纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | bla |
Uniprot No | P09326 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 27-220aa |
氨基酸序列 | QGHLVHMTVVSGSNVTLNISESLPENYKQLTWFYTFDQKIVEWDSRKSKYFESKFKGRVRLDPQSGALYISKVQKEDNSTYIMRVLKKTGNEQEWKIKLQVLDPVPKPVIKIEKIEDMDDNCYLKLSCVIPGESVNYTWYGDKRPFPKELQNSVLETTLMPHNYSRCYTCQVSNSVSSKNGTVCLSPPCTLARS |
预测分子量 | 51.3 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BLA(β-内酰胺酶)重组蛋白研究的3篇代表性文献示例(注:文献信息为示例性概括,非真实文献):
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1. **文献名称**: "Optimization of Recombinant Beta-Lactamase Expression in Escherichia coli for Industrial Applications"
**作者**: Smith A, et al. (2018)
**摘要**: 研究通过优化大肠杆菌表达系统(诱导温度、IPTG浓度等),显著提高了重组BLA蛋白的产量和活性,为规模化生产提供可行方案。
2. **文献名称**: "A Novel Beta-Lactamase-Based Biosensor for Rapid Detection of Penicillin Residues"
**作者**: Chen L, et al. (2020)
**摘要**: 利用重组BLA蛋白与荧光底物结合,开发了一种高灵敏度生物传感器,可快速检测牛奶中青霉素类抗生素残留,检测限达0.1 ppb。
3. **文献名称**: "Structural Insights into the Substrate Specificity of Engineered Bla Proteins via Directed Evolution"
**作者**: Johnson R, et al. (2021)
**摘要**: 通过定向进化技术改造BLA重组蛋白,解析其晶体结构,揭示了关键氨基酸突变对第三代头孢菌素水解活性的增强机制。
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**说明**:以上文献为模拟示例,实际研究中建议通过PubMed或Web of Science以关键词"recombinant beta-lactamase"、"bla protein expression"等检索最新论文。
**Background of Recombinant Bla Proteins**
Recombinant Bla (β-lactamase) proteins are engineered variants of naturally occurring β-lactamases, enzymes produced by bacteria to hydrolyze β-lactam antibiotics like penicillins and cephalosporins, conferring antibiotic resistance. The study of Bla proteins gained prominence with the rise of antibiotic resistance in clinical settings, driving research into their structure, function, and mechanisms. Recombinant DNA technology enabled the production of these proteins in heterologous systems (e.g., *E. coli*, yeast), facilitating large-scale purification and detailed biochemical characterization.
The bla gene, encoding β-lactamase, was among the earliest targets for genetic manipulation due to its role in resistance and utility as a selectable marker in cloning vectors. Recombinant Bla proteins have been optimized for industrial and research applications, including antibiotic degradation studies, enzyme kinetics, and as reporter proteins in biosensors. Engineered Bla variants with altered substrate specificity or enhanced stability also serve as models for protein engineering and directed evolution.
In biotechnology, Bla is widely used as a marker in plasmid selection (via ampicillin resistance). Additionally, fusion tags derived from Bla improve protein solubility and purification. Recent advancements focus on designing "silent" Bla mutants for safer molecular tools and developing Bla inhibitors to combat resistance. The versatility, ease of production, and functional relevance of recombinant Bla proteins make them indispensable in both basic research and applied microbiology, bridging gaps between antibiotic resistance mechanisms and biotechnological innovation.
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