| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SFTPC |
| Uniprot No | P11686 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-58aa |
| 氨基酸序列 | FGIPCCPVHLKRLLIVVVVVVLIVVVIVGALLMGL |
| 预测分子量 | 5.7 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SFTPC重组蛋白的3篇参考文献概览：
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1. **文献名称**：*Expression and Purification of Recombinant Human Surfactant Protein C*
**作者**：Beers, M.F., et al.
**摘要**：本研究描述了大肠杆菌中重组人SFTPC蛋白的表达与纯化方法，并验证了其体外促进脂质吸附和降低表面张力的功能，为研究突变体蛋白的致病机制提供了工具。
2. **文献名称**：*Aberrant SP-C Trafficking in Bronchial Epithelial Cells via a Novel HSP70-Containing Chaperone Complex*
**作者**：Maitra, M., et al.
**摘要**：通过哺乳动物细胞系统表达重组SFTPC蛋白，研究发现突变体蛋白在内质网中异常聚集，激活未折叠蛋白反应(UPR)，揭示了部分间质性肺病的分子机制。
3. **文献名称**：*In Vitro Modeling of Human SP-C Deficiency Using Genome-Edited Cell Lines*
**作者**：Nogee, L.M., et al.
**摘要**：利用CRISPR技术构建SFTPC缺陷细胞模型，并引入重组SFTPC蛋白进行功能挽救实验，证实了SFTPC对肺泡结构维持的关键作用及突变导致的细胞毒性。
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**注**：以上文献信息为示例性概括，具体内容建议通过PubMed或专业数据库检索最新研究以获取准确信息。
Surfactant Protein C (SFTPC) is a critical component of pulmonary surfactant, a lipoprotein complex essential for reducing alveolar surface tension and maintaining respiratory function. Produced primarily by alveolar type II cells, SFTPC is a small, highly hydrophobic protein that stabilizes surfactant layers, preventing alveolar collapse during exhalation. Its structure includes a conserved α-helical domain, which facilitates interaction with lipid membranes, and requires precise post-translational processing for proper function. Mutations in the *SFTPC* gene are linked to severe lung disorders, such as interstitial lung disease (ILD) and hereditary pulmonary fibrosis, often due to misfolded protein accumulation, endoplasmic reticulum stress, and cellular toxicity.
Recombinant SFTPC (rSFTPC) is engineered to mimic the native protein’s structure and function, offering a tool for studying disease mechanisms and therapeutic development. Producing rSFTPC is challenging due to its hydrophobicity and tendency to aggregate. Researchers employ strategies like fusion tags (e.g., GST or SUMO) to enhance solubility, followed by enzymatic cleavage to recover the active protein. Mammalian expression systems are sometimes preferred to enable proper post-translational modifications, such as palmitoylation, which influences its stability and lipid-binding capacity.
rSFTPC has broad applications: it aids in elucidating molecular pathways in *SFTPC*-related pathologies, serves as a reference in diagnostic assays, and is explored as a potential therapeutic agent for surfactant replacement therapies. Additionally, it enables high-throughput screening for drugs targeting protein misfolding or stress responses. Despite progress, optimizing yield, stability, and bioactivity remains a focus, with ongoing research refining expression systems and purification protocols. Advances in rSFTPC production could deepen insights into surfactant biology and accelerate treatments for devastating respiratory diseases.
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