| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OXA |
| Uniprot No | P39952 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-402aa |
| 氨基酸序列 | MFKLTSRLVTSRFAASSRLATARTIVLPRPHPSWISFQAKRFNSTGPNANDVSEIQTQLPSIDELTSSAPSLSASTSDLIANTTQTVGELSSHIGYLNSIGLAQTWYWPSDIIQHVLEAVHVYSGLPWWGTIAATTILIRCLMFPLYVKSSDTVARNSHIKPELDALNNKLMSTTDLQQGQLVAMQRKKLLSSHGIKNRWLAAPMLQIPIALGFFNALRHMANYPVDGFANQGVAWFTDLTQADPYLGLQVITAAVFISFTRLGGETGAQQFSSPMKRLFTILPIISIPATMNLSSAVVLYFAFNGAFSVLQTMILRNKWVRSKLKITEVAKPRTPIAGASPTENMGIFQSLKHNIQKARDQAERRQLMQDNEKKLQESFKEKRQNSKIKIVHKSNFINNKK |
| 预测分子量 | 44,8 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OXA重组蛋白的3篇代表性文献的简要列举(注：文献信息为示例性质，具体引用需核实原文)：
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1. **文献名称**: *"Functional Characterization of OXA-48 Carbapenemase by Recombinant Expression in Escherichia coli"*
**作者**: Poirel, L., et al.
**摘要**: 本研究通过在大肠杆菌中重组表达OXA-48蛋白，分析了其对β-内酰胺类抗生素(包括碳青霉烯类)的水解活性，揭示了OXA-48介导耐药性的分子机制。
2. **文献名称**: *"Crystal Structure of OXA-23 Reveals Insights into Carbapenem Hydrolysis"*
**作者**: Smith, C.A., Antunes, N.T., et al.
**摘要**: 通过重组表达并纯化OXA-23蛋白，解析其三维晶体结构，阐明了该酶与碳青霉烯类抗生素结合的关键活性位点，为抑制剂设计提供结构基础。
3. **文献名称**: *"Inhibitor Screening against Recombinant OXA-24/40 β-Lactamase"*
**作者**: Drawz, S.M., Bonomo, R.A.
**摘要**: 利用重组表达的OXA-24/40蛋白，筛选了多种β-内酰胺酶抑制剂，发现部分化合物可有效抑制其活性，为治疗多重耐药菌感染提供潜在策略。
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**注意**：上述文献信息为示例，实际引用时需通过PubMed或Web of Science等数据库核对准确性，并补充年份、期刊及卷期页码。建议使用关键词“OXA recombinant protein expression”或“OXA beta-lactamase characterization”进一步检索最新研究。
**Background of OXA Recombinant Proteins**
OXA (Oxacillinase) recombinant proteins are engineered versions of β-lactamase enzymes originally identified in Gram-negative bacteria. These enzymes belong to the class D β-lactamases, characterized by their ability to hydrolyze a broad spectrum of β-lactam antibiotics, including penicillins, cephalosporins, and carbapenems. The OXA family is particularly notable for contributing to carbapenem resistance in clinically significant pathogens like *Acinetobacter baumannii* and *Enterobacteriaceae*, posing a major challenge in treating hospital-acquired infections.
The term "recombinant" refers to the production of these proteins through genetic engineering techniques. Genes encoding OXA enzymes are cloned into expression vectors (e.g., *E. coli* or yeast systems) to produce purified proteins for research or industrial applications. Recombinant OXA proteins retain the functional properties of their native counterparts, enabling studies on enzyme kinetics, substrate specificity, and inhibitor interactions.
Research on OXA recombinant proteins focuses on understanding their catalytic mechanisms, structural features, and evolution. These studies aim to develop inhibitors or novel antibiotics to counteract resistance. Additionally, recombinant OXA enzymes are used in diagnostic tools to detect carbapenemase activity in bacterial isolates, aiding infection control.
The emergence of OXA variants (e.g., OXA-23. OXA-48) through horizontal gene transfer and mutations underscores their clinical relevance. Characterizing recombinant forms helps track resistance trends and design targeted therapies. Overall, OXA recombinant proteins serve as critical tools in combating antimicrobial resistance and advancing infectious disease research.
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