SRP2090
RAD51 human
recombinant, expressed in E. coli, ≥80% (SDS-PAGE)
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Synonym(s):
BRCC5, HRAD51, HsRad51, HsT16930, RAD51A, RECA
UNSPSC Code:
12352200
NACRES:
NA.26
Recommended Products
biological source
human
recombinant
expressed in E. coli
assay
≥80% (SDS-PAGE)
form
frozen liquid
mol wt
~39.1 kDa
packaging
pkg of 10 μg
storage condition
avoid repeated freeze/thaw cycles
concentration
500 μg/mL
technique(s)
electrophoretic mobility shift assay: suitable
color
clear colorless
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... RAD51(5888)
General description
RAD51 gene is mapped to human chromosome 15q15.1. It is an Escherichia coli Recombinase A (RecA) homolog and comprises an N-terminal DNA binding domain.
RAD51 is a member of the RecA/RadA/Rad51 protein family which is characterized by a conserved ATP binding core. Human RAD51 shows predominant expression in testis, ovary, and lymphoid tissue.
Biochem/physiol Actions
Properly controlled recombination between homologous DNA molecules (Homologous Recombination - HR) is essential for the maintenance of genome stability and for the prevention of tumorigenesis. RAD51 is a mammalian homologue of yeast RAD51 and bacterial RecA and, like its counterparts, plays a central role in HR. RAD51 coats ssDNA to form a nucleoprotein filament that invades and pairs with a homologous region in duplex DNA. It can then activate strand exchange to generate a crossover between the juxtaposed DNA molecules. In addition to RAD51, these steps require the coordinated action of a number of other homologous-recombination proteins, including the RP-A protein, which binds single-stranded DNA, RAD52, which can bind DNA ends, anneal complementary single-stranded DNA molecules and enhance the specificity of RAD51, and a number of RAD51 paralogs. The tumour-suppressor proteins BRCA1 and BRCA2 colocalize with RAD51 in DNA-damage-induced nuclear foci. BRCA2 has been shown to interact directly with RAD51 and thus plays a direct role in repair by HR, through control of the availability and function of the central mediator, RAD51.
RAD51 interacts with BRCA2 (breast cancer susceptibility protein) and participates in DSB (double strand DNA breaks) repair. BRCA2 sequesters and recruits RAD51 to the site of the damage and promotes the formation of the helical RAD51–single stranded DNA (ssDNA) nucleoprotein filaments. These filaments look for and infiltrate the homologous DNA template, and promote homologous recombination by inducing DNA polymerization and strand exchange. A dominant-negative mutation in this gene is linked with a novel Fanconi anaemia (FA) subtype, a disorder characterized by developmental abnormalities, bone marrow failure and a strong susceptibility to cancer. Association of RAD51 gene with congenital mirror movement disorders signifies the importance of RAD51-mediated homologous recombination in neurodevelopment apart from in DNA repair, cancer susceptibility.
Physical form
Clear and colorless frozen liquid solution
Preparation Note
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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R Gonzalez et al.
British journal of cancer, 81(3), 503-509 (1999-10-03)
Loss of heterozygosity (LOH) in loci of the 15q15.1, 12p13, 1p32, 17q21 and 13q12-13 regions may collaborate in the inactivation of RAD51, RAD52, RAD54, BRCA1, BRCA2 and possibly other genes implicated in the repair of double-stranded DNA and in DNA
Modesti, M., et al.
Genome Biology, 2 (2001)
A novel Fanconi anaemia subtype associated with a dominant-negative mutation in RAD51.
Ameziane N, et al.
Nature Communications, 6:8829 (2015)
X Yu et al.
Proceedings of the National Academy of Sciences of the United States of America, 98(15), 8419-8424 (2001-07-19)
Both the bacterial RecA protein and the eukaryotic Rad51 protein form helical nucleoprotein filaments on DNA that catalyze strand transfer between two homologous DNA molecules. However, only the ATP-binding cores of these proteins have been conserved, and this same core
Junyeop Lee et al.
Nature communications, 13(1), 3396-3396 (2022-06-14)
BRCA2-deficient cells precipitate telomere shortening upon collapse of stalled replication forks. Here, we report that the dynamic interaction between BRCA2 and telomeric G-quadruplex (G4), the non-canonical four-stranded secondary structure, underlies telomere replication homeostasis. We find that the OB-folds of BRCA2
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