| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | rbtD |
| Uniprot No | P00335 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-249aa |
| 氨基酸序列 | MKHSVSSMNTSLSGKVAAITGAASGIGLECARTLLGAGAKVVLIDREGEKLNKLVAELGENAFALQVDLMQADQVDNLLQGILQLTGRLDIFHANAGAYIGGPVAEGDPDVWDRVLHLNINAAFRCVRSVLPHLIAQKSGDIIFTAVIAGVVPVIWEPVYTASKFAVQAFVHTTRRQVAQYGVRVGAVLPGPVVTALLDDWPKAKMDEALANGSLMQPIEVAESVLFMVTRSKNVTVRDIVILPNSVDL |
| 预测分子量 | 30.5 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rbtD重组蛋白的3篇示例参考文献(内容为虚构，供参考)：
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1. **文献名称**: *Cloning and Expression of the rbtD Gene in Escherichia coli for Recombinant Protein Production*
**作者**: Zhang L, et al.
**摘要**: 本研究成功克隆了来自百日咳杆菌的rbtD基因，并在大肠杆菌BL21中实现高效可溶性表达。通过优化诱导条件(如IPTG浓度、温度)，获得高纯度重组rbtD蛋白，并验证其与天然蛋白的抗原相似性，为后续疫苗开发奠定基础。
2. **文献名称**: *Structural and Functional Analysis of rbtD Recombinant Protein in Bordetella pertussis Pathogenesis*
**作者**: Martinez R, et al.
**摘要**: 通过X射线晶体学解析rbtD重组蛋白的三维结构，揭示其与宿主细胞表面受体结合的活性区域。体外实验表明，敲除rbtD的百日咳杆菌毒力显著降低，提示该蛋白在细菌黏附和免疫逃逸中起关键作用。
3. **文献名称**: *Immunogenicity Evaluation of rbtD-Based Subunit Vaccine Against Pertussis*
**作者**: Wang Y, et al.
**摘要**: 在小鼠模型中评估重组rbtD蛋白的免疫原性。结果显示，该蛋白能诱导高水平IgG抗体和Th1/Th17细胞免疫应答，攻毒实验证实其对百日咳杆菌感染的保护率达85%，提示其作为新型无细胞疫苗组分的潜力。
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注：以上文献为示例性质，实际研究中请通过PubMed或Google Scholar以关键词“rbtD recombinant protein”“Bordetella rbtD”等检索真实文献。
**Background of rbtD Recombinant Protein**
The rbtD recombinant protein is a genetically engineered protein derived from the *rbtD* gene, originally identified in certain bacterial species. This gene is part of metabolic or regulatory pathways, often associated with stress response, virulence, or niche adaptation. For instance, in *Escherichia coli* and related enterobacteria, *rbtD* is linked to the ribitol metabolism operon, playing a role in carbohydrate utilization under specific environmental conditions.
Recombinant rbtD is produced via heterologous expression systems, such as *E. coli* or yeast, enabling large-scale purification for functional studies. Its production typically involves cloning the *rbtD* gene into expression vectors, followed by induction, lysis, and chromatography-based purification. This approach ensures high yield and purity, critical for structural and biochemical analyses.
Research on rbtD focuses on elucidating its biological role, particularly in microbial metabolism or host-pathogen interactions. Structural studies (e.g., X-ray crystallography) aim to resolve its 3D conformation, shedding light on substrate binding or enzymatic mechanisms. Additionally, rbtD has potential biotechnological applications, including industrial enzyme engineering or vaccine development, given its possible immunogenicity in pathogenic strains.
Despite progress, knowledge gaps remain regarding its precise physiological functions or regulatory networks. Ongoing studies leverage recombinant rbtD to explore its interactions with other cellular components, aiding the development of antimicrobial strategies or metabolic engineering tools. Overall, rbtD exemplifies how recombinant proteins bridge basic microbiology and applied biotechnology.
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