纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | yjbL |
Uniprot No | P32693 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-84aa |
氨基酸序列 | MLKIIPGATGYFNKTLNSNQFDNEDAIKDKLDNRGSIKGKLNNIYGKSIDYAALRHRDIIIAKIDLFIQRITHNLWHARKKMCF |
预测分子量 | 25.1 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yjbL重组蛋白的3篇虚构参考文献示例(注:内容基于领域常见研究方向模拟,非真实文献):
1. **文献名称**:Functional Characterization of the yjbL Gene in Escherichia coli Stress Response
**作者**:Majdalani, N.; Gottesman, S.
**摘要**:本研究探讨了yjbL基因在大肠杆菌中的功能,发现其编码的蛋白参与氧化应激反应。通过重组蛋白表达和表型分析,证实yjbL缺失导致细胞对过氧化氢敏感性增加,提示其在抗氧化防御中的作用。
2. **文献名称**:Purification and Structural Analysis of Recombinant YjbL Protein
**作者**:Wang, L.; Zhang, Y.
**摘要**:报道了yjbL重组蛋白的高效表达与纯化方法,采用X射线晶体学解析其三维结构,揭示了其具有典型的硫氧还蛋白折叠结构,为后续功能机制研究提供结构基础。
3. **文献名称**:YjbL Interacts with RcsB to Regulate Biofilm Formation in Salmonella
**作者**:Garcia, C.; Detweiler, C.S.
**摘要**:通过重组YjbL蛋白的体外结合实验,证明其与RcsB调控蛋白相互作用,共同调控沙门氏菌生物膜形成。基因敲除实验显示yjbL缺失显著降低细菌黏附能力。
(注:以上文献及内容均为示例性模拟,实际研究需以真实数据库检索结果为准。)
**Background of YjbL Recombinant Protein**
YjbL is a conserved bacterial protein encoded by the *yjbL* gene, prominently studied in *Escherichia coli* (*E. coli*). It belongs to the DUF1528 protein family, characterized by a conserved domain of unknown function. YjbL is implicated in bacterial stress response pathways, particularly under oxidative stress or during biofilm formation. Studies suggest it interacts with the stationary-phase sigma factor σS (RpoS), a global regulator of stress adaptation, though its exact mechanistic role remains under investigation.
Recombinant YjbL protein is produced via genetic engineering, typically by cloning the *yjbL* gene into expression vectors (e.g., pET or pGEX systems) and overexpressing it in host cells like *E. coli*. Purification methods often employ affinity tags (e.g., His-tag) for efficient isolation. The recombinant form enables structural and functional analyses, including crystallography, enzymatic assays, or interaction studies with nucleic acids or partner proteins.
YjbL's potential involvement in biofilm regulation and stress survival makes it a target for antimicrobial research, as disrupting these pathways could weaken bacterial resilience. Additionally, its conserved nature across Gram-negative bacteria highlights its evolutionary significance. Despite progress, gaps persist in understanding its precise biochemical role, driving ongoing research to elucidate its contributions to bacterial physiology and pathogenicity.
In summary, YjbL recombinant protein serves as a critical tool for dissecting bacterial stress adaptation mechanisms and exploring novel therapeutic strategies against biofilm-associated infections.
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