| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DEFa6 |
| Uniprot No | Q01524 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-100aa |
| 氨基酸序列 | MRTLTILTAVLLVALQAKAEPLQAEDDPLQAKAYEADAQEQRGANDQDFA VSFAEDASSSLRALGSTRAFTCHCRRSCYSTEYSYGTCTVMGINHRFCCL |
| 预测分子量 | 37 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DEFa6重组蛋白的假设性参考文献示例(文献内容为虚构，仅作演示)：
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1. **标题**：*Recombinant DEFa6 Protein Exhibits Broad-Spectrum Antimicrobial Activity In Vitro*
**作者**：Zhang, L. et al.
**摘要**：研究报道了通过大肠杆菌表达系统成功纯化DEFa6重组蛋白，并证实其对革兰氏阳性菌(如金黄色葡萄球菌)和真菌(如白色念珠菌)具有显著抑制活性，MIC值低于10 μg/mL。
2. **标题**：*Engineering DEFa6 for Enhanced Stability and Therapeutic Potential in Chronic Wound Infections*
**作者**：Smith, J.R. & Patel, K.
**摘要**：通过定点突变优化DEFa6重组蛋白的结构稳定性，发现其突变体在模拟体液环境中半衰期延长2倍，并在糖尿病小鼠模型中加速感染创面愈合。
3. **标题**：*DEFa6 Recombinant Protein Modulates Inflammatory Response in Intestinal Epithelial Cells*
**作者**：Chen, X. et al.
**摘要**：研究发现DEFa6重组蛋白通过TLR4/NF-κB信号通路抑制LPS诱导的肠道上皮细胞炎症因子(IL-6、TNF-α)释放，提示其在炎症性肠病治疗中的潜在应用。
4. **标题**：*Structural and Functional Characterization of DEFa6 Fusion Protein in Mammalian Expression Systems*
**作者**：Gupta, S. et al.
**摘要**：利用哺乳动物细胞(HEK293)表达DEFa6-Fc融合蛋白，通过晶体学解析其三维结构，并验证其与宿主细胞膜磷脂的相互作用机制，为其靶向递送提供理论依据。
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注：以上文献为示例性内容，实际研究中请通过PubMed、Web of Science等数据库检索真实文献。
DEFa6 (Defensin Alpha 6) is a small cationic peptide belonging to the alpha-defensin family, which plays a critical role in innate immunity. Defensins are evolutionarily conserved antimicrobial peptides broadly distributed in vertebrates, functioning as first-line defenders against pathogens such as bacteria, viruses, and fungi. Human alpha-defensins are primarily secreted by neutrophils (HNP1-4) or Paneth cells in the small intestine (HD5-6). DEFa6. also known as human defensin 6 (HD6), is encoded by the DEFA6 gene and is notably expressed in Paneth cells. Unlike other defensins that directly disrupt microbial membranes, HD6 exhibits unique mechanisms: it self-assembles into fibrils or nanonets to entrap pathogens, limiting their invasion across mucosal surfaces.
Recombinant DEFa6 protein is produced using biotechnological systems (e.g., E. coli or mammalian cell expression) for research and therapeutic exploration. Its structure includes six conserved cysteine residues forming three disulfide bonds, stabilizing a β-sheet-rich fold. Studies highlight its role in gut homeostasis, microbiome regulation, and protection against enteric infections (e.g., Salmonella). Emerging evidence suggests HD6 may modulate immune responses and exhibit anti-inflammatory or anticancer properties, though mechanisms remain under investigation.
Interest in recombinant DEFa6 stems from its potential in antimicrobial therapy, particularly amid rising antibiotic resistance. It is also explored as a biomarker for inflammatory bowel disease (IBD) and colorectal cancer. Challenges include optimizing stable production, minimizing cytotoxicity, and enhancing bioavailability. Ongoing research aims to harness its unique pathogen-trapping mechanism for novel antimicrobial strategies or immunomodulatory applications.
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