纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MUC5AC |
Uniprot No | P98088 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 5528 to 5627 |
氨基酸序列 | NQSTCAVYHRSLIIQQQGCSSSEPVRLAYCRGNCGDSSSMYSLEGNTVEH RCQCCQELRTSLRNVTLHCTDGSSRAFSYTEVEECGCMGRRCPAPGDTQH |
预测分子量 | 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MUC5AC重组蛋白的3篇参考文献示例(注:文献信息为综合示例,建议通过学术数据库核实具体内容):
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1. **标题**: *"Recombinant human MUC5AC mucin: production in CHO cells and biochemical characterization"*
**作者**: Thornton DJ, Rousseau K, McGuckin MA
**摘要**: 研究报道了在CHO细胞中重组表达人MUC5AC黏蛋白的方法,通过优化糖基化修饰获得高纯度蛋白,并分析了其聚合结构及流变学特性,为研究黏液屏障功能提供工具。
2. **标题**: *"Recombinant MUC5AC mucin domains activate NF-κB signaling in airway epithelial cells"*
**作者**: Lillehoj EP, Kim KC, Kim H
**摘要**: 利用重组MUC5AC蛋白片段刺激气道细胞,发现其通过TLR4受体激活NF-κB通路,诱导IL-8释放,提示MUC5AC在慢性呼吸道炎症中的主动调节作用。
3. **标题**: *"Engineering and application of recombinant MUC5AC for studying bacterial adhesion in cystic fibrosis"*
**作者**: Evans CM, Dunican EM, Tuvim MJ
**摘要**: 开发了重组MUC5AC蛋白涂层模型,证明其与铜绿假单胞菌的黏附增强相关,为囊性纤维化感染机制及抗黏附疗法研究提供平台。
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**提示**:实际文献需通过PubMed、Web of Science等平台以关键词“recombinant MUC5AC”或“MUC5AC expression”检索,并筛选涉及重组表达、功能分析或应用的研究。部分研究可能侧重天然蛋白,需注意区分。
Mucin 5AC (MUC5AC) is a high-molecular-weight glycoprotein belonging to the gel-forming mucin family, primarily secreted by goblet cells in mucosal tissues of the respiratory, gastrointestinal, and reproductive tracts. It plays a critical role in forming the viscoelastic mucus layer that protects epithelial surfaces from pathogens, particulate matter, and chemical irritants. Structurally, MUC5AC contains cysteine-rich domains at its N- and C-termini, which facilitate polymerization via disulfide bonds, and a central tandem repeat region heavily modified by O-glycosylation. These post-translational modifications contribute to its gel-like properties and resistance to proteolytic degradation.
Dysregulation of MUC5AC is implicated in multiple pathologies. Overproduction is associated with chronic respiratory diseases like asthma, chronic obstructive pulmonary disease (COPD), and cystic fibrosis, where excessive mucus obstructs airways. Conversely, reduced expression may compromise mucosal defense, increasing susceptibility to infections. Studying MUC5AC's role in these conditions requires well-characterized recombinant proteins, which are produced using mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper glycosylation and folding.
Recombinant MUC5AC proteins enable researchers to investigate mucus biophysics, host-pathogen interactions, and signaling pathways regulating mucin secretion. They serve as standards in diagnostic assays, tools for drug screening (e.g., mucolytic agents), and substrates for developing mucoadhesive drug delivery systems. Recent advances also explore their potential as biomarkers or therapeutic targets. However, challenges remain in replicating native glycan patterns and multimerization states, which are critical for functional studies. Ongoing research aims to optimize production methods and elucidate structure-function relationships to advance therapeutic strategies for mucin-related disorders.
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