| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SLPI |
| Uniprot No | P03973 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-132aa |
| 氨基酸序列 | SGKSFKAGVCPPKKSAQCLRYKKPECQSDWQCPGKKRCCPDTCGIKCLDPVDTPNPTRRKPGKCPVTYGQCLMLNPPNFCEMDGQCKRDLKCCMGMCGKSCVSPVKA |
| 预测分子量 | 16.7 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SLPI(分泌性白细胞蛋白酶抑制剂)重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: *"Production and characterization of recombinant human secretory leukocyte protease inhibitor in Pichia pastoris"*
**作者**: Tomee, J. F., et al.
**摘要**: 该研究利用毕赤酵母表达系统成功表达并纯化了重组人SLPI蛋白。作者验证了其抑制弹性蛋白酶和抗炎活性的功能，并证明其结构与天然SLPI相似，为大规模生产提供了可行方案。
2. **文献名称**: *"Recombinant SLPI reduces inflammation and prevents alveolar epithelial injury in a murine model of acute lung injury"*
**作者**: Lentsch, A. B., et al.
**摘要**: 在小鼠急性肺损伤模型中，重组SLPI通过抑制中性粒细胞蛋白酶(如弹性蛋白酶)和调节促炎细胞因子(如TNF-α、IL-6)，显著减轻肺部炎症反应，并保护肺泡上皮细胞完整性。
3. **文献名称**: *"Antiviral activity of secretory leukocyte protease inhibitor against HIV-1 infection in vitro"*
**作者**: McNeely, T. B., et al.
**摘要**: 该研究证实重组SLPI能够通过阻断HIV-1病毒进入宿主细胞的机制(可能与抑制蛋白酶活性及干扰病毒包膜融合有关)，在体外实验中有效降低HIV-1对单核细胞的感染率。
---
注：以上文献信息为示例性概括，实际引用时建议通过PubMed或Web of Science核对具体细节。
**Background of Recombinant SLPI Protein**
Secretory Leukocyte Protease Inhibitor (SLPI), a 11-12 kDa endogenous protein, is a serine protease inhibitor primarily produced by epithelial cells, macrophages, and neutrophils. It plays a critical role in modulating inflammation, tissue repair, and innate immunity. SLPI inhibits proteolytic enzymes such as neutrophil elastase, cathepsin G, and trypsin, thereby protecting tissues from protease-mediated damage during inflammatory responses. Additionally, it exhibits anti-microbial and anti-viral properties, contributing to host defense mechanisms. Beyond protease inhibition, SLPI modulates immune cell activity by suppressing NF-κB signaling, reducing pro-inflammatory cytokine production, and promoting resolution of inflammation.
Recombinant SLPI protein is produced using genetic engineering techniques, typically expressed in *E. coli*, yeast, or mammalian cell systems to ensure high purity and bioactivity. This engineered form retains the functional domains of native SLPI, enabling scalable production for research and therapeutic applications. Its stability and bioavailability are often enhanced through formulation optimizations.
Research highlights SLPI’s therapeutic potential in conditions like chronic obstructive pulmonary disease (COPD), cystic fibrosis, arthritis, and wound healing, where excessive protease activity and inflammation drive pathology. It is also being explored in HIV infection due to its ability to block viral entry into target cells. Furthermore, recombinant SLPI has shown promise in mitigating acute lung injury and sepsis in preclinical models.
Despite its versatility, challenges remain in optimizing delivery methods and understanding tissue-specific interactions. Ongoing studies aim to refine its clinical applications, leveraging recombinant technology to address unmet needs in inflammatory and infectious diseases.
×
