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Merck
모든 사진(1)

문서

SRP2090

Sigma-Aldrich

RAD51 human

recombinant, expressed in E. coli, ≥80% (SDS-PAGE)

동의어(들):

BRCC5, HRAD51, HsRad51, HsT16930, RAD51A, RECA

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About This Item

UNSPSC 코드:
12352200
NACRES:
NA.26

생물학적 소스

human

재조합

expressed in E. coli

분석

≥80% (SDS-PAGE)

형태

frozen liquid

분자량

~39.1 kDa

포장

pkg of 10 μg

저장 조건

avoid repeated freeze/thaw cycles

농도

500 μg/mL

기술

electrophoretic mobility shift assay: suitable

색상

clear colorless

NCBI 수납 번호

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−70°C

유전자 정보

human ... RAD51(5888)

일반 설명

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.

생화학적/생리학적 작용

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.

물리적 형태

Clear and colorless frozen liquid solution

제조 메모

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


시험 성적서(COA)

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문서 라이브러리 방문

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)
Hiom, K.,
Current Biology, 9, 446-448 (2000)
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

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