Product Details

Uniprot No.

Target Names

RAD1

Alternative Names

Cell cycle checkpoint protein Hrad1 antibody; Cell cycle checkpoint protein Rad 1 A / B antibody; Cell cycle checkpoint protein RAD1 antibody; Checkpoint control protein HRAD1 antibody; Checkpoint control protein RAD1 antibody; DNA repair exonuclease antibody; DNA repair exonuclease rad1 antibody; DNA repair exonuclease rad1 homolog antibody; DNA repair exonuclease REC1 antibody; DNA repair protein RAD1 antibody; EC 3.1.11.2 antibody; Exonuclease homolog RAD1 antibody; GTP-binding protein RAD antibody; hRAD 1 antibody; hRAD1 antibody; MGC77779 antibody; RAD 1 antibody; RAD antibody; RAD1 antibody; RAD1 homolog (S. pombe) antibody; RAD1 homolog antibody; Rad1 like DNA damage checkpoint antibody; Rad1 like DNA damage checkpoint protein antibody; RAD1; S. pombe; homolog of antibody; Rad1-like DNA damage checkpoint protein antibody; RAD1_HUMAN antibody; Ras associated with diabetes antibody; REC 1 antibody; REC1 antibody; RRAD antibody

Raised in

Rabbit

Species Reactivity

Human,Mouse,Rat

Immunogen

Human RAD1

Immunogen Species

Homo sapiens (Human)

Isotype

IgG

Purification Method

Antigen Affinity Purified

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. -20°C, Avoid freeze / thaw cycles.

Tested Applications

ELISA,WB,IHC

Protocols

ELISA Protocol
Western Blotting(WB) Protocol
Immunohistochemistry (IHC) Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Target Background

Function

Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity.

Gene References into Functions

Dominant alleles of RAD51, TP53 and XRCC1 combined genotypes indicated a strong protective role against hereditary breast cancer. PMID: 26954070
Intramolecular binding of the rad9 C-terminus in the checkpoint clamp Rad9-Hus1-Rad1 is closely linked with its DNA binding. PMID: 26088138
Data show models for the ternary PCNA/FEN1/DNA and Rad9-Rad1-Hus1 (9-1-1 complex)/FEN1/DNA assemblies. PMID: 22586102
The RAD1 is loaded to damaged sites where it serves as a platform for the selective recruitment of checkpoint and repair proteins. PMID: 21978893
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 PMID: 20545769
9-1-1 complex is a component of the mismatch repair involved in MNNG-induced damage response. PMID: 20188637
Rad9-Rad1-Hus1 complex enhances in vitro activity of 8-oxoguanine DNA glycosylase. PMID: 19615952
Rad9, Hus1, and Rad1 heterotrimeric complex chromatin binding is a proximal event in the checkpoint signaling cascade PMID: 12228248
RAD1 is a potential intrinsic chaperone in the stabilization of HUS1 for the heterotrimeric (RAD9-RAD1-HUS1) checkpoint complex formation. PMID: 15122316
The human Rad9/Rad1/Hus1 complex interacts with and stimulates DNA polymerase beta activity. PMID: 15314187
complex with rad9 and hus1 is a damage-specific activator of flap endonuclease 1 PMID: 15556996
The long-patch base excision machinery is an important target of the Rad9-Rad1-Hus1 complex, thus enhancing the quality control of DNA. PMID: 15871698
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 PMID: 16216273
human DNA ligase I is stimulated by the Rad9-rad1-Hus1 checkpoint complex PMID: 16731526
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. PMID: 16814252
Human NEIL1 DNA glycosylase activity is significantly stimulated by hRad1 and by the Rad9/Rad1/Hus1 heterotrimer. PMID: 17395641
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. PMID: 17493829
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 PMID: 17583730
Human thymine DNA glycosylase activity is significantly stimulated by hHus1, hRad1, hRad9 separately, and by the 9-1-1 complex. PMID: 17855402
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). PMID: 19523882
The interdomain connecting loops (IDC loop) of hRad9, hHus1, and hRad1 are largely divergent and unique structural features of the 9-1-1 complex that are proposed to contribute to DNA damage recognition. PMID: 19535328