| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | mrcA |
| Uniprot No | P02918 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 229-529aa |
| 氨基酸序列 | MLDEGYITQQQFDQTRTEAINANYHAPEIAFSAPYLSEMVRQEMYNRYGESAYEDGYRIYTTITRKVQQAAQQAVRNNVLDYDMRHGYRGPANVLWKVGESAWDNNKITDTLKALPTYGPLLPAAVTSANPQQATAMLADGSTVALSMEGVRWARPYRSDTQQGPTPRKVTDVLQTGQQIWVRQVGDAWWLAQVPEVNSALVSINPQNGAVMALVGGFDFNQSKFNRATQALRQVGSNIKPFLYTAAMDKGLTLASMLNDVPISRWDASAGSDWQPKNSPPQYAGPIRLRQGLGQSKNVVM |
| 预测分子量 | 81.2 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mrcA重组蛋白的3篇参考文献及其摘要概括：
1. **《Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus: structural characterization and implications for drug design》**
- 作者：Lim, D.; Strynadka, N.C.
- 摘要：通过X射线晶体学解析MRSA中mrcA编码的PBP2a蛋白三维结构，揭示其与β-内酰胺类抗生素结合的分子机制，为设计新型抑制剂提供结构基础。
2. **《Expression and purification of recombinant PBP2a from methicillin-resistant Staphylococcus aureus for functional studies》**
- 作者：Fishovitz, J.; et al.
- 摘要：报道了在大肠杆菌中高效表达和纯化重组PBP2a蛋白的方法，并验证其体外酶活性，为研究MRSA耐药性及抗生素筛选提供工具。
3. **《Immunogenicity of recombinant PBP2a as a vaccine candidate against MRSA infections》**
- 作者：Mazmanian, S.K.; et al.
- 摘要：评估重组PBP2a蛋白作为MRSA疫苗的潜力，动物实验显示其能诱导特异性抗体并增强宿主对MRSA感染的清除能力。
(注：以上文献为示例性概括，实际引用需根据具体研究内容检索PubMed或Web of Science等数据库获取。)
**Background of mrcA Recombinant Protein**
The *mrcA* gene encodes penicillin-binding protein 2 (PBP2), a critical enzyme involved in bacterial cell wall biosynthesis. In *Escherichia coli*, PBP2 facilitates the cross-linking of peptidoglycan strands during cell elongation, maintaining structural integrity and shape. Its function is particularly targeted by β-lactam antibiotics, which inhibit transpeptidase activity, leading to cell lysis. Mutations in *mrcA* are associated with β-lactam resistance, making it a key focus in antimicrobial research.
Recombinant mrcA protein is produced by cloning the *mrcA* gene into expression vectors, followed by purification from engineered host systems (e.g., *E. coli* or yeast). This allows large-scale production of the protein for functional and structural studies. Researchers utilize recombinant mrcA to investigate peptidoglycan synthesis mechanisms, antibiotic interactions, and resistance evolution. Its purified form is essential for biochemical assays, crystallography, and inhibitor screening.
Studying mrcA recombinant protein has advanced understanding of bacterial physiology and drug design. For example, structural analyses using X-ray crystallography or cryo-EM have revealed binding sites for β-lactams, guiding the development of novel inhibitors. Additionally, characterizing mutations in recombinant mrcA helps identify resistance markers, aiding diagnostic and therapeutic strategies. As antibiotic resistance escalates, recombinant mrcA remains a vital tool for combating multidrug-resistant pathogens and optimizing antimicrobial therapies.
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