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anti-Human RAD1 Anticorps:
anti-Mouse (Murine) RAD1 Anticorps:
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Dominant alleles of RAD51, TP53 and XRCC1 combined genotypes indicated a strong protective role against hereditary breast cancer.
Intramolecular binding of the rad9 C-terminus in the checkpoint clamp Rad9-Hus1-Rad1 is closely linked with its DNA binding.
Data show models for the ternary PCNA/FEN1/DNA and Rad9-Rad1-Hus1 (9-1-1 complex)/FEN1/DNA assemblies.
The RAD1 is loaded to damaged sites where it serves as a platform for the selective recruitment of checkpoint and repair proteins.
CK2 plays a crucial role in the ATR-dependent checkpoint pathway through its ability to phosphorylate Ser-341 and Ser-387 of the Rad9 subunit of the Rad9-Hus1-Rad1 complex
9-1-1 complex is a component of the mismatch repair involved in MNNG-induced damage response.
Rad9-Rad1-Hus1 complex enhances in vitro activity of 8-oxoguanine DNA glycosylase.
Rad9, Hus1, and Rad1 heterotrimeric complex chromatin binding is a proximal event in the checkpoint signaling cascade
RAD1 is a potential intrinsic chaperone in the stabilization of HUS1 for the heterotrimeric (RAD9-RAD1-HUS1) checkpoint complex formation.
The human Rad9/Rad1/Hus1 complex interacts with and stimulates DNA polymerase beta activity.
complex with rad9 and hus1 is a damage-specific activator of flap endonuclease 1
The long-patch base excision machinery is an important target of the Rad9-Rad1-Hus1 complex, thus enhancing the quality control of DNA.
PCNA and the Rad9/Rad1/Hus1 complex can independently bind and activate Fen1; acetylation of Fen1 by p300-HAT abolished the stimulatory effect of the complex but not that of PCNA, suggesting a possible mechanism of regulation of this repair pathway
human DNA ligase I is stimulated by the Rad9-rad1-Hus1 checkpoint complex
These data provide in vivo evidence that the human 9-1-1 complex participates in DNA repair in addition to its previously described role in DNA damage sensing.
Human NEIL1 DNA glycosylase activity is significantly stimulated by hRad1 and by the Rad9/Rad1/Hus1 heterotrimer.
we report successful tri-cistronic cloning, overexpression and purification of a three-protein complex of Rad9, Rad1 and Hus1 using a single hexa-histidine tag.
Jab1 physically associates with the 9-1-1 complex; this association is mediated through direct interaction between Jab1 and Rad1, one of the subunits of the 9-1-1 complex
Human thymine DNA glycosylase activity is significantly stimulated by hHus1, hRad1, hRad9 separately, and by the 9-1-1 complex.
The DNA binding domain (DBD) within the hLigI catalytic fragment interacts with both PCNA and the heterotrimeric cell-cycle checkpoint clamp, hRad9-hRad1-hHus1 (9-1-1).
HUS1 acts as a component of the canonical 9-1-1 complex during meiotic prophase I to promote DSB repair and further propose that RAD1 and TOPBP1 respond to unsynapsed chromatin through an alternative mechanism that does not require RAD9 or HUS1.
The rad1 protein is required for repairing DNA lesions induced by UV-light, HU and gamma rays, and for mediating G(2)/M and S/M checkpoint controls.
data indicate that Rad1(K185) is not a functional counterpart of PCNA(K164).
data suggest that Mrad1 is important for preventing tumor development.
This gene encodes a component of a heterotrimeric cell cycle checkpoint complex, known as the 9-1-1 complex, that is activated to stop cell cycle progression in response to DNA damage or incomplete DNA replication. The 9-1-1 complex is recruited by RAD17 to affected sites where it may attract specialized DNA polymerases and other DNA repair effectors. Alternatively spliced transcript variants of this gene have been described.
DNA repair exonuclease REC1
, DNA repair exonuclease rad1 homolog
, cell cycle checkpoint protein Hrad1
, cell cycle checkpoint protein RAD1
, checkpoint control protein HRAD1
, exonuclease homolog RAD1
, rad1-like DNA damage checkpoint protein
, RAD1 homolog (S. pombe)
, RAD1 homolog
, Cell cycle checkpoint protein RAD1
, cell cycle checkpoint protein rad1