纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | DEFb126 |
Uniprot No | Q9BYW3 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 21-63aa |
氨基酸序列 | NWYVKKCLND VGICKKKCKP EEMHVKNGWA MCGKQRDCCV PAD |
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DEFb126重组蛋白的假设参考文献示例(注:文献为虚构,仅供示例参考):
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1. **文献名称**: *Structural and Functional Analysis of Recombinant DEFb126 in Sperm Motility*
**作者**: Tollner, T.L., et al.
**摘要**: 本研究通过重组表达人DEFb126蛋白,证实其通过结合精子表面糖基结构增强精子穿透宫颈黏液的能力,并解析了其C端结构域的关键作用。
2. **文献名称**: *DEFb126 Recombinant Protein: A Potential Biomarker for Male Infertility*
**作者**: Zhou, Y., et al.
**摘要**: 利用大肠杆菌系统表达DEFb126重组蛋白,发现其表达水平与男性精子质量下降显著相关,提示其可作为少弱精症的诊断标志物。
3. **文献名称**: *Antimicrobial Properties of Engineered DEFb126 Against Urogenital Pathogens*
**作者**: Bevins, C.L., & Ganz, T.
**摘要**: 通过体外实验证明,重组DEFb126对淋球菌和衣原体具有选择性抑菌活性,其机制可能与细胞膜穿孔作用有关。
4. **文献名称**: *Optimization of DEFb126 Recombinant Expression in Mammalian Cells*
**作者**: Smith, J.P., et al.
**摘要**: 开发了基于CHO细胞的高效DEFb126重组表达体系,通过糖基化修饰提升了蛋白稳定性,为未来临床应用奠定基础。
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注:以上内容为模拟生成,实际文献需通过PubMed/Google Scholar等平台检索确认。
DEFb126. a member of the β-defensin family, is a small cysteine-rich cationic protein primarily studied for its roles in innate immunity and reproductive biology. Initially identified in the human epididymis, DEFb126 is notably expressed in the male reproductive tract and secreted into seminal fluid. It binds to sperm surfaces post-ejaculation, forming a protective glycoprotein coating critical for immune evasion during sperm transit through the female reproductive tract. This coating is hypothesized to shield sperm from innate immune responses, facilitate mucosal penetration, and enhance fertilization potential. Structural studies reveal its conserved disulfide-stabilized fold, characteristic of defensins, which mediates interactions with microbial membranes and host cells.
Interest in recombinant DEFb126 (rDEFb126) stems from its dual functional potential: antimicrobial activity against pathogens (e.g., bacteria, viruses) and immunomodulatory effects in fertility. However, native DEFb126 is challenging to isolate in quantity due to tissue-specific expression and low abundance. Recombinant production, typically using *E. coli* or mammalian expression systems (e.g., HEK293), enables scalable synthesis for functional studies. Purification often involves affinity chromatography and refolding steps to restore native conformation.
Research on rDEFb126 has clarified its molecular interactions, including binding to glycosaminoglycans on sperm and epithelial cells, and its pH-dependent antimicrobial mechanisms. Clinically, it is explored as a biomarker for male infertility, as reduced DEFb126 levels correlate with impaired sperm function. Additionally, synthetic analogs or recombinant forms are being evaluated for therapeutic applications, such as antimicrobial agents or fertility enhancers. Despite progress, challenges remain in optimizing its stability, bioavailability, and tissue-specific targeting. Current studies also investigate its role in non-reproductive contexts, such as airway mucosal immunity, expanding its potential biomedical relevance.
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