Rad51 Protein (Human) Rad51 Protein (Human)
- Known as:
- Rad51 Protein (Human) Rad51 Protein (Human)
- Catalog number:
- 10-001
- Product Quantity:
- 20 ug
- Category:
- -
- Supplier:
- BBridge
- Gene target:
- Rad51 Protein (Human)
Related genes to: Rad51 Protein (Human) Rad51 Protein (Human)
- Gene:
- RAD51 NIH gene
- Name:
- RAD51 recombinase
- Previous symbol:
- RAD51A, RECA
- Synonyms:
- HsRad51, HsT16930, BRCC5, FANCR
- Chromosome:
- 15q15.1
- Locus Type:
- gene with protein product
- Date approved:
- 1993-05-26
- Date modifiied:
- 2017-05-02
Related products to: Rad51 Protein (Human) Rad51 Protein (Human)
Related articles to: Rad51 Protein (Human) Rad51 Protein (Human)
- RAD51 paralogs (RAD51B, RAD51C, RAD51D, XRCC2, and XRCC3) are evolutionarily conserved essential proteins for cell survival and genome maintenance. RAD51 paralogs were originally identified to play a role in homologous recombination-mediated repair of DNA double-strand breaks (DSBs). However, investigations over the last decade have uncovered new roles of RAD51 paralogs beyond DSB repair in replication stress responses, including replication fork progression, fork stability, and its restart. Recent structural studies have not only uncovered the molecular architecture of previously known RAD51 paralog complexes but also identified novel paralog complex assemblies, providing mechanistic insights into their various genome-maintenance functions. Additionally, a role for RAD51 paralogs in resolving R-loops has been identified, and studies with cancer-associated variants suggest that RAD51 paralogs are potential determinants of cancer susceptibility and therapeutic responses. In the present review, we highlight the recently deciphered structures and novel functions of RAD51 paralog complexes and discuss the clinical and therapeutic implications. - Source: PubMed
Dwivedi Harsh KumarBhattacharya DebanjaliKadupatil SharivaNagaraju Ganesh - The BRCA1-associated RING domain protein 1 (BARD1) is the obligate binding partner of the tumor suppressor breast cancer type 1 susceptibility protein (BRCA1) and plays a critical role in maintaining genome integrity. BARD1 contains structured N- and C-terminal domains that mediate heterodimerization with BRCA1, recognition of chromatin marks, and DNA repair functions. Approximately 40% of BARD1 is intrinsically disordered, particularly in the central region of the protein. This intrinsically disordered region (IDR) engages DNA and key repair proteins such as RAD51, BLM, and WRN. DNA binding through the BARD1 IDR facilitates H2A ubiquitination by the BRCA1-BARD1 complex and is essential for stimulating long-range DNA end resection during homologous recombination, underscoring its role in accurate DNA repair. Despite these insights, structural characterization of the IDR remains limited, leaving questions regarding its functional interplay with BRCA1 and other repair factors unresolved. Here, we report the backbone resonance assignments of a BARD1 IDR construct spanning residues 124-270, providing a foundation for future studies aimed at understanding how the disordered regions of BARD1 interact with various binding partners, and cooperates with itself and BRCA1 to regulate genome stability. - Source: PubMed
Publication date: 2026/09/01
Dinh Hoang HJasper Angela MBaudin AntoineSung PatrickLibich David S - Heat stress (HS) impairs boar reproductive capacity via damaging Sertoli cells (SCs) and disrupting the integrity of the blood-testis barrier (BTB). This present study investigated the protective effects and underlying molecular mechanisms of PTD-FNK against HS-induced injury in porcine SCs. A HS model (43 °C, 1 h) was established, and 0.1 nM was determined as the optimal working concentration of PTD-FNK. Results showed that PTD-FNK effectively reversed HS-induced BTB disruption by restoring the expression levels of tight junction proteins (Claudin-1, Occludin, ZO-1, and Cx43) to baseline levels ( < 0.05). Concurrently, PTD-FNK alleviated HS-induced oxidative stress by enhancing total antioxidant capacity (T-AOC) and superoxide dismutase (SOD) activity, while reducing malondialdehyde (MDA) content ( < 0.05). It also suppressed HS-triggered apoptosis by downregulating the expression of pro-apoptotic proteins (Caspase-3/8/9 and Bax) and upregulating the anti-apoptotic protein Bcl-2 ( < 0.05). Furthermore, PTD-FNK maintained cellular homeostasis by regulating mitochondrial dynamics-restoring mitochondrial membrane potential (MMP) and balancing the expression of fusion-related protein Mfn1 and fission-related protein Drp1.Transcriptomic and LY294002 experiments confirmed PTD-FNK exerted effects via the PI3K/AKT pathway, modulating ID3, H2AX, DDIT3, CDKN1C, RAD51, and TP53. Thus, PTD-FNK protects SCs from HS through multi-target regulation dependent on PI3K/AKT, providing a novel strategy for boar reproductive health under HS. - Source: PubMed
Publication date: 2026/08/12
Huang QiuyanMa QiqiYang ShiyuWang YanlingZheng BinJi WeixiaSong XingxingZhang XinLi XunWang XiaoyeWang SutianHu Chuanhuo - Prophylactic gynecologic surgery is increasingly performed for non-BRCA germline mutations despite limited evidence regarding pathologic findings and long-term outcomes. This study compares histopathologic findings at prophylactic surgery (serous tubal intra-epithelial carcinoma and/or high-grade serous carcinoma) and longitudinal oncologic outcomes between the largest reported cohort of low- and moderate-risk non-BRCA mutation carriers and a cohort of high-risk BRCA1/2 mutation carriers. - Source: PubMed
Publication date: 2026/08/07
Mubeen AyshaDhall DeeptiSharma Aarti E - Myotonic Dystrophy Type 2 is a genetic disorder caused by expanded CCTG DNA repeats in the gene. By using a genetic assay in and knocking out , we previously found that homologous recombination is involved in large-scale CCTG repeat contractions. In this study, we measured contraction rates using the allele, which is defective in homology search and strand invasion. We found that the mean contraction rate in the strain was indistinguishable from , indicating that structural properties alone of the repetitive CCTG sequence cannot initiate double strand break repair by promoting strand invasion. - Source: PubMed
Publication date: 2026/08/10
Rutkowski Symphony ASerumaga Neila VBond Eva JKim Jane C