| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ophA1 |
| Uniprot No | P33164 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-322aa |
| 氨基酸序列 | MTTPQEDGFLRLKIASKEKIARDIWSFELTDPQGAPLPPFEAGANLTVAVPNGSRRTYSLCNDSQERNRYVIAVKRDSNGRGGSISFIDDTSEGDAVEVSLPRNEFPLDKRAKSFILVAGGIGITPMLSMARQLRAEGLRSFRLYYLTRDPEGTAFFDELTSDEWRSDVKIHHDHGDPTKAFDFWSVFEKSKPAQHVYCCGPQALMDTVRDMTGHWPSGTVHFESFGATNTNARENTPFTVRLSRSGTSFEIPANRSILEVLRDANVRVPSSCESGTCGSCKTALCSGEADHRDMVLRDDEKGTQIMVCVSRAKSAELVL |
| 预测分子量 | 35,6 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ophA1重组蛋白的3篇代表性文献的示例(注：内容为示例性概括，实际文献需通过学术数据库查询)：
1. **文献名称**：Cloning and Expression of the ophA1 Gene Encoding a Novel β-Lactamase in *Acinetobacter baumannii*
**作者**：Y. Doi, et al.
**摘要**：本研究成功克隆了来自鲍曼不动杆菌的ophA1基因，并在大肠杆菌中实现重组表达。纯化的OphA1蛋白表现出对广谱β-内酰胺类抗生素(如氨苄西林)的水解活性，证实其作为Ambler分类中B类金属β-内酰胺酶的功能。
2. **文献名称**：Biochemical Characterization of Recombinant OphA1: A Carbapenem-Hydrolyzing Enzyme
**作者**：K. Poole, et al.
**摘要**：通过体外酶动力学分析，发现重组OphA1可有效水解碳青霉烯类抗生素(如亚胺培南)，并受金属离子螯合剂抑制。研究揭示了其耐药机制，为开发新型抑制剂提供依据。
3. **文献名称**：Structural Insights into OphA1-mediated Antibiotic Resistance by X-ray Crystallography
**作者**：H. T. Nguyen, et al.
**摘要**：通过X射线晶体学解析了OphA1重组蛋白的三维结构，发现其活性中心含锌离子结合位点。突变实验证明关键氨基酸残基(如His102)对酶活性和耐药表型至关重要。
建议通过PubMed或Google Scholar检索关键词“ophA1 recombinant protein”或“ophA1 beta-lactamase”获取具体文献。
The ophA1 gene encodes a metallo-β-lactamase enzyme, initially identified in pathogenic bacteria such as *Aeromonas* and *Pseudomonas* species. This enzyme hydrolyzes β-lactam antibiotics, including carbapenems, conferring resistance to these clinically important drugs. The emergence of antibiotic resistance mediated by metallo-β-lactamases like OphA1 has driven interest in understanding their structure, function, and mechanisms to combat multidrug-resistant infections.
Recombinant OphA1 protein is produced through heterologous expression systems, typically in *Escherichia coli*, enabling large-scale purification for biochemical and structural studies. Its production facilitates detailed analysis of substrate specificity, catalytic mechanisms, and interactions with inhibitors. Structurally, OphA1 belongs to the B3 subclass of metallo-β-lactamases, characterized by a conserved zinc-binding active site critical for hydrolyzing β-lactam rings. Studies using recombinant OphA1 have revealed insights into zinc ion coordination, substrate binding pockets, and conformational dynamics during catalysis.
Research on recombinant OphA1 also supports drug discovery efforts. By screening inhibitors or designing zinc-chelating compounds, scientists aim to restore the efficacy of β-lactam antibiotics. Additionally, recombinant OphA1 serves as a tool for detecting β-lactamase activity in clinical isolates, aiding surveillance of resistance genes. Its role in horizontal gene transfer studies highlights its contribution to the dissemination of resistance traits among bacterial populations.
Despite its clinical relevance, OphA1’s substrate profile differs from other metallo-β-lactamases, making it a unique model for studying enzyme evolution and diversity. Ongoing work focuses on deciphering its regulatory elements, kinetic properties, and potential as a target for novel antimicrobial strategies. Overall, recombinant OphA1 remains a critical resource for addressing the global challenge of antibiotic resistance.
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