| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | gyrA |
| Uniprot No | P0AES4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-875aa |
| 氨基酸序列 | SDLAREITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLYAMNVLGNDWNKAYKKSARVVGDVIGKYHPHGDSAVYGTIVRMAQPFSLRYMLVDGQGNFGSIDGDSAAAMRYTEIRLAKIAHELMADLEKETVDFVDNYDGTEKIPDVMPTKIPNLLVNGSSGIAVGMATNIPPHNLTEVINGCLAYIDDEDISIEGLMEHIPGPDFPTAAIINGRRGIEEAYRTGRGKVYIRARAEVEVDAKTGRETIIVHEIPYQVNKARLIEKIAELVKEKRVEGISALRDESDKDGMRIVIEVKRDAVGEVVLNNLYSQTQLQVSFGINMVALHHGQPKIMNLKDIIAAFVRHRREVVTRRTIFELRKARDRAHILEALAVALANIDPIIELIRHAPTPAEAKTALVANPWQLGNVAAMLERAGDDAARPEWLEPEFGVRDGLYYLTEQQAQAILDLRLQKLTGLEHEKLLDEYKELLDQIAELLRILGSADRLMEVIREELELVREQFGDKRRTEITANSADINLEDLITQEDVVVTLSHQGYVKYQPLSEYEAQRRGGKGKSAARIKEEDFIDRLLVANTHDHILCFSSRGRVYSMKVYQLPEATRGARGRPIVNLLPLEQDERITAILPVTEFEEGVKVFMATANGTVKKTVLTEFNRLRTAGKVAIKLVDGDELIGVDLTSGEDEVMLFSAEGKVVRFKESSVRAMGCNTTGVRGIRLGEGDKVVSLIVPRGDGAILTATQNGYGKRTAVAEYPTKSRATKGVISIKVTERNGLVVGAVQVDDCDQIMMITDAGTLVRTRVSEISIVGRNTQGVILIRTAEDENVVGLQRVAEPVDEEDLDTIDGSAAEGDDEIAPEVDVDDEPEEE |
| 预测分子量 | 102.8 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gyrA重组蛋白的3条参考文献示例(注：文献信息为模拟示例，仅供参考)：
1. **文献名称**: "Functional Analysis of Recombinant gyrA Protein in Quinolone Resistance"
**作者**: Smith J, et al.
**摘要**: 本研究通过克隆和表达大肠杆菌gyrA基因的重组蛋白，分析了其DNA旋转酶活性及与喹诺酮类药物的相互作用。实验表明，gyrA的S83L突变显著降低药物与酶的结合能力，揭示了该突变导致抗生素耐药的分子机制。
2. **文献名称**: "Purification and Structural Characterization of gyrA Subunit from Mycobacterium tuberculosis"
**作者**: Lee H, et al.
**摘要**: 报道了结核分枝杆菌gyrA重组蛋白的高效表达和纯化方法，并通过X射线晶体学解析其三维结构。研究为针对该靶点的新型抗结核药物设计提供了结构基础。
3. **文献名称**: "Site-Directed Mutagenesis of gyrA Reveals Key Residues for DNA Supercoiling Activity"
**作者**: Zhang Y, et al.
**摘要**: 通过定点诱变技术构建多种gyrA突变体重组蛋白，结合酶活测定发现D87和G81残基对DNA超螺旋活性至关重要，为理解DNA旋转酶的功能机制提供实验依据。
如需具体文献，建议在PubMed或Web of Science中检索关键词：**gyrA recombinant protein + quinolone resistance/purification/mutation**。
The gyrA gene encodes the A subunit of DNA gyrase, a type II topoisomerase essential in prokaryotes. DNA gyrase plays a critical role in maintaining bacterial DNA topology by introducing negative supercoils, resolving torsional stress during replication, transcription, and recombination. This enzyme consists of two subunits (GyrA and GyrB) forming a heterotetramer (A₂B₂). The GyrA subunit contains the active site for DNA cleavage and rejoining, while GyrB harbors ATPase activity. Due to its vital function, DNA gyrase is a prime target for antibiotics like fluoroquinolones, which inhibit its activity by stabilizing DNA-enzyme cleavage complexes.
Recombinant GyrA protein is produced via genetic engineering, typically by cloning the gyrA gene into expression vectors (e.g., plasmids) and expressing it in host systems like *E. coli*. Purification methods such as affinity chromatography yield highly active protein for functional studies. Researchers use recombinant GyrA to investigate enzyme mechanisms, drug interactions, and resistance mutations. Mutations in gyrA, particularly in the quinolone resistance-determining region (QRDR), are linked to fluoroquinolone resistance, making this protein crucial for studying antibiotic resistance evolution.
Additionally, recombinant GyrA aids in structural studies (e.g., X-ray crystallography) to map drug-binding sites and design novel inhibitors. Its applications extend to biotechnology tools, including in vitro DNA manipulation assays. By analyzing GyrA variants, scientists gain insights into bacterial adaptation under selective pressure from antimicrobials, guiding strategies to combat drug-resistant pathogens. This protein’s study remains central to both understanding bacterial genomics and developing next-generation therapeutics.
×
