| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DEFa1B |
| Uniprot No | P59665 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-94aa |
| 氨基酸序列 | MRTLAILAAILLVALQAQAEPLQARADEVAAAPEQIAADIPEVVVSLAWDESLAPKHPGSRKNMACYCRIPACIAGERRYGTCIYQGRLWAFCC |
| 预测分子量 | 37.2 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DEFa1B重组蛋白的3篇示例参考文献(注：DEFa1B相关研究较少，以下为模拟内容，实际文献需通过学术数据库核实)：
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1. **文献名称**：Expression and Antimicrobial Characterization of Recombinant DEFa1B in Escherichia coli
**作者**：Smith J, et al.
**摘要**：本研究成功在大肠杆菌中表达并纯化了DEFa1B重组蛋白，证实其对革兰氏阴性菌具有显著抗菌活性，为开发新型抗菌剂提供了实验依据。
2. **文献名称**：Structural Analysis of DEFa1B and Its Role in Innate Immunity
**作者**：Zhang L, Wang H.
**摘要**：通过核磁共振解析了DEFa1B的三维结构，发现其通过破坏病原体细胞膜发挥免疫防御功能，并揭示了关键活性位点。
3. **文献名称**：DEFa1B Recombinant Protein Attenuates Inflammation in Murine Sepsis Models
**作者**：Kim S, et al.
**摘要**：首次报道DEFa1B重组蛋白在脓毒症小鼠模型中抑制过度炎症反应的作用，提示其潜在临床抗炎治疗价值。
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**提示**：若检索不到相关文献，建议：
1. 确认蛋白名称拼写(如是否为DEFB1、DEFA1等);
2. 尝试关键词组合(如“DEFa1B recombinant expression”或“defensin family”);
3. 查阅特定领域期刊(如《Antimicrobial Peptides》《Protein Expression and Purification》)。
DEFa1B, a member of the defensin family, is a small cationic antimicrobial peptide (AMP) encoded by the DEFA1B gene in humans. Defensins are evolutionarily conserved components of innate immunity, broadly categorized into α-, β-, and θ-subfamilies based on disulfide bond patterns. As an α-defensin, DEFa1B is primarily produced by neutrophils and epithelial cells, playing critical roles in host defense against pathogens. Its microbicidal activity stems from its ability to disrupt microbial membranes via electrostatic interactions with negatively charged phospholipids, leading to pore formation and cell lysis. Additionally, DEFa1B exhibits immunomodulatory functions, such as chemoattracting immune cells and regulating inflammatory responses.
Recombinant DEFa1B protein is engineered using biotechnological platforms like bacterial (E. coli) or mammalian expression systems. Production often involves codon optimization, fusion tags (e.g., His-tag), and refolding protocols to maintain its native tertiary structure, which relies on three conserved disulfide bonds. Purification typically employs affinity chromatography followed by enzymatic tag removal. Challenges include achieving proper folding for functional activity and minimizing endotoxin contamination.
Research on recombinant DEFa1B focuses on its therapeutic potential against antibiotic-resistant bacteria, viruses, and fungi. Preclinical studies highlight its synergy with conventional antibiotics and anti-biofilm properties. It is also explored in cancer immunotherapy due to its ability to induce tumor cell apoptosis and enhance dendritic cell maturation. Despite promising applications, clinical translation faces hurdles such as proteolytic degradation in vivo and manufacturing scalability. Ongoing efforts aim to optimize stability through PEGylation or nanoparticle encapsulation while investigating its safety profile in early-phase trials.
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