RAD51 Antibody - N-terminal region (ARP31731_P050)
- Known as:
- RAD51 Antibody - N-terminal region (ARP31731_P050)
- Catalog number:
- arp31731_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- RAD51 Antibody - N-terminal region (ARP31731_P050)
Related genes to: RAD51 Antibody - N-terminal region (ARP31731_P050)
- 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
- Gene:
- RAD51B NIH gene
- Name:
- RAD51 paralog B
- Previous symbol:
- RAD51L1
- Synonyms:
- REC2, hREC2, R51H2
- Chromosome:
- 14q24.1
- Locus Type:
- gene with protein product
- Date approved:
- 1997-09-12
- Date modifiied:
- 2016-10-05
- Gene:
- RAD51C NIH gene
- Name:
- RAD51 paralog C
- Previous symbol:
- -
- Synonyms:
- RAD51L2, FANCO
- Chromosome:
- 17q22
- Locus Type:
- gene with protein product
- Date approved:
- 1998-02-26
- Date modifiied:
- 2019-04-23
- Gene:
- RAD51D NIH gene
- Name:
- RAD51 paralog D
- Previous symbol:
- RAD51L3
- Synonyms:
- R51H3, Trad, HsTRAD
- Chromosome:
- 17q12
- Locus Type:
- gene with protein product
- Date approved:
- 1998-05-27
- Date modifiied:
- 2019-04-23
Related products to: RAD51 Antibody - N-terminal region (ARP31731_P050)
Related articles to: RAD51 Antibody - N-terminal region (ARP31731_P050)
- Hexavalent chromium [Cr(VI)] is a lung carcinogen. Central to its carcinogenic mechanism are Cr(VI)-induced DNA double strand breaks and chromosome instability. While breaks are usually repaired in healthy cells, Cr(VI) inhibits homologous recombination repair by targeting RAD51. RAD51 paralogs (RAD51B, RAD51C, RAD51D, XRCC2, and XRCC3) are responsible for RAD51 loading and the stabilization of nucleoprotein filaments necessary for DNA strand exchange and repair. This study aimed to investigate the effects of Cr(VI) exposure on RAD51 paralogs. WTHBF-6 cells, a human lung cell line, were exposed to various environmentally and occupationally relevant concentrations of zinc chromate for acute (24 h) and prolonged (120 h) exposure times. After exposure to Cr(VI), we collected RNA for sequencing and assessed the ability of DNA repair proteins to form foci using immunofluorescence. Protein levels were measured with western blotting, RNA-Seq was validated with RT-qPCR, and protein-protein interactions were assessed with the Proximity Ligation Assay (PLA) assay. Cr(VI) transcriptionally repressed all RAD51 paralogs. Further functional analyses showed that Cr(VI) inhibited the foci formation of RAD51D after acute and prolonged exposures and of XRCC2 and XRCC3 after prolonged exposure. Cr(VI) also inhibited overall RAD51D protein expression, as well as its interaction with RAD51. These findings suggest that Cr(VI) inhibits all RAD51 paralogs, but RAD51D might be an early target of Cr(VI), leading to the loss of RAD51 filament formation and function and the overall inhibition of homologous recombination repair. - Source: PubMed
Publication date: 2026/03/23
Williams Aggie RMeaza IdoiaLu HaiyanWise James T FDiven Sandra SToyoda Jennifer HKouokam J CalvinWise John Pierce - The RAD51 recombinase is central to repair of DNA damage arising from stalled or collapsed replication forks and DNA double strand breaks. Its essential role is revealed by the fact that this function evolved in bacteria but was retained in eukaryotes. In humans some of the RAD51 functions have been relegated to several paralogues which evolved by gene duplication. In addition to mutations, most cancers are also characterized by increased chromosomal instability manifesting as translocations, deletions, insertions, and other more complex forms of chromosomal re-arrangements. Given the central role of RAD51 in protecting against chromosomal instability it stands to reason that RAD51 mutations that alter its function should register in cancer cells. However, pan-cancer analyses of analyzed cancer genomes show a marked absence of RAD51 loss of function mutations leading to a so-called "RAD51 paradox": increased chromosomal instability despite normal RAD51 function. One hypothesis is that mutations in the RAD51 paralogues may contribute to the genomic instability, meaning that a lack of mutations in RAD51 may be compensated by an increase of mutations in the paralogues. We queried analyzed cancer genomes from COSMIC and mapped all mutations in RAD51 and its paralogues. This revealed an increase in RAD51B, RAD51C and RAD51D paralogue mutations in human cancers. We used established algorithms to determine the probability that any mutation may affect enzyme function. Although, we did not find many "driver" mutations, numerous paralogue mutations were pathogenic or likely to destabilize enzyme function. In silico 3D structure analysis was then used to analyze the potential effect of some of these mutations on protein structure. Gene expression analysis did not reveal any changes in paralogue expression levels. Further, an evolutionary analysis did not uncover any selective pressure for mutations in RAD51 and its paralogues. A comparison of mutations reported on COSMIC with those reported on ClinVar revealed that many mutations primarily in RAD51C and RAD51D are also hereditary. Thus, it appears that an apparent low level of RAD51 mutations in cancer cells is compensated by an increase in paralogues mutations. - Source: PubMed
