ABE367
Anti-RNF168 Antibody
from rabbit, purified by affinity chromatography
Synonim(y):
E3 ubiquitin-protein ligase RNF168, hRNF168, RING finger protein 168, RNF168
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About This Item
Kod UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Polecane produkty
pochodzenie biologiczne
rabbit
Poziom jakości
forma przeciwciała
affinity isolated antibody
rodzaj przeciwciała
primary antibodies
klon
polyclonal
oczyszczone przez
affinity chromatography
reaktywność gatunkowa
human, mouse
metody
immunocytochemistry: suitable
western blot: suitable
numer dostępu NCBI
numer dostępu UniProt
Warunki transportu
wet ice
docelowa modyfikacja potranslacyjna
unmodified
informacje o genach
human ... RNF168(165918)
Opis ogólny
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.
Specyficzność
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.
Zastosowanie
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.
Jakość
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.
Opis wartości docelowych
~75 kDa observed. Uncharacterized band(s) may appear in some lysates.
Postać fizyczna
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.
Przechowywanie i stabilność
Stable for 1 year at 2-8°C from date of receipt.
Komentarz do analizy
Control
HeLa cell lysate
HeLa cell lysate
Inne uwagi
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Oświadczenie o zrzeczeniu się odpowiedzialności
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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Kod klasy składowania
12 - Non Combustible Liquids
Klasa zagrożenia wodnego (WGK)
WGK 1
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
Certyfikaty analizy (CoA)
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
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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