Product Details

Purity

Greater than 85% as determined by SDS-PAGE.

Target Names

RNF168

Uniprot No.

Q8IYW5

Research Area

Epigenetics and Nuclear Signaling

Alternative Names

(hRNF168)(RING finger protein 168)(RING-type E3 ubiquitin transferase RNF168)

Species

Homo sapiens (Human)

Source

Baculovirus

Expression Region

1-571aa

Target Protein Sequence

MALPKDAIPSLSECQCGICMEILVEPVTLPCNHTLCKPCFQSTVEKASLCCPFCRRRVSSWTRYHTRRNSLVNVELWTIIQKHYPRECKLRASGQESEEVADDYQPVRLLSKPGELRREYEEEISKVAAERRASEEEENKASEEYIQRLLAEEEEEEKRQAEKRRRAMEEQLKSDEELARKLSIDINNFCEGSISASPLNSRKSDPVTPKSEKKSKNKQRNTGDIQKYLTPKSQFGSASHSEAVQEVRKDSVSKDIDSSDRKSPTGQDTEIEDMPTLSPQISLGVGEQGADSSIESPMPWLCACGAEWYHEGNVKTRPSNHGKELCVLSHERPKTRVPYSKETAVMPCGRTESGCAPTSGVTQTNGNNTGETENEESCLLISKEISKRKNQESSFEAVKDPCFSAKRRKVSPESSPDQEETEINFTQKLIDLEHLLFERHKQEEQDRLLALQLQKEVDKEQMVPNRQKGSPDEYHLRATSSPPDKVLNGQRKNPKDGNFKRQTHTKHPTPERGSRDKNRQVSLKMQLKQSVNRRKMPNSTRDHCKVSKSAHSLQPSISQKSVFQMFQRCTK
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.

Mol. Weight

66.6 kDa

Protein Length

Full Length

Tag Info

C-terminal 10xHis-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Target Background

Function

E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8-dependent H2A ubiquitination, promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. Following DNA damage, promotes the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF8, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Not able to initiate 'Lys-63'-linked ubiquitination in vitro; possibly due to partial occlusion of the UBE2N/UBC13-binding region. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively).

