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Merck
CN

06-1130

Anti-RNF168 Antibody

别名:

E3 ubiquitin-protein ligase RNF168, RING finger protein 168

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eCl@ss:
32160702
UNSPSC Code:
12352203
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biological source

rabbit

antibody form

affinity isolated antibody

clone

polyclonal

purified by

affinity chromatography

species reactivity

human

technique(s)

immunoprecipitation (IP): suitable, western blot: suitable

NCBI accession no.

UniProt accession no.

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General description

RNF168 is a ubiquitin ligand that binds to ubiquinated histone H2A and localizes to sites of DNA damage. RNF168-dependent chromatin modifications cause 53BP1 and BRCA1 to accumulated at the site. A mutation in RNF168 has been associated with RIDDLE syndrome, an immunodeficiency and radiosensitivity disorder. RNF168 is responsible for securing repair factors at sites of DNA damage. RNF168 has two MIU (motif interacting with ubiquitin) and one UMI (UIM- and MIU-related UBD) ubiquitin binding domains (UBDs) which are essential for proper localization of RNF168.
~79 kDa observed.

Immunogen

Histidine-tagged recombinant protein corresponding to the C-terminus of human RNF168.

Application

Anti-RNF168 Antibody is a Rabbit Polyclonal Antibody for detection of RNF168 also known as E3 ubiquitin-protein ligase RNF168 & has been validated in WB.
Immunoprecipitation Analysis: A representative lot of this antibody was used to immunoprecipitate RNF168 from whole cell lysates (Zhao, H., et al. (2014) Cell Cycle. 13(11):1–11).
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Chromatin Biology

Biochem/physiol Actions

This antibody recognizes RNF168 at the C-terminus.

Physical form

Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Preparation Note

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Control
Jurkat cell lysate
Evaluated by Western Blot in Jurkat cell lysate.

Western Blot Analysis: 0.1 μg/mL of this antibody detected RNF168 on 10 μg of Jurkat cell lysate.

Other Notes

Concentration:Please refer to the Certificate of Analysis for the lot-specific concentration.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial

存储类别

10-13 - German Storage Class 10 to 13

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Hongchang Zhao et al.
Cell cycle (Georgetown, Tex.), 13(11), 1777-1787 (2014-04-16)
Timely and proper cellular response to DNA damage is essential for maintenance of genome stability and integrity. B-cell lymphoma/leukemia 10 (BCL10) facilitates ubiquitination of NEMO in the cytosol, activating NFκB signaling. Translocation and/or point mutations of BCL10 associate with mucosa-associated
Katherine N Choe et al.
EMBO reports, 17(6), 874-886 (2016-05-06)
Defects in DNA replication, DNA damage response, and DNA repair compromise genomic stability and promote cancer development. In particular, unrepaired DNA lesions can arrest the progression of the DNA replication machinery during S-phase, causing replication stress, mutations, and DNA breaks.
Meilen C Muñoz et al.
The Journal of biological chemistry, 287(48), 40618-40628 (2012-10-12)
RNF168 promotes chromosomal break localization of 53BP1 and BRCA1; 53BP1 loss rescues homologous recombination (HR) in BRCA1-deficient cells. RNF168 depletion suppresses HR defects caused by BRCA1 silencing; RNF168 influences HR similarly to 53BP1. RNF168 is important for HR defects caused
Kathy Shire et al.
Journal of cell science, 129(3), 580-591 (2015-12-18)
Promyelocytic leukemia (PML) protein forms the basis of PML nuclear bodies (PML NBs), which control many important processes. We have screened an shRNA library targeting ubiquitin pathway proteins for effects on PML NBs, and identified RNF8 and RNF168 DNA-damage response
Lianzhong Zhang et al.
Genomics, proteomics & bioinformatics, 16(6), 428-438 (2018-12-12)
DNA damage response (DDR) is essential for maintaining genome stability and protecting cells from tumorigenesis. Ubiquitin and ubiquitin-like modifications play an important role in DDR, from signaling DNA damage to mediating DNA repair. In this report, we found that the

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