Publication date: 2026/05/14
Valentine Anna LHuth Isabella LDuff Nika MRabbani Aisha ZDonahue Kateri NBush Wesley ABouley Renee APetreaca Ruben C - HELQ is a 3'-5' DNA helicase whose loss sensitizes cells to DNA-damaging agents, particularly DNA crosslinkers. HELQ interacts with the RAD51 paralog complex RAD51B-RAD51C-RAD51D-XRCC2 (BCDX2), a key mediator of replication fork reversal. Using DNA fiber assays, we show that HELQ and BCDX2 act epistatically to slow replication fork progression under replication stress. Because fork reversal transiently regresses nascent strands into a four-way junction and reduces net DNA synthesis, this fork slowing provides a functional readout of fork reversal. Directly supporting this model, electron microscopy reveals that reversed fork structures are reduced in HELQ-knockout cells. Consistent with a role in fork reversal, HELQ deletion suppresses nascent strand degradation when BRCA2- or FANCD2-dependent fork protection is lost. Mechanistically, biochemical reconstitution shows that HELQ is stimulated by RPA on fork substrates containing a leading strand gap, and these findings are consistent with the cell-based DNA fiber assays. Together, these results identify HELQ as a specialized regulator of replication fork remodeling that promotes fork reversal through the BCDX2 pathway. - Source: PubMed
Dunbayev YerkinChen Yen-JuSassi LorenzoLee Eun ARa Jae SunChoi MoonjungMukherjee AnirbanVasquez Karen MCostanzo VincenzoChi PeterTakata Kei-Ichi - The repair of DNA double-strand breaks by homologous recombination is essential for genomic integrity, and its dysregulation is a hallmark of cancer. Central to homologous recombination is the RAD51 recombinase, whose assembly into a nucleoprotein filament is governed by five RAD51 paralogues (RAD51B, RAD51C, RAD51D, XRCC2 and XRCC3). Mutations in any of these proteins predispose individuals to multiple cancers or genetic disorders. These paralogues are thought to form two functionally separate complexes RAD51B-RAD51C-RAD51D-XRCC2 (BCDX2) and RAD51C-XRCC3 (CX3), that act independently at different stages of homologous recombination. Here we demonstrate that all five paralogues can assemble into a single, ATP-dependent BCDX2-CX3-RAD51 supercomplex. The architecture of this assembly bound to single-stranded DNA reveals a contiguous filament where the CX3 module stacks atop BCDX2, creating a protofilament template for RAD51 filament formation. We further identify a novel, RAD51B-independent DX2-CX3 complex (RAD51D-XRCC2-RAD51C-XRCC3) functioning as a stable RAD51 anchor on single-stranded DNA, and we capture it in multiple states, including capping RAD51 filament segment. These distinct assemblies are differentially regulated by ATPase activity, defining a dynamic BCDX2-CX3 'loader' and a stable DX2-CX3 'anchor' that provide functional modularity to the homologous recombination machinery. This work provides a unifying mechanism for human RAD51 paralogue function and delivers an atomic blueprint for interpreting disease-causing mutations. - Source: PubMed
Publication date: 2026/03/02
Koo Christopher WXiao JiaqiCoassolo SebastienLiu JieYu ChristineAzumaya Caleigh MGore Steven KCheung Tommy KBrillantes BobbyRose Christopher MHeyer Wolf-DietrichCiferri ClaudioYatskevich Stanislau - Double-strand break (DSB) repair occurs through non-homologous end joining (NHEJ) or homologous recombination (HR). To identify non-canonical factors that influence DSB repair outcomes, we parsed data from pooled genetic screens. Through this approach, we identified the splicing factor SFPQ, which has been previously reported to associate with DSBs and promote repair. Here, we show that SFPQ depletion alters DSB repair via HR. However, in contrast to other published work, we find that SFPQ does not localize to DSBs but instead stabilizes the expression of RAD51 and its paralogs independently of p53 activation or DNA damage. Our findings suggest that SFPQ contributes to constitutive DSB repair by maintaining RAD51 paralog mRNA stability rather than through direct interaction with DSBs or RAD51 proteins. Ultimately, our results highlight indirect mechanisms by which RNA-binding proteins can influence genome stability. - Source: PubMed
Publication date: 2026/02/10
Gotthold SofiaHansen Keile RBrown Andrew NChowdhury Soham PJoyce Christine MVinish VirajRodriguez Sofie IJain SambhavGhasemi Hannah IYoon Amanda CBacal JulienMorrissey Meghan AGardner Brooke MRichardson Chris D