| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | BPI |
| Uniprot No | P17213 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 32-487aa |
| 氨基酸序列 | VNPGVVVRISQKGLDYASQQGTAALQKELKRIKIPDYSDSFKIKHLGKGHYSFYSMDIREFQLPSSQISMVPNVGLKFSISNANIKISGKWKAQKRFLKMSGNFDLSIEGMSISADLKLGSNPTSGKPTITCSSCSSHINSVHVHISKSKVGWLIQLFHKKIESALRNKMNSQVCEKVTNSVSSELQPYFQTLPVMTKIDSVAGINYGLVAPPATTAETLDVQMKGEFYSENHHNPPPFAPPVMEFPAAHDRMVYLGLSDYFFNTAGLVYQEAGVLKMTLRDDMIPKESKFRLTTKFFGTFLPEVAKKFPNMKIQIHVSASTPPHLSVQPTGLTFYPAVDVQAFAVLPNSSLASLFLIGMHTTGSMEVSAESNRLVGELKLDRLLLELKHSNIGPFPVELLQDIMNYIVPILVLPRVNEKLQKGFPLPTPARVQLYNVVLQPHQNFLLFGADVVYK |
| 预测分子量 | 57.6 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BPI(杀菌/通透性增加蛋白)重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Recombinant BPI protein (rBPI21) protects against meningococcal sepsis by reducing endotoxin and bacterial load"*
**作者**：Giroir BP, et al.
**摘要**：该研究通过动物模型和临床试验证明，重组BPI蛋白(rBPI21)能有效中和革兰氏阴性菌释放的内毒素，降低败血症患者的炎症反应和细菌负荷，显著改善生存率。
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2. **文献名称**：*"Antibacterial and anti-inflammatory effects of recombinant BPI in a murine model of Pseudomonas aeruginosa pneumonia"*
**作者**：Levy O, et al.
**摘要**：实验表明，重组BPI蛋白通过直接杀灭铜绿假单胞菌并抑制其内毒素活性，减轻肺部感染小鼠的炎症损伤，提示其在多重耐药菌感染治疗中的潜力。
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3. **文献名称**：*"Structural and functional characterization of a recombinant N-terminal fragment of bactericidal/permeability-increasing protein (rBPI21)"*
**作者**：Little RG, et al.
**摘要**：该研究解析了重组BPI蛋白片段(rBPI21)的晶体结构，揭示其通过疏水结构域结合细菌脂多糖(LPS)的分子机制，为优化蛋白设计提供理论基础。
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如需更具体的文献年份或期刊信息，可进一步补充说明。
**Background of BPI Recombinant Protein**
Bactericidal/Permeability-Increasing Protein (BPI) is a naturally occurring host defense protein first identified in the 1970s. It is predominantly produced by neutrophils, a type of white blood cell, and plays a critical role in innate immunity by targeting Gram-negative bacteria. BPI binds to lipopolysaccharides (LPS) on bacterial outer membranes through its N-terminal domain, exerting potent bactericidal activity and neutralizing endotoxins that trigger inflammatory responses. Its dual function—direct microbial killing and LPS detoxification—makes it a key player in combating infections and modulating sepsis-related pathologies.
The human BPI gene encodes a 55 kDa protein composed of two functional domains: a cytotoxic N-terminal domain responsible for antimicrobial activity and a C-terminal domain that facilitates protein anchoring and immune modulation. Recombinant BPI (rBPI) is engineered using genetic cloning techniques, often expressed in *E. coli* or mammalian cell systems, to mimic the natural protein’s structure and function. Early research focused on rBPI21. a truncated version retaining the N-terminal bioactive region, which showed promise in preclinical and clinical studies for sepsis and endotoxemia.
Therapeutic interest in BPI stems from its ability to address antibiotic resistance and inflammation. Clinical trials have explored its use in conditions like severe sepsis, cystic fibrosis, and trauma-induced immune dysregulation. However, challenges such as short plasma half-life, potential immunogenicity, and high production costs have limited widespread clinical adoption. Recent advances in protein engineering, including PEGylation and fusion technologies, aim to enhance stability and bioavailability.
Overall, BPI recombinant protein represents a bridge between innate immunity and therapeutic innovation, with ongoing research refining its application in infectious and inflammatory diseases.
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