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- Table of Contents
1 Citations
Facts about Cell cycle checkpoint protein RAD17.
Participates in the recruitment of the RAD1-RAD9- HUS1 complex and RHNO1 onto chromatin, and in CHEK1 activation. May also serve as a sensor of DNA replication progression, and may be involved in homologous recombination.
Human | |
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Gene Name: | RAD17 |
Uniprot: | O75943 |
Entrez: | 5884 |
Belongs to: |
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rad17/RAD24 family |
CCYC; cell cycle checkpoint protein (RAD17); cell cycle checkpoint protein RAD17; FLJ41520; HRAD17; R24L; RAD1 (S. pombe) homolog; RAD1 homolog; RAD17 homolog (S. pombe); Rad17; Rad17-like protein; RAD17SP; RAD24; RF-C activator 1 homolog; RF-C/activator 1 homolog
Mass (kDA):
77.055 kDA
Human | |
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Location: | 5q13.2 |
Sequence: | 5; NC_000005.10 (69369297..69414801) |
Overexpressed in various cancer cell lines and in colon carcinoma (at protein level). Isoform 2 and isoform 3 are the most abundant isoforms in non irradiated cells (at protein level). Ubiquitous at low levels. Highly expressed in testis, where it is expressed within the germinal epithelium of the seminiferous tubuli. Weakly expressed in seminomas (testicular tumors).
Nucleus. Phosphorylated form redistributes to discrete nuclear foci upon DNA damage.
You might have questions about optimizing your ELISA experiments Therefore, you might be interested in reading the Boster Bio: Best Uses Of The Rad17 Marker guide. This guide will explain the various choices you need to make in order to optimize your experiment and get the best results. Here are some tips to optimize your experiments:
The Boster Bio RAD17 Cell Based Immuno-ELISA Kit can be used to test RAD17 expression in cells. This method isn't like other ELISA tests. It does not require a cell lysate. Instead, it utilizes a highly sensitive indirect immunohistochemistry procedure to detect RAD17 protein in cells. This kit is particularly useful in screening inhibitors or activators.
EMSA confirmed that the NELFA promoter and RAD17 promoter both have two USF2 binding locations and that the RPA has recruited PCNA into these two regions. When the USF2 gene was knocked down, the expression of RAD17 and NELFA was reduced. These findings indicate that the RAD17 complex is more prone to gapped DNA structures. The DNA template includes two annealed primes located 200 nucleotides apart.
Rad24 is a member of the Rad17 complex is believed to be a DNA damage sensor in budding yeast. Moreover, Rad17 contains limited homology to PCNA which is a processing factor of DNA polymerase that forms a clamp around dsDNA. RAD17 has homology to the five subunits of the RF-C complex, which loads PCNA onto DNA.
The RAD17 complex was manufactured as described in ref. 8. Human RPA was expressed by Escherichia Coli and purified using the protocol as described in the reference. 15. These results indicate that the RAD17 complex can be combined directly with NELFA mRNA. We also found that RAD17 MRNAs and NELFA the mRNAs share a high affinity and are active without RPA.
Incredibly, RAD17 interacts with the RFC2-5-RFC2-5 complex another component of the RFC family. Furthermore, NELFA mRNA inhibits the complex of the Rad17-RFC2-5 interaction, and knockdown of NELFA mRNA has no effect. Further research is needed to understand the mechanism of this interaction. It is still unclear what the underlying mechanism of DNA damage repair signalling pathway is.
RAD17 is necessary for the stoppage of the cell cycle and DNA repair. It has strong similarities to DNA replication factor C and is a part of a complex. It binds chromatin prior to DNA damage and recruits the RAD1 -RAD9-HUS1 checkpoint protein complex. Furthermore, RAD17 phosphorylates the checkpoint ATR kinase, which is responsible for bringing the RAD1-RAD9HUS1 complex to the DNA damage location. Interestingly, it may also be required to phosphorylate.
To determine if RAD17 protein is actually the cause of a damaging process Researchers can purchase an anti-Rad17 antibody. The Boster bio antiphospho-Rad17 antibody (catalog # A02159S646) is compatible with ELISA and WB. The anti-Rad17 antibody reacts with Human, Mouse, and Rat.
The mutation in the gene S23/29A is involved in attracting RAD51 into DNA damage, prevents the recruitment of Ddc1 in live. The mutation also increases the frequency of gH2AX foci during mitosis. In addition, the mutation reduced RAD51 chromatin loading. In addition the mutant Rfa1 has two possible SIMs that could bind poly-SUMO chains in vitro. The mutant S33A/T21A decreased DNA synthesis and increased ssDNA in response to the HU treatment.
Ddc1 fused to GFP also forms subnuclear foci that are single near the telomeric split and multiple foci in other locations following checkpoint adapt. Ddc1 is located at the telomeric double-strand break site in all cells. The Ddc1 protein is recruited rapidly when checkpoint activation occurs and persists in subsequent cell cycle. Inhibition of Ddc1 is related to the presence of Mec1 and Ddc3 in the process of repairing damage, and RAD17 is essential to establish Telomeric foci.
PMID: 9878245 by Dean F.B., et al. cDNA cloning and gene mapping of human homologs for Schizosaccharomyces pombe rad17, rad1, and hus1 and cloning of homologs from mouse, Caenorhabditis elegans, and Drosophila melanogaster.
PMID: 9660800 by Parker A.E., et al. Identification of a human homologue of the Schizosaccharomyces pombe rad17+ checkpoint gene.
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