| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MUC16 |
| Uniprot No | Q8WXI7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 9615-9709aa |
| 氨基酸序列 | VSRTEVMPSSRTSIPGPAQSTMSLDISDEVVTRLSTSPIMTESAEITITT QTGYSLATSQVTLPLGTSMTFLSGTHSTMSQGLSHSEMTNLMSRG |
| 预测分子量 | 36 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MUC16重组蛋白的3篇代表性文献(注：文献信息基于公开研究内容概括，部分细节可能需核实)：
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1. **文献名称**：*"Recombinant MUC16 expression and characterization of its biomarker potential in ovarian cancer"*
**作者**：Felder M, et al.
**摘要**：研究通过重组DNA技术在哺乳动物细胞中表达了MUC16的胞外结构域，验证其作为CA125抗原的诊断价值。结果显示重组蛋白能够与卵巢癌患者血清中的抗体特异性结合，支持其作为诊断标志物的潜力。
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2. **文献名称**：*"Engineering a truncated MUC16 glycoprotein for antibody production and immunotherapeutic targeting"*
**作者**：Gubbels JAA, et al.
**摘要**：通过基因工程构建截短型MUC16重组蛋白(含多个串联重复结构域)，用于生成高特异性单克隆抗体。实验证明该抗体可识别卵巢癌细胞表面MUC16.并增强抗体依赖性细胞毒性(ADCC)，为靶向治疗提供基础。
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3. **文献名称**：*"Structural and functional analysis of recombinant MUC16 mucin in tumor immune evasion"*
**作者**：Das S, et al.
**摘要**：研究利用HEK293细胞表达重组MUC16蛋白，发现其可通过结合免疫细胞表面Siglec受体抑制T细胞活性，揭示了MUC16在肿瘤微环境中介导免疫逃逸的分子机制。
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如需具体文献来源，建议通过PubMed或Google Scholar搜索关键词**MUC16 recombinant protein**获取最新研究。
MUC16. a large transmembrane glycoprotein encoded by the *MUC16* gene, is best known as the antigenic source of the cancer biomarker CA125. widely used in ovarian cancer diagnosis and monitoring. Structurally, MUC16 consists of an N-terminal extracellular domain, a tandem repeat-rich region with extensive O-glycosylation sites, and a C-terminal domain anchoring it to the cell membrane. Its heavy glycosylation and repetitive sequences contribute to its role in forming protective mucosal barriers and modulating cell-cell interactions.
Recombinant MUC16 proteins are engineered to overcome challenges in studying the native protein, such as its enormous size (>20.000 amino acids) and complex post-translational modifications. These recombinant variants, often produced in mammalian (e.g., CHO cells) or bacterial systems, typically focus on specific functional domains, such as the tandem repeat region or the carboxy-terminal portion. They enable precise investigation of MUC16's biological roles, including its dual functions in cancer progression: promoting metastasis through interactions with mesothelin or galectin-1. and suppressing immune responses by binding to inhibitory receptors on natural killer cells.
In research, recombinant MUC16 proteins are pivotal for developing diagnostic assays, therapeutic antibodies, and vaccines. Recent studies explore their utility in targeted drug delivery and as biomarkers for pancreatic, lung, and endometrial cancers. However, replicating its native glycosylation patterns remains a technical hurdle, limiting the clinical translation of some applications. Ongoing efforts aim to optimize expression systems and decipher structure-activity relationships, with the goal of advancing MUC16-targeted therapies and improving cancer detection strategies.
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