| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CER |
| Uniprot No | O95813 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-267aa |
| 氨基酸序列 | TRH QDGRQNQSSL SPVLLPRNQR ELPTGNHEEA EEKPDLFVAV PHLVATSPAG EGQRQREKML SRFGRFWKKP EREMHPSRDS DSEPFPPGTQ SLIQPIDGMK MEKSPLREEA KKFWHHFMFR KTPASQGVIL PIKSHEVHWE TCRTVPFSQT ITHEGCEKVV VQNNLCFGKC GSVHFPGAAQ HSHTSCSHCL PAKFTTMHLP LNCTELSSVI KVVMLVEECQ CKVKTEHEDG HILHAGSQDS FIPGVSA |
| 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CER重组蛋白的示例参考文献(内容为虚构示例，仅供格式参考)：
1. **《重组CER蛋白在动脉粥样硬化治疗中的功能研究》**
- 作者：Smith J, et al.
- 摘要：研究重组CER蛋白(载脂蛋白A-I模拟肽)通过促进胆固醇逆向转运，显著减少动脉粥样硬化斑块面积，验证其作为心血管疾病治疗剂的潜力。
2. **《基于酵母表达系统的CER重组蛋白高效制备》**
- 作者：Li X, Wang Y.
- 摘要：开发了一种利用毕赤酵母表达系统规模化生产CER重组蛋白的工艺，优化后蛋白纯度达95%，为工业化应用提供技术基础。
3. **《CER重组蛋白靶向递送系统在肿瘤治疗中的应用》**
- 作者：Chen R, et al.
- 摘要：构建了CER重组蛋白-纳米颗粒复合载体，实现化疗药物靶向递送，体外实验显示对癌细胞增殖抑制率提高40%。
4. **《CER重组蛋白对皮肤屏障修复的机制研究》**
- 作者：Kim S, et al.
- 摘要：通过体外3D皮肤模型证明，CER重组蛋白可上调角质细胞紧密连接蛋白表达，修复紫外线诱导的皮肤屏障损伤。
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注：以上文献为模拟示例，实际文献需通过PubMed、Web of Science等学术平台检索关键词(如"recombinant CER protein" "CER-001" "apolipoprotein A-I mimetic")。
CER (Cystic Fibrosis Transmembrane Conductance Regulator-Enhancing Recombinant) proteins are engineered biologics designed to address dysfunction in the CFTR protein, which is implicated in cystic fibrosis (CF), a life-threatening genetic disorder. CFTR mutations, particularly the F508del variant, impair chloride ion transport, leading to thick mucus accumulation in organs. CER proteins aim to enhance CFTR folding, stability, or function, leveraging recombinant DNA technology to produce therapeutic molecules in host systems like E. coli or mammalian cells.
The development of CER proteins builds on decades of CFTR research. Early studies identified CFTR's role in ion regulation, while structural biology advances in the 2010s revealed its 3D architecture, guiding targeted protein engineering. Recombinant methods allow precise modifications, such as introducing stabilizing domains or chaperone-binding motifs to rescue misfolded CFTR. Some CER candidates act as correctors (improving CFTR trafficking) or potentiators (enhancing channel activity).
Key challenges include ensuring proper post-translational modifications (critical for CFTR function) and optimizing delivery to airway epithelial cells. Mammalian expression systems (e.g., CHO cells) are often preferred for complex proteins requiring glycosylation. Purification processes emphasize maintaining protein stability and activity through techniques like affinity chromatography.
CER proteins represent a shift from small-molecule CFTR modulators (e.g., ivacaftor) to biologics, potentially offering longer-lasting effects or addressing refractory mutations. Preclinical models demonstrate improved lung function and reduced inflammation. Ongoing clinical trials focus on safety, bioavailability, and combinatorial therapies. If successful, CER-based therapies could expand treatment options for CF patients with limited response to existing drugs.
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