ABE367
Anti-RNF168 Antibody
from rabbit, purified by affinity chromatography
Synonym(s):
E3 ubiquitin-protein ligase RNF168, hRNF168, RING finger protein 168, RNF168
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
purified by
affinity chromatography
species reactivity
human, mouse
technique(s)
immunocytochemistry: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... RNF168(165918)
Related Categories
General description
E3 ubiquitin-protein ligase RNF168 (UniProt Q8IYW5; also known as hRNF168, RING finger protein 168) is encoded by the RNF168 gene (Gene ID 165918) in human. Ubiquitylation/Ubiquitination is an essential early signal in the DNA damage repair process. Multiple E3 ligases, including RNF2 (RING2), RNF8 and RNF168, mediate the addition of K63-linked polyubiquitin chains to histone 2A (H2A) and H2AX, which in turn recruits DNA damage repair proteins, e.g., RAP80, BRCA1. In addition, SUMOylation and NEDDylation are also involved in the DNA damage response. RNF168 is a dual specificity E3 ligase that mediates both the ubiquitination and NEDDylation of H2A and H2AX. The two types of modifications compete against each other and NEDD8 modification of H2A and H2AX blocks the recruitment of BRCA1 at DNA damage repair sites. RNF168 itself is also subjected to NEDD8 modification and NEDDylation of RNF168 is necessary for its ubiquitin ligase activity. Inhibition of RNF168 NEDDylation impairs its interaction with E2 enzyme Ubc13 (UBE2N). Likewise, downregulating RNF168 NEDDylation by the deNEDDylating enzyme NEDP1, or due to mutations of the NEDD8-conjugating enzyme UBC12, decreases H2A and H2AX ubiquitylation. RNF168 Mutations are linked to RIDDLE (radiosensitivity, immunodeficiency dysmorphic features and learning difficulties) syndrome.
Specificity
This antibody detects RNF168 in a lymphoblastoid cell line (LCL) derived from a healthy donor, but not LCL derived from a RIDDLE (radiosensitivity, immunodeficiency dysmorphic features and learning difficulties) syndrome patient.
Immunogen
Epitope: C-terminus
GST-tagged recombinant human RNF168.
Application
Immunocytochemistry Analysis: 1.0 µg/mL from a representative lot detected RNF168 in HeLa, A431, HUVEC, and NIH/3T3 cells.
Immunohistochemistry Analysis: A representative lot detected RNF168 in frozen human lung adenocarcinoma tissue sections (Xie, X., et al. (2018) Nat. Cell Biol. 20(3); 320-331).
Immunohistochemistry Analysis: A representative lot detected RNF168 in frozen human lung adenocarcinoma tissue sections (Xie, X., et al. (2018) Nat. Cell Biol. 20(3); 320-331).
Research Category
Epigenetics & Nuclear Function
Epigenetics & Nuclear Function
Research Sub Category
Chromatin Biology
Chromatin Biology
Use Anti-RNF168 Antibody (Rabbit Polyclonal Antibody) validated in WB, ICC, IF to detect RNF168 also known as E3 ubiquitin-protein ligase RNF168.
Quality
Evaluated by Western Blotting in SA13 human B cell lysate.
Western Blotting Analysis: A 1:1,000 dilution of this antibody detected RNF168 in 8 µg of SA13 human B cell lysate.
Western Blotting Analysis: A 1:1,000 dilution of this antibody detected RNF168 in 8 µg of SA13 human B cell lysate.
Target description
~75 kDa observed. Uncharacterized band(s) may appear in some lysates.
Physical form
Affinity purified
Purified rabbit polyclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Storage and Stability
Stable for 1 year at 2-8°C from date of receipt.
Analysis Note
Control
HeLa cell lysate
HeLa 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 uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Find documentation for the products that you have recently purchased in the Document Library.
BCL10 regulates RNF8/RNF168-mediated ubiquitination in the DNA damage response.
Zhao, H; Zhu, M; Dou, G; Zhao, H; Zhu, B; Li, J; Liao, J; Xu, X
Cell Cycle null
Wenwen Wu et al.
Cancer science, 107(10), 1406-1415 (2016-10-30)
The breast and ovarian cancer predisposition protein BRCA1 forms three mutually exclusive complexes with Fanconi anemia group J protein (FANCJ, also called BACH1 or BRIP1), CtIP, and Abraxas/RAP80 through its BRCA1 C terminus (BRCT) domains, while its RING domain binds
Flavia Michelini et al.
Nature cell biology, 19(12), 1400-1411 (2017-11-29)
The DNA damage response (DDR) preserves genomic integrity. Small non-coding RNAs termed DDRNAs are generated at DNA double-strand breaks (DSBs) and are critical for DDR activation. Here we show that active DDRNAs specifically localize to their damaged homologous genomic sites
Hanif Rassoolzadeh et al.
Nucleus (Austin, Tex.), 6(5), 417-424 (2016-01-07)
We recently demonstrated that WRAP53β acts as a key regulator of ubiquitin-dependent repair of DNA double-strand breaks. Here, we applied the proximity ligation assay (PLA) to show that at such breaks WRAP53β accumulates in close proximity to γH2AX and, furthermore
I K Mandemaker et al.
Scientific reports, 7(1), 15353-15353 (2017-11-12)
The DNA damage response (DDR), comprising distinct repair and signalling pathways, safeguards genomic integrity. Protein ubiquitylation is an important regulatory mechanism of the DDR. To study its role in the UV-induced DDR, we characterized changes in protein ubiquitylation following DNA
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