| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MUC21 |
| Uniprot No | Q5SSG8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 501-566aa |
| 氨基酸序列 | CVRNSLSLRNTFNTAVYHPHGLNHGLGPGPGGNHGAPHRPRWSPNWFWRRPVSSIAMEMSGRNSGP |
| 预测分子量 | 7.3 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. |
以下是模拟的关于MUC21重组蛋白的参考文献示例(请注意，部分文献信息为假设性概括，实际文献需通过学术数据库查询确认)：
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1. **文献名称**: *"Recombinant MUC21 Protein Expression in Lung Cancer and Its Role in Tumor Metastasis"*
**作者**: Zhang Y, et al.
**摘要**: 本研究通过哺乳动物表达系统成功重组表达了MUC21蛋白，并发现其在肺癌细胞中高表达。实验表明，MUC21重组蛋白可激活EGFR信号通路，促进肿瘤细胞的迁移和侵袭。
2. **文献名称**: *"Structural Characterization of MUC21 Glycoprotein Expressed in HEK293 Cells"*
**作者**: Kim S, et al.
**摘要**: 利用HEK293细胞系统表达并纯化重组MUC21蛋白，通过质谱和糖基化分析揭示了其复杂的O-糖基化修饰模式，为研究其与宿主免疫系统的相互作用提供了结构基础。
3. **文献名称**: *"MUC21 Recombinant Protein as a Potential Biomarker for Head and Neck Squamous Cell Carcinoma"*
**作者**: Chen L, et al.
**摘要**: 通过原核系统表达重组MUC21蛋白，并验证其在头颈鳞癌患者血清中的特异性高表达，提示其可能作为早期诊断的生物标志物。
4. **文献名称**: *"MUC21 Modulates Airway Epithelial Immune Responses via TLR2/4 Signaling"*
**作者**: Lee JH, et al.
**摘要**: 研究利用重组MUC21蛋白体外刺激气道上皮细胞，发现其通过TLR2/4受体激活NF-κB通路，增强促炎因子分泌，可能在慢性呼吸道疾病中起调控作用。
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**备注**：以上文献为基于领域研究的模拟示例，实际文献需通过PubMed、Web of Science或Google Scholar等平台以关键词“MUC21 recombinant protein”或“MUC21 expression”检索获取。建议结合具体研究方向筛选近年高影响力论文。
**Background of MUC21 Recombinant Protein**
MUC21. a member of the mucin family, is a transmembrane glycoprotein predominantly expressed in epithelial tissues, including the respiratory tract, skin, and gastrointestinal system. Mucins are characterized by their heavily glycosylated extracellular domains, which contribute to protective mucosal barriers, cell adhesion, and signaling. MUC21. also known as epiglycan, plays roles in maintaining epithelial integrity, immune modulation, and cellular communication. Its structure includes a large extracellular region with tandem repeats rich in serine, threonine, and proline residues—sites for O-glycosylation—a transmembrane domain, and a short cytoplasmic tail. Dysregulation of MUC21 has been implicated in pathologies such as cancer, chronic inflammation, and autoimmune disorders, where its overexpression or altered glycosylation may promote tumor progression, immune evasion, or aberrant inflammation.
Recombinant MUC21 protein is engineered using biotechnological platforms (e.g., mammalian or insect cell systems) to mimic the native protein’s structure and post-translational modifications, particularly glycosylation. This recombinant form enables researchers to study MUC21’s biological functions, interactions with immune cells (e.g., through lectin receptors), and mechanisms in disease contexts. It is also explored for therapeutic applications, such as developing monoclonal antibodies, vaccines, or decoy proteins to block pathogenic signaling. Challenges in production include preserving its complex glycosylation patterns, which are critical for functional studies. Current research focuses on elucidating MUC21’s role in tumor microenvironments, its potential as a diagnostic biomarker, and its utility in designing targeted therapies against epithelial cancers or inflammatory conditions.
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