| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | NDM1 |
| Uniprot No | A0A6C0L5R1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-85aa |
| 氨基酸序列 | MTLTNILVNAGVKVRLTDAYKIHHDKVIIIDRSTVETGSFNFTKAAEYSNSENALVLNDMPQVASVYLEHWQSRWETGRDWKSTY |
| 预测分子量 | 9,7 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NDM1重组蛋白的3篇参考文献，涵盖其表达、结构及功能研究：
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1. **文献名称**：*Biochemical characterization of the New Delhi metallo-β-lactamase-1*
**作者**：Yong, D., Toleman, M.A., Giske, C.G., Cho, H.S., Lee, K., & Walsh, T.R.
**摘要**：该研究在大肠杆菌中重组表达了NDM-1蛋白，证实其能水解碳青霉烯类抗生素(如亚胺培南)和头孢菌素，并发现其活性依赖锌离子。研究为NDM-1介导的耐药性提供了生化证据。
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2. **文献名称**：*Crystal Structure of NDM-1 Reveals a Common β-Lactam Hydrolysis Mechanism*
**作者**：King, D.T., Worrall, L.J., Gruninger, R., Strynadka, N.C.J.
**摘要**：通过重组表达纯化NDM-1蛋白，利用X射线晶体学解析其三维结构，揭示了其水解β-内酰胺类抗生素的催化机制，为抑制剂设计奠定结构基础。
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3. **文献名称**：*Structural Insights into the Mechanism of New Delhi Metallo-β-lactamase-1*
**作者**：Zhang, H., Hao, Q., Gao, J., Wang, Q.
**摘要**：本研究通过重组NDM-1蛋白的动力学分析和突变实验，阐明了其底物结合口袋的关键氨基酸残基，解释了其对多种β-内酰胺抗生素的广谱水解能力。
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**备注**：上述文献示例基于真实研究主题，但具体标题和作者可能存在差异。建议通过PubMed或Google Scholar以关键词“NDM-1 recombinant protein”“crystal structure”“metallo-β-lactamase”检索获取准确信息。
**Background of NDM-1 Recombinant Protein**
NDM-1 (New Delhi metallo-β-lactamase-1) is a bacterial enzyme that confers resistance to a broad range of β-lactam antibiotics, including carbapenems, which are often considered last-resort treatments for multidrug-resistant infections. First identified in *Klebsiella pneumoniae* isolated from a Swedish patient in India in 2008. NDM-1 quickly gained global attention due to its plasmid-mediated horizontal gene transfer, facilitating rapid spread among bacterial species. The enzyme belongs to the metallo-β-lactamase (MBL) family, characterized by its reliance on zinc ions for hydrolytic activity against β-lactams.
Recombinant NDM-1 protein is produced via genetic engineering for research purposes, enabling scientists to study its structure, mechanism, and interaction with antibiotics or inhibitors. Its crystal structure, resolved through X-ray crystallography, reveals a distinctive active-site architecture with two zinc ions critical for substrate binding and catalysis. These structural insights aid in designing inhibitors to counteract resistance.
The emergence of NDM-1 poses significant clinical challenges, as infections caused by NDM-1-producing pathogens are linked to high mortality due to limited therapeutic options. Research on recombinant NDM-1 focuses on understanding its enzymatic kinetics, substrate specificity, and resistance evolution. Additionally, it supports screening potential inhibitors and evaluating novel therapies, such as combination drugs or metallo-β-lactamase inhibitors.
Despite advances, no clinically approved inhibitors specifically targeting NDM-1 exist, underscoring the urgency of this research. Studies using recombinant NDM-1 also explore its role in bacterial pathogenesis and co-resistance mechanisms with other antibiotic-resistance genes. Overall, NDM-1 recombinant protein serves as a vital tool in combating the global spread of carbapenem resistance and guiding the development of next-generation antimicrobial strategies.
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