cryptic epitopes that promote tumor progression, metastasis, and immune evasion. These characteristics make it a prominent therapeutic target and biomarker for adenocarcinomas (e.g., breast, pancreatic, and lung cancers). Recombinant MUC1 proteins are engineered to mimic specific domains (e.g., the VNTR region) for research and clinical applications. They are produced using expression systems like mammalian cells (e.g., CHO) or bacteria (e.g., *E. coli*), enabling scalable production with controlled post-translational modifications.
Recombinant MUC1 is widely used to study tumor immunology, develop diagnostic assays, and design vaccines or targeted therapies. For instance, MUC1-based vaccines aim to stimulate immune responses against cancer-specific epitopes, while antibody-drug conjugates (ADCs) leverage recombinant MUC1 as a homing signal for cytotoxic payloads. Challenges remain in optimizing glycosylation patterns and overcoming immune tolerance, but ongoing advances in protein engineering and glyco-biology continue to enhance its therapeutic potential.
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