| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | btuF |
| Uniprot No | P37028 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-266aa |
| 氨基酸序列 | PRVITLSPANTELAFAAGITPVGVSSYSDYPPQAQKIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQLASLGIKVMWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFGINPPFTSGKESIQNQVLEVCGGENIFKDSRVPWPQVSREQVLARSPQAIVITGGPDQIPKIKQYWGEQLKIPVIPLTSDWFERASPRIILAAQQLCNALSQVD |
| 预测分子量 | 53.9 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btuF重组蛋白的3篇模拟参考文献(内容基于领域知识模拟，非真实文献)：
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1. **文献名称**: *Crystal structure of the vitamin B12 transporter BtuF from Escherichia coli*
**作者**: Locher, K.P. et al.
**摘要**: 本研究解析了大肠杆菌BtuF蛋白的晶体结构，揭示其通过构象变化结合维生素B12的机制，并阐明了其与ABC转运蛋白BtuCD的相互作用界面。
2. **文献名称**: *Functional characterization of recombinant BtuF in vitamin B12 uptake*
**作者**: Borths, E.L. et al.
**摘要**: 通过重组表达纯化BtuF蛋白，结合体外实验证明其对维生素B12的高亲和力结合能力，并利用荧光淬灭技术分析其底物结合的动力学参数。
3. **文献名称**: *Engineering BtuF for enhanced stability and ligand binding*
**作者**: Karpowieski, D. & Smith, J.
**摘要**: 通过定点突变优化重组BtuF蛋白的热稳定性及底物结合效率，为开发基于BtuF的维生素B12检测探针提供理论依据。
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**注**：以上文献为示例性内容，实际研究中请通过PubMed或Web of Science检索真实文献。建议使用关键词“BtuF recombinant protein”“vitamin B12 transporter”进行查询。
BtuF is a periplasmic binding protein critical for vitamin B12 (cobalamin) uptake in *Escherichia coli* and related Gram-negative bacteria. It functions as part of the BtuCD-F system, an ATP-binding cassette (ABC) transporter that imports vitamin B12 across the bacterial inner membrane. BtuF specifically recognizes and binds vitamin B12 with high affinity in the periplasm, delivering it to the transmembrane BtuCD transporter complex. This process is energy-dependent, coupling ATP hydrolysis by BtuD subunits with conformational changes in BtuF to facilitate B12 translocation into the cytoplasm.
Structurally, BtuF adopts a bilobed "Venus flytrap" architecture common to substrate-binding proteins. Its two globular domains enclose the B12 molecule through hinge-bending motions. Studies using X-ray crystallography and biophysical assays have revealed key residues involved in B12 coordination and conformational dynamics. Recombinant BtuF protein, typically expressed in *E. coli* and purified via affinity chromatography, serves as a model system for investigating substrate recognition, transport mechanisms, and protein-ligand interactions in ABC transporters.
Research on BtuF has broader implications for understanding microbial nutrient acquisition, antibiotic resistance (due to structural similarities with efflux pumps), and biotechnological applications. Engineered BtuF variants are explored for biosensing, targeted drug delivery, or synthetic biology tools. Additionally, studying BtuF-B12 interactions informs strategies to disrupt bacterial metabolism, potentially aiding antimicrobial development. Its well-characterized structure-function relationship makes BtuF a valuable prototype for deciphering fundamental principles of membrane transport systems.
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