| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | pcrA |
| Uniprot No | P56255 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 10-289aa |
| 氨基酸序列 | AHLNKEQQEAVRTTEGPLLIMAGAGSGKTRVLTHRIAYLMAEKHVAPWNILAITFTNKAAREMRERVQSLLGGAAEDVWISTFHSMCVRILRRDIDRIGINRNFSILDPTDQLSVMKTILKEKNIDPKKFEPRTILGTISAAKNELLPPEQFAKRASTYYEKVVSDVYQEYQQRLLRNHSLDFDDLIMTTIQLFDRVPDVLHYYQYKFQYIHIDEYQDTNRAQYTLVKKLAERFQNICAVGDADQSIYRWRGADIQNILSFERDYPNAKVILLEQNYRST |
| 预测分子量 | 34.6 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PcrA重组蛋白的3篇参考文献，简要总结研究内容：
1. **"Functional characterization of the Staphylococcus aureus PcrA helicase"**
*作者：R. M. Sivaramakrishnan, et al. (2019)*
摘要：研究通过重组表达纯化了金黄色葡萄球菌PcrA解旋酶，分析了其ATP酶活性及DNA解旋功能，揭示了其在DNA修复中的关键作用。
2. **"Structural insights into the DNA unwinding mechanism of PcrA helicase"**
*作者：T. J. Smith, et al. (2016)*
摘要：利用重组PcrA蛋白进行X射线晶体学研究，解析了其与DNA结合的构象变化，阐明了解旋酶活性的分子机制。
3. **"PcrA helicase as a potential target for combating multidrug-resistant Staphylococcus aureus"**
*作者：L. Chen & H. Wang (2021)*
摘要：通过重组PcrA蛋白筛选小分子抑制剂，发现特定化合物可抑制其解旋酶活性，为开发新型抗生素提供理论基础。
注：以上文献信息为示例性质，实际研究中建议通过PubMed或Web of Science核对具体文献。
**Background of PcrA Recombinant Protein**
PcrA recombinant protein is a biologically engineered version of the PcrA helicase, originally derived from Gram-positive bacteria such as *Staphylococcus aureus*. PcrA is an ATP-dependent, superfamily 1 (SF1) helicase involved in critical DNA metabolic processes, including replication, repair, and recombination. It unwinds double-stranded DNA into single strands, a function essential for maintaining genomic stability and facilitating DNA transactions.
The interest in PcrA stems from its role in bacterial survival and pathogenicity. Studies have linked PcrA to antibiotic resistance mechanisms, particularly in methicillin-resistant *S. aureus* (MRSA), where it may compensate for helicase deficiencies or interact with mobile genetic elements (e.g., plasmids) to promote resistance gene transfer. Additionally, PcrA shares structural and functional similarities with helicases in other pathogens, making it a model for understanding helicase-driven processes in prokaryotes.
Recombinant PcrA is produced via heterologous expression in *Escherichia coli*, enabling large-scale purification for biochemical and structural studies. Its recombinant form retains native enzymatic activity, allowing researchers to study ATP hydrolysis, DNA binding, and unwinding kinetics *in vitro*. Such studies have provided insights into helicase mechanics and informed the design of inhibitors targeting bacterial helicases.
Furthermore, PcrA’s role in resolving DNA-RNA hybrids (R-loops) and repairing stalled replication forks highlights its potential as a therapeutic target. Inhibiting PcrA could disrupt bacterial DNA repair pathways, sensitizing pathogens to existing antibiotics. Structural analyses (e.g., X-ray crystallography) of recombinant PcrA have revealed conformational changes during ATP-dependent unwinding, offering a blueprint for drug development.
In summary, PcrA recombinant protein serves as a vital tool for exploring bacterial DNA dynamics, antibiotic resistance, and novel antimicrobial strategies, bridging fundamental research and translational applications.
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