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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OB |
| Uniprot No | P55287 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 54-617aa |
| 氨基酸序列 | MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMGWV WNQFFVIEEY TGPDPVLVGR LHSDIDSGDG NIKYILSGEG AGTIFVIDDK SGNIHATKTL DREERAQYTL MAQAVDRDTN RPLEPPSEFI VKVQDINDNP PEFLHETYHA NVPERSNVGT SVIQVTASDA DDPTYGNSAK LVYSILEGQP YFSVEAQTGI IRTALPNMDR EAKEEYHVVI QAKDMGGHMG GLSGTTKVMI TLTDVNDNPP KFPQSVYQMS VSEAAVPGEE VGRVKAKDPD IGENGLVTYN IVDGDGMESF EITTDYETQE GVIKLKKPVD FETKRAYSLK VEAANVHIDP KFISNGPFKD TVTVKIAVED ADEPPMFLAP SYIHEVQENA AAGTVVGRVH AKDPDAANSP IRYSIDRHTD LDRFFTINPE DGFIKTTKPL DREETAWLNI TVFAAEIHNR HQEAKVPVAI RVLDVNDNAP KFAAPYEGFI CESDQTKPLS NQPIVTISAD DKDDTANGPR FIFSLPPEII HNPNFTVRDN RDNTAGVYAR RGGFSRQKQD LYLLPIVISD GGIPPMSSTN TLTIKVCGCD VNGALLSCNA EAYILNAGLS T |
| 预测分子量 | 66 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OB重组蛋白的3篇参考文献示例(内容基于领域内典型研究方向整合，非真实文献)：
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1. **文献名称**：Recombinant Expression and Structural Analysis of the OB-Fold Domain in Human Single-Stranded DNA-Binding Protein 1
**作者**：Smith J. et al.
**摘要**：本研究通过大肠杆菌表达系统成功制备了人源单链DNA结合蛋白1(hSSB1)的OB结构域重组蛋白，并利用X射线晶体学解析了其三维结构。结果显示，该OB结构域在结合单链DNA时发生构象变化，为理解DNA修复机制提供了结构基础。
2. **文献名称**：Functional Characterization of a Recombinant OB-Protein from Thermus thermophilus in DNA Replication
**作者**：Chen L. et al.
**摘要**：作者克隆并表达了嗜热菌来源的OB-fold重组蛋白TtSSB，证明其在高温下仍能稳定结合单链DNA，并显著增强DNA聚合酶的延伸效率。该研究为开发耐高温PCR试剂提供了理论支持。
3. **文献名称**：Engineering OB-Fold Proteins for Enhanced Nucleic Acid Recognition in Biosensing Applications
**作者**：Wang Y. et al.
**摘要**：通过定向进化技术改造OB结构域重组蛋白的核酸结合位点，获得了对特定RNA序列高亲和力的突变体。此蛋白被成功应用于荧光传感器中，实现了低浓度病毒RNA的快速检测。
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**说明**：以上文献为示例性内容，实际研究中建议通过PubMed或Web of Science搜索关键词"OB-fold recombinant protein"、"SSB protein expression"等获取最新具体文献。OB蛋白研究多聚焦于DNA/RNA结合、结构解析及生物工程应用领域。
**Background of OB-Fold Recombinant Proteins**
The OB-fold (oligonucleotide/oligosaccharide-binding fold) is a conserved structural motif found in proteins involved in diverse biological processes, including DNA/RNA metabolism, replication, repair, and telomere maintenance. This β-barrel-like domain, typically composed of 70–150 amino acids, facilitates interactions with nucleic acids, carbohydrates, or other proteins through its characteristic curved β-sheet architecture. OB-fold-containing proteins, such as bacterial single-stranded DNA-binding proteins (SSBs), eukaryotic replication protein A (RPA), and telomere-associated proteins, play essential roles in genome stability and cellular homeostasis.
Recombinant OB-fold proteins are engineered using biotechnological platforms (e.g., *E. coli*, yeast, or mammalian expression systems*) to enable large-scale production for research and therapeutic applications. Their ability to bind single-stranded DNA/RNA with high specificity and affinity makes them valuable tools in molecular biology, including nucleic acid stabilization, PCR enhancement, and structural studies of protein-nucleic acid interactions. For example, modified SSB proteins are utilized in DNA sequencing and diagnostics to improve sensitivity.
Beyond nucleic acid handling, OB-fold domains are explored in synthetic biology for designing artificial proteins or biosensors. Their structural versatility allows engineering of chimeric proteins with tailored functions, such as targeted drug delivery or pathogen detection. Additionally, OB-fold motifs in viral proteins (e.g., adenovirus E1B) highlight their evolutionary adaptability and potential as antiviral targets.
Despite their utility, challenges remain in optimizing recombinant OB-fold proteins for stability, solubility, and functional precision. Advances in computational modeling and directed evolution are addressing these limitations, paving the way for novel biomedical and biotechnological innovations.
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