| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | fla |
| Uniprot No | P11089 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-336aa |
| 氨基酸序列 | MIINHNTSAINASRNNGINAANLSKTQEKLSSGYRINRASDDAAGMGVSGKINAQIRGLSQASRNTSKAINFIQTTEGNLNEVEKVLVRMKELAVQSGNGTYSDADRGSIQIEIEQLTDEINRIADQAQYNQMHMLSNKSASQNVRTAEELGMQPAKINTPASLSGSQASWTLRVHVGANQDEAIAVNIYAANVANLFSGEGAQTAQAAPVQEGVQQEGAQQPAPATAPSQGGVNSPVNVTTTVDANTSLAKIENAIRMISDQRANLGAFQNRLESIKDSTEYAIENLKASYAQIKDATMTDEVVAATTNSILTQSAMAMIAQANQVPQYVLSLLR |
| 预测分子量 | 51.8 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3篇关于FLA(Flagellin)重组蛋白的参考文献示例，涵盖其应用与机制研究：
1. **文献名称**: *"Flagellin-F1-V vaccine synergistically enhances protection against pneumonic plague by activation of mucosal immunity"*
**作者**: A. Fernández-Santos 等
**摘要**: 研究利用重组FLA蛋白作为佐剂，与鼠疫疫苗抗原F1-V融合，显著增强呼吸道黏膜免疫应答，提升对肺鼠疫的保护效果。
2. **文献名称**: *"Recombinant flagellin A proteins containing CD4+ T cell epitopes as vaccine candidates for *Mycobacterium tuberculosis*"*
**作者**: J. Huleatt 等
**摘要**: 构建携带结核杆菌T细胞表位的重组FLA蛋白，证明其可激活TLR5通路并诱导强效Th1型免疫应答，为结核疫苗开发提供新策略。
3. **文献名称**: *"Engineered flagellin as a broad-spectrum influenza vaccine candidate"*
**作者**: Y. Wang 等
**摘要**: 通过结构优化将流感病毒保守抗原M2e与FLA重组，显著提升交叉保护性抗体水平，验证其在广谱流感疫苗中的潜力。
注：以上为示例性内容，实际文献需通过数据库(如PubMed)检索确认。
**Background of Fla Recombinant Protein**
Fla (flagellin) recombinant protein is derived from bacterial flagella, a key structural component enabling bacterial motility. Flagellin, the primary subunit of flagellar filaments, is a highly conserved protein across species, notably in pathogens like *Salmonella* and *E. coli*. Its inherent immunogenicity stems from recognition by the innate immune system via Toll-like receptor 5 (TLR5), which triggers pro-inflammatory signaling pathways (e.g., NF-κB activation). This property has driven interest in leveraging recombinant Fla as a vaccine adjuvant or therapeutic agent.
Recombinant Fla is produced using genetic engineering techniques, where the *fla* gene is cloned into expression vectors (e.g., *E. coli* or yeast systems) to enable large-scale, purified protein production. Advances in codon optimization and purification methods (e.g., affinity chromatography) have enhanced yield and stability. Unlike native flagellin, recombinant variants can be engineered to exclude hypervariable regions, reducing potential cross-reactivity while retaining TLR5 agonist activity.
Applications of Fla recombinant protein span immunology and biotechnology. In vaccinology, it serves as a potent adjuvant, enhancing antigen-specific antibody and T-cell responses by stimulating mucosal and systemic immunity. It is also explored in cancer immunotherapy, where Fla-TLR5 signaling promotes dendritic cell maturation and antitumor immunity. Additionally, Fla serves as a model protein for studying innate immune mechanisms or as a fusion partner to deliver heterologous antigens.
Challenges include mitigating potential endotoxin contamination during production and addressing TLR5 polymorphism-related variability in human responses. Despite this, Fla recombinant protein remains a versatile tool in biomedical research and therapeutic development due to its unique balance of immunogenicity, safety, and adaptability.
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