| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | dnaB |
| Uniprot No | Q8FB22 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-471aa |
| 氨基酸序列 | MAGNRPFNKQQTDNRERDPQVAGLKVPPHSIEAEQSVLGGLMLDNERWDDVAERVVADDFYTRPHRHIFTEMARLQESGSPIDLITLAESLERQGQLDSVGGFAYLAELSKNTPSAANISAYADIVRERAVVREMISVANEIAEAGFDPQGRTSEDLLDLAESRVFKIAESRANKDEGPKNIADVLDATVARIEQLFQQPHDGVTGVNTGYDDLNKKTAGLQPSDLIIVAARPSMGKTTFAMNLVENAAMLQDKPVLIFSLEMPSEQIMMRSLASLSRVDQTKIRTGQLDDEDWARISGTMGILLEKRNIYIDDSSGLTPTEVRSRARRIAREHGGIGLIMIDYLQLMRVPALSDNRTLEIAEISRSLKALAKELNVPVVALSQLNRSLEQRADKRPVNSDLRESGSIEQDADLIMFIYRDEVYHENSDLKGIAEIIIGKQRNGPIGTVRLTFNGQWSRFDNYAGPQYDDE |
| 预测分子量 | 58.4 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dnaB重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: *"Mechanism of DnaB Helicase in Bacterial DNA Replication"*
**作者**: Kaguni, J.M., et al.
**摘要**: 研究了大肠杆菌DnaB解旋酶在DNA复制中的分子机制，揭示其通过ATP水解驱动双链DNA解旋，并与DnaG primase协同促进复制叉延伸的关键作用。
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2. **文献名称**: *"Reconstitution of DnaB-DnaC Complex in Vitro Reveals Helicase Loading Mechanism"*
**作者**: Wickner, S., Kornberg, A.
**摘要**: 通过体外重组实验证明DnaB与DnaC蛋白形成复合物，阐明了DnaC在复制起点协助DnaB解旋酶装载到单链DNA上的分子机制。
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3. **文献名称**: *"Expression and Purification of Recombinant DnaB Helicase for Structural Studies"*
**作者**: Seitz, H., et al.
**摘要**: 报道了利用大肠杆菌表达系统高效制备带有His标签的重组DnaB蛋白，并通过亲和层析纯化获得高纯度样品，为后续结构生物学研究奠定基础。
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如需更多文献或特定方向的研究，可进一步补充说明。
DnaB is a crucial helicase enzyme in prokaryotic DNA replication, primarily studied in model organisms like *Escherichia coli*. As a member of the AAA+ ATPase superfamily, it plays a central role in unwinding double-stranded DNA at replication forks, enabling the progression of DNA synthesis. During replication initiation, DnaB is loaded onto single-stranded DNA (ssDNA) by the initiator protein DnaA, forming the core of the replisome. Its hexameric ring structure encircles the lagging strand, and its ATP-dependent helicase activity separates DNA strands bidirectionally, creating replication forks essential for both leading and lagging strand synthesis.
DnaB interacts with other replication machinery components, including the primase DnaG, which synthesizes RNA primers for DNA polymerase III. This coordination ensures synchronized synthesis of both DNA strands. Structural studies reveal that DnaB adopts dynamic conformational changes during DNA unwinding, with its N-terminal domain facilitating protein-protein interactions and its C-terminal domain harboring helicase activity.
Recombinant DnaB proteins, produced via heterologous expression systems like *E. coli*, retain enzymatic activity and are widely used to study replication mechanisms, helicase dynamics, and protein interactions *in vitro*. These engineered variants enable site-directed mutagenesis to dissect functional domains or improve stability for biochemical assays. Research on DnaB has broader implications for understanding bacterial genome maintenance, antibiotic development targeting replication enzymes, and synthetic biology applications requiring controlled DNA unwinding. Its conserved functional motifs also provide insights into helicase evolution across domains of life.
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