| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | yfbU |
| Uniprot No | P0A8W9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-164aa |
| 氨基酸序列 | MEMTNAQRLILSNQYKMMTMLDPANAERYRRLQTIIERGYGLQMRELDREFGELKEETCRTIIDIMEMYHALHVSWSNLQDQQSIDERRVTFLGFDAATEARYLGYVRFMVNVEGRYTHFDAGTHGFNAQTPMWEKYQRMLNVWHACPRQYHLSANEINQIINA |
| 预测分子量 | 67.3 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yfbU重组蛋白的模拟参考文献(基于常见研究方向推测，非真实文献)：
1. **《Structural characterization of the YfbU protein from Escherichia coli》**
*作者：Smith J, et al. (2020)*
摘要：本研究通过X射线晶体学解析了大肠杆菌YfbU重组蛋白的三维结构，发现其具有典型的β-螺旋结构域，推测其可能参与细菌外膜蛋白的组装或稳定性维持。
2. **《Functional analysis of YfbU in bacterial biofilm formation》**
*作者：Zhang L, et al. (2018)*
摘要：通过构建yfbU基因敲除菌株，发现YfbU缺失显著抑制生物膜形成。重组YfbU蛋白体外实验表明其与多糖合成酶相互作用，提示其在胞外多糖分泌中的调控作用。
3. **《Cloning and high-level expression of recombinant YfbU in Pichia pastoris》**
*作者：Kim S, et al. (2019)*
摘要：成功在毕赤酵母系统中高效分泌表达YfbU重组蛋白，优化后产量达120 mg/L。纯化蛋白可用于抗体开发及下游致病机制研究。
4. **《YfbU as a potential vaccine candidate against pathogenic E. coli strains》**
*作者：Wang H, et al. (2021)*
摘要：评估重组YfbU蛋白在小鼠模型中的免疫保护效果，显示其诱导高水平IgG抗体并降低致病性大肠杆菌的肠道定植能力，提示其疫苗开发潜力。
注：以上内容为基于重组蛋白常见研究方向的模拟数据，实际文献需通过学术数据库检索确认。
**Background of YfbU Recombinant Protein**
YfbU is a bacterial protein originally identified in *Escherichia coli* and other Enterobacteriaceae. It belongs to the DUF1621 (Domain of Unknown Function 1621) family, characterized by conserved structural features but poorly understood biological roles. Genomic studies suggest its association with bacterial stress response, biofilm formation, or virulence, though its exact mechanism remains unclear.
The protein’s recombinant form is engineered for experimental studies, enabling scalable production via heterologous expression systems (e.g., *E. coli* expression vectors). Recombinant YfbU is often purified using affinity tags (e.g., His-tag) for structural and functional analyses. Research focuses on elucidating its interaction with host cells, potential enzymatic activities, or involvement in bacterial adaptation to environmental stressors.
Interest in YfbU stems from its possible role in bacterial pathogenesis. For instance, homologs in pathogens like *Salmonella* or *Klebsiella* may contribute to host immune evasion or antibiotic resistance. Structural studies using recombinant YfbU aim to resolve its 3D conformation, aiding in hypotheses about ligand binding or protein-protein interactions. Additionally, it is explored as a potential vaccine candidate or antimicrobial target due to its conservation across pathogenic strains.
Despite progress, YfbU’s precise biological function requires further validation. Current work integrates genetic knockout models, biochemical assays, and omics approaches to decode its contributions to bacterial physiology and infection pathways. Recombinant YfbU remains a valuable tool for bridging gaps in understanding bacterial adaptive mechanisms and developing novel biotechnological or therapeutic strategies.
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