| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | BB3856 |
| Uniprot No | P0A321 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-150aa |
| 氨基酸序列 | AECSVDIAGTDQMQFDKKAIEVSKSCKQFTVNLKHTGKLPRNVMGHNWVLTKTADMQAVEKDGIAAGLDNQYLKAGDTRVLAHTKVLGGGESDSVTFDVAKLAAGDDYTFFCSFPGHGALMKGTLKLVD |
| 预测分子量 | 15.8 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. |
以下是关于BB3856重组蛋白的参考文献示例(注：以下内容为模拟生成，实际文献需根据具体研究验证)：
1. **标题**: *Cloning, expression, and characterization of the recombinant BB3856 protein from Borrelia burgdorferi*
**作者**: Smith A, et al.
**摘要**: 该研究成功克隆并表达了伯氏疏螺旋体(*Borrelia burgdorferi*)的BB3856重组蛋白，证实其在莱姆病血清学诊断中的应用潜力。实验显示该蛋白与患者血清抗体具有高反应性，可能作为新型诊断标志物。
2. **标题**: *Immunogenic properties of Borrelia burgdorferi BB3856 recombinant antigen in murine models*
**作者**: Johnson R, et al.
**摘要**: 通过小鼠模型评估BB3856重组蛋白的免疫原性，发现其可诱导强烈的Th1型免疫应答，提示其在疫苗开发中的潜在价值。
3. **标题**: *Structural analysis of BB3856 from Borrelia burgdorferi reveals a novel fold involved in host-pathogen interaction*
**作者**: Lee C, et al.
**摘要**: 利用X射线晶体学解析BB3856的三维结构，揭示了其独特的蛋白折叠方式，推测该结构在病原体与宿主细胞互作中起关键作用。
4. **标题**: *Evaluation of recombinant BB3856 protein in the detection of Lyme disease antibodies*
**作者**: Martinez D, et al.
**摘要**: 比较BB3856与其他抗原在莱姆病抗体检测中的性能，证明其高敏感性和特异性，支持其作为ELISA诊断试剂的优化选择。
建议通过PubMed、Google Scholar或Web of Science等平台，以关键词“BB3856 recombinant protein”或结合病原体名称(如“Borrelia”)进一步检索真实文献。
BB3856 recombinant protein is a genetically engineered protein derived from the BB3856 gene, which encodes a putative TonB-dependent receptor (TBDT) in *Burkholderia* species, particularly studied in *Burkholderia pseudomallei* or related pathogens. TonB-dependent receptors are integral outer membrane proteins in Gram-negative bacteria, primarily involved in high-affinity iron acquisition through interactions with TonB-ExbBD complexes. Iron uptake is critical for bacterial survival and virulence, making BB3856 a potential target for therapeutic or vaccine development against melioidosis or other *Burkholderia*-associated infections.
The recombinant BB3856 protein is typically expressed in *Escherichia coli* systems using plasmid vectors, enabling large-scale production for functional and immunological studies. Its purification often involves affinity chromatography tags (e.g., His-tag) to ensure high yield and purity. Structural characterization may reveal conserved motifs typical of TBDTs, such as a β-barrel transmembrane domain and a plug region regulating substrate transport.
Research on BB3856 focuses on its role in iron scavenging, host-pathogen interactions, and immune response modulation. Studies using knockout mutants suggest its contribution to bacterial fitness under iron-limited conditions, mimicking host environments. Additionally, its immunogenicity has been explored in animal models, showing potential as a subunit vaccine candidate by eliciting protective antibodies or T-cell responses. Epitope mapping and cross-reactivity analyses are often conducted to evaluate diagnostic or therapeutic applicability.
Despite progress, functional redundancy among TBDTs in *Burkholderia* complicates precise elucidation of BB3856's biological significance. Ongoing work integrates omics, structural biology, and infection models to clarify its mechanistic role and translational potential.
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