| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Bb |
| Uniprot No | P49770 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-351aa |
| 氨基酸序列 | MPGSAAKGSELSERIESFVETLKRGGGPRSSEEMARETLGLLRQIITDHRWSNAGELMELIRREGRRMTAAQPSETTVGNMVRRVLKIIREEYGRLHGRSDESDQQESLHKLLTSGGLNEDFSFHYAQLQSNIIEAINELLVELEGTMENIAAQALEHIHSNEVIMTIGFSRTVEAFLKEAARKRKFHVIVAECAPFCQGHEMAVNLSKAGIETTVMTDAAIFAVMSRVNKVIIGTKTILANGALRAVTGTHTLALAAKHHSTPLIVCAPMFKLSPQFPNEEDSFHKFVAPEEVLPFTEGDILEKVSVHCPVFDYVPPELITLFISNIGGNAPSYIYRLMSELYHPDDHVL |
| 预测分子量 | 66.0 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条与伯氏疏螺旋体(Borrelia burgdorferi, Bb)重组蛋白相关的研究文献摘要示例：
1. **文献名称**: *Recombinant OspA protects mice against infection with Borrelia burgdorferi*
**作者**: Fikrig, E. et al.
**摘要**: 该研究通过表达Bb表面蛋白OspA的重组蛋白，证明其在小鼠模型中可诱导保护性免疫反应，显著降低伯氏疏螺旋体感染后的组织损伤，为莱姆病疫苗开发提供依据。
2. **文献名称**: *Expression of Borrelia burgdorferi OspC and DbpA antigens in Escherichia coli for immunoblot analysis*
**作者**: Gilmore, R.D. et al.
**摘要**: 研究利用大肠杆菌系统高效表达Bb的OspC和DbpA重组蛋白，验证其在莱姆病血清学诊断中的特异性，为改进免疫印迹法(Western blot)提供标准化抗原。
3. **文献名称**: *Fibronectin-binding protein of Borrelia burgdorferi: a potential virulence factor*
**作者**: Probert, W.S. & LeFebvre, R.B.
**摘要**: 通过重组表达Bb的BBK32蛋白，揭示其与宿主纤维连接蛋白的结合能力，分析该互作在细菌黏附和致病机制中的作用，为理解Bb感染提供分子机制支持。
(注：以上文献信息为示例，实际引用需核对原文及发表年份。)
**Background of Bb Recombinant Proteins**
Recombinant proteins derived from *Borrelia burgdorferi* (Bb), the spirochete bacterium responsible for Lyme disease, have become critical tools in understanding and managing this globally prevalent tick-borne illness. Bb transmits to humans through *Ixodes* ticks, causing multisystemic symptoms ranging from erythema migrans rashes to severe neurological and articular complications if untreated. Traditional diagnostic methods, such as serological assays, often rely on whole-cell lysates, which may yield cross-reactivity due to shared epitopes with other pathogens. To improve specificity, recombinant proteins mimicking key Bb antigens (e.g., OspA, OspC, VlsE, BmpA, DbpA) are engineered using molecular cloning techniques. These proteins are expressed in heterologous systems like *E. coli* or yeast, ensuring high purity and scalability.
The development of Bb recombinant proteins has revolutionized Lyme disease diagnostics. For instance, the C6 peptide, a synthetic analog of the VlsE antigen, forms the basis of sensitive ELISA kits, enhancing early detection accuracy. Similarly, recombinant OspA has been central to vaccine research. The discontinued LYMErix vaccine (1998–2002) utilized OspA to induce antibodies blocking bacterial transmission in ticks, though safety concerns and low demand led to its withdrawal. Recent efforts focus on next-generation OspA-based vaccines targeting diverse Bb strains.
Beyond diagnostics and vaccines, recombinant Bb proteins facilitate pathogenesis studies. Proteins like decorin-binding protein A (DbpA) or fibronectin-binding BBK32 help unravel mechanisms of bacterial adhesion, immune evasion, and tissue colonization. However, challenges persist, including genetic variability among Bb strains and the need for conserved antigen targets. Ongoing research aims to refine recombinant protein design, incorporating structural biology insights or multi-epitope chimeras to address these limitations. Overall, Bb recombinant proteins remain indispensable in advancing Lyme disease research, therapeutics, and public health strategies.
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