| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SP-B |
| Uniprot No | Q15427 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-424aa |
| 氨基酸序列 | AAGPISERN QDATVYVGGL DEKVSEPLLW ELFLQAGPVV NTHMPKDRVT GQHQGYGFVE FLSEEDADYA IKIMNMIKLY GKPIRVNKAS AHNKNLDVGA NIFIGNLDPE IDEKLLYDTF SAFGVILQTP KIMRDPDTGN SKGYAFINFA SFDASDAAIE AMNGQYLCNR PITVSYAFKK DSKGERHGSA AERLLAAQNP LSQADRPHQL FADAPPPPSA PNPVVSSLGS GLPPPGMPPP GSFPPPVPPP GALPPGIPPA MPPPPMPPGA AGHGPPSAGT PGAGHPGHGH SHPHPFPPGG MPHPGMSQMQ LAHHGPHGLG HPHAGPPGSG GQPPPRPPPG MPHPGPPPMG MPPRGPPFGS PMGHPGPMPP HGMRGPPPLM PPHGYTGPPR PPPYGYQRGP LPPPRPTPRP PVPPRGPLRG PLPQ |
| 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. |
以下是关于重组SP-B蛋白的参考文献概览(内容基于真实研究领域，具体文献标题和作者为模拟示例)：
1. **"Recombinant Surfactant Protein B in the Treatment of Neonatal Respiratory Distress Syndrome"**
- 作者：Johannsen, H. et al.
- 摘要：研究重组SP-B蛋白联合脂质用于早产儿呼吸窘迫综合征的临床试验，证明其可改善氧合并减少机械通气需求，安全性良好。
2. **"Structural and Functional Characterization of Recombinant SP-B Expressed in E. coli"**
- 作者：Curstedt, T. & Jobe, A.
- 摘要：报道通过大肠杆菌表达重组SP-B蛋白的方法，纯化后蛋白与天然SP-B结构相似，并在体外模型中恢复肺表面活性功能。
3. **"Role of Recombinant SP-B in Acute Lung Injury Models"**
- 作者：Wang, L. et al.
- 摘要：动物实验显示，雾化吸入重组SP-B能减轻脂多糖诱导的急性肺损伤，机制涉及降低肺泡炎症和增强表面活性膜稳定性。
4. **"Optimization of Mammalian Cell Expression Systems for High-Yield SP-B Production"**
- 作者：Zhang, Y. et al.
- 摘要：对比CHO细胞与HEK293系统表达重组SP-B的工艺，优化后产量提升3倍，且蛋白具备更优的磷脂结合活性。
注：以上为领域内典型研究方向示例，实际文献需通过学术数据库检索确认。
Surfactant protein B (SP-B) is a critical component of pulmonary surfactant, a lipoprotein complex essential for reducing surface tension at the air-liquid interface in the alveoli, preventing lung collapse during expiration. SP-B, encoded by the *SFTPB* gene, is a hydrophobic protein synthesized by alveolar type II cells as a precursor (pro-SP-B) that undergoes proteolytic processing to form the mature, functionally active peptide. It plays a vital role in organizing surfactant phospholipids and stabilizing lipid membranes, ensuring efficient respiration. Genetic deficiencies or mutations in SP-B cause severe respiratory distress in newborns, often fatal without intervention.
Traditional surfactant replacement therapies, derived from animal lungs, contain SP-B but face limitations such as batch variability, immunogenicity risks, and ethical concerns. Recombinant SP-B (rSP-B) production emerged to address these challenges, leveraging biotechnological platforms like bacterial, yeast, or mammalian cell systems. However, replicating SP-B’s complex structure—requiring precise folding, disulfide bonding, and lipid interactions—has proven difficult. Early efforts focused on simplified SP-B mimics or peptide analogs, but recent advances in protein engineering and expression systems have improved the yield and functionality of full-length rSP-B.
Therapeutic applications of rSP-B aim to enhance synthetic surfactant formulations for treating neonatal respiratory distress syndrome (NRDS) and hereditary SP-B deficiency. Its recombinant nature offers consistency, scalability, and reduced immunogenicity compared to animal-derived products. Despite progress, obstacles remain, including maintaining structural stability during production and ensuring bioavailability in clinical settings. Ongoing research explores hybrid surfactants combining rSP-B with other surfactant proteins (e.g., SP-C) to mimic natural surfactant more closely. Successful development could revolutionize respiratory care, providing safer, standardized therapies for acute and genetic lung disorders.
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