| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RAD51 |
| Uniprot No | Q06609 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-339aa |
| 氨基酸序列 | GSHMAMQMQL EANADTSVEE ESFGPQPISR LEQCGINAND VKKLEEAGFH TVEAVAYAPK KELINIKGIS EAKADKILAE AAKLVPMGFT TATEFHQRRS EIIQITTGSK ELDKLLQGGI ETGSITEMFG EFRTGKTQIC HTLAVTCQLP IDRGGGEGKA MYIDTEGTFR PERLLAVAER YGLSGSDVLD NVAYARAFNT DHQTQLLYQA SAMMVESRYA LLIVDSATAL YRTDYSGRGE LSARQMHLAR FLRMLLRLAD EFGVAVVITN QVVAQVDGAA MFAADPKKPI GGNIIAHAST TRLYLRKGRG ETRICKIYDS PCLPEAEAMF AINADGVGDA KD |
| 预测分子量 | 37 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RAD51重组蛋白的3-4篇关键文献及其摘要概述：
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1. **文献名称**：*Mechanisms and regulation of mitotic recombination in Saccharomyces cerevisiae*
**作者**：Symington, L. S., Rothstein, R., & Lisby, M.
**摘要**：综述了RAD51蛋白在真核生物同源重组修复(HR)中的核心作用，包括其与单链DNA结合形成核蛋白丝的机制，以及与其他辅助因子(如BRCA2)协同修复DNA双链断裂(DSBs)的过程。
2. **文献名称**：*Homologous recombination and its role in cancer genesis and treatment*
**作者**：Jasin, M., & Rothstein, R.
**摘要**：探讨了RAD51介导的同源重组在维持基因组稳定性中的重要性，指出RAD51功能缺陷可能导致染色体异常和癌症发生，同时强调了其在化疗耐药性中的潜在影响。
3. **文献名称**：*Human RAD51 recombination: A key player in DNA repair and genome maintenance*
**作者**：Kowalczykowski, S. C.
**摘要**：通过体外实验揭示了RAD51在DNA链交换和重组中间体形成中的动态行为，并分析了其与辅助蛋白(如RAD54)的协同作用机制。
4. **文献名称**：*Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy*
**作者**：Ashworth, A., & D'Andrea, A. D.
**摘要**：讨论了BRCA1/2突变肿瘤细胞依赖RAD51介导的修复通路的合成致死效应，为PARP抑制剂等靶向疗法的开发提供了理论依据。
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这些文献涵盖了RAD51在DNA修复、癌症发生及治疗中的核心机制和临床应用。
RAD51 is a crucial eukaryotic recombinase that plays a central role in homologous recombination (HR), a high-fidelity DNA repair pathway essential for maintaining genomic stability. It is evolutionarily conserved and functionally analogous to bacterial RecA. RAD51 facilitates the repair of DNA double-strand breaks (DSBs) and stalled replication forks by promoting strand pairing and exchange between homologous DNA sequences. This process ensures accurate repair while minimizing mutagenic outcomes, distinguishing HR from error-prone repair mechanisms.
During HR, RAD51 assembles into helical filaments on single-stranded DNA (ssDNA) regions generated by resection of DSBs. These nucleoprotein filaments mediate homology search and strand invasion into undamaged sister chromatids or homologous chromosomes, forming a displacement loop (D-loop) that serves as a template for accurate repair. RAD51 activity is tightly regulated by various accessory proteins, including BRCA2. RAD52. and RAD51 paralogs, which facilitate filament formation, stability, and disassembly. Post-translational modifications such as phosphorylation and ubiquitination further modulate its function.
Dysregulation of RAD51 is linked to genome instability, cancer predisposition, and therapy resistance. Germline mutations in BRCA1/2. which interact directly with RAD51. are associated with hereditary breast and ovarian cancers. Paradoxically, while HR defects in cancers can sensitize cells to DNA-damaging agents, RAD51 overexpression in tumors often confers resistance to radiotherapy and chemotherapy by enhancing repair capacity. This dual role makes RAD51 a potential therapeutic target; inhibitors are being explored to sensitize HR-proficient cancers or exploit synthetic lethality in combination with PARP inhibitors.
Beyond repair, RAD51 participates in meiotic recombination and telomere maintenance. Its expression levels are being investigated as predictive biomarkers for cancer treatment response. Structural studies of RAD51-DNA complexes continue to inform the development of small-molecule modulators, highlighting its significance in both basic biology and translational applications.
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