Gene References into Functions

Results suggest that RNF168 acts as a counterpart of PARP1 in DDR and regulates the HR/NHEJ repair processes through the ubiquitination of PARP1. PMID: 30037213
RNF168 interacts with TOP2alpha to mediate its polyubiquitylation and RNF168 deficiency confers resistance to ICRF-193, a TOP2 catalytic inhibitor, and cytotoxic anti-cancer drug etoposide in cultured human cancers cells. PMID: 27558965
Ub-interacting residues in UDM2 prevent the accumulation of RNF168 to double-strand breaks sites in U2OS cells, whereas those in UDM1 have little effect. PMID: 29330428
We identified 85 overlapping deletions, of which six included the RPL35A gene and all should be had Diamond-Blackfan anemia (DBA).we sequenced the remaining RNF168 gene and examined her fibroblast culture for a DNA double strand break repair deficiency. These results were normal, indicating that the immunodeficiency is unlikely to result from a RNF168 deficiency. PMID: 28432740
deregulated RNF168/53BP1 pathway could promote tumorigenesis by selecting for a more robust, better stress-adapted cancer cell phenotype, through altered DNA repair, fueling genomic instability and tumor heterogeneity PMID: 27841863
The association of RNF168 with PML NBs resulted in increased ubiquitylation. PMID: 26675234
Results reveal an important role of USP7 in regulating ubiquitin-dependent signaling via stabilization of RNF168. PMID: 25894431
CK2/WIP1-mediated modulation of LSD1 phosphorylation facilitates RNF168-dependent ubiquitination and recruitment of 53BP1 to the DNA damage sites. PMID: 25999347
The ubiquitin ligase RNF168 is strictly dependent on the activity that UbK27 is required to promote chromatin ubiquitination following DNA damage. PMID: 25578731
Finding that RNF8 is less abundant than RNF168 identifies RNF8 as a rate-limiting determinant of focal repair complex assembly PMID: 25304081
Depletion of RNF8 or RNF168 blocks the degradation of diffusely localized nuclear 53BP1. PMID: 25337968
The E3 ligase RNF168 promotes both H2A ubiquitylation and neddylation. RNF168 is itself a substrate for NEDD8, and neddylation of RNF168 is necessary for its E3 ubiquitin activity. PMID: 24634510
The acidic patch functions within the nucleosome as nucleosomes containing a mutated acidic patch exhibit defective H2A/H2AXub by RNF168 and RING1B/BMI1 in vitro PMID: 24603765
Taken together, the results suggested that USP3 is a negative regulator of ubiquitination signaling, counteracting RNF168- and RNF8-mediated ubiquitination PMID: 24196443
Before their localization to DNA double strand breaks, RNF168 interacts with 53BP1 and modifies it through the addition of a chain of ubiquitin-polypeptides. PMID: 24324146
RNF168 physically interacts with LSD1 and we find this interaction to be important for LSD1 recruitment to DNA damage sites. PMID: 24217620
study unveils a functional link between DNA damage-induced poly(ADP-ribosyl)ation, SMARCA5-mediated chromatin remodeling and RNF168-dependent signaling and repair of DSBs. PMID: 23264744
RNF168, in complex with RAD6A or RAD6B, is activated in the DNA-damage-induced protein ubiquitination cascade. PMID: 23525009
Unlike RNF8, RNF168 RING domain did not stably associate with UBC13 at double-stranded DNA breaks in vitro or in vivo. PMID: 23255131
RNF168 is important for defects in homologous recombination caused by loss of the BRCA1 in breast cancer cells. PMID: 23055523
Ubiquitin-dependent signaling during the DNA damage response (DDR) to double-strand breaks is initiated by two E3 ligases, RNF8 and RNF168, targeting histone H2A and H2AX. Study shows that ubiquitin chains per se are insufficient for signaling, but RNF168 target ubiquitination is required for DDR. PMID: 22980979
Inactivation of K13 and K15 reduces RNF168- dependent ubiquitination of histones H2As, while inactivation of both N- and C-terminal sites completely abolishes histone ubiquitination. PMID: 22713238
RNF168, its paralog RNF169, RAD18, and the BRCA1-interacting RAP80 protein accumulate at DNA double strand break sites through the use of bipartite modules composed of ubiquitin binding domains. PMID: 22742833
Data show RING finger (RNF) E3 ubiquitin ligase RNF8 dimerizes and binds to E2 ubiquitin-conjugating complex Ubc13/Mms2 with formation of Lys-63 ubiquitin chains, whereas the RNF168 RING domain is a monomer and does not catalyze Lys-6 ubiquitylation. PMID: 22589545
Data show that depletion of RNF8, as well as of the E3 ligase RNF168, reduces telomere-induced genome instability. PMID: 21857671
Studies indicate that Non-proteolytic ubiquitylation of chromatin surrounding DSBs, mediated by the RNF8/RNF168 ubiquitin ligase cascade, has emerged as a key mechanism for restoration of genome integrity. PMID: 21664912
The viral protein ICP0 targets RNF8 and RNF168 for degradation, thereby preventing the deposition of repressive ubiquitin marks and counteracting this repair protein recruitment. PMID: 21698222
this study reveals that human NIPBL is a novel protein recruited to DSB sites, and the recruitment is controlled by MDC1, RNF168 and HP1gamma. PMID: 21784059
The E3 Ubiquitin ligases, RNF8 and RNF168, are recruited to DNA damage foci in late mitosis, presumably to prime sites for the DNA damage response, 53BP1, recruitment in early G1. PMID: 21412056
identification of a novel ubiquitin binding domain present in RNF168, and characterized the interaction surface with ubiquitin, centered on two Leu residues PMID: 21041483
Data identify RNF8 and RNF168, cellular histone ubiquitin ligases responsible for anchoring repair factors at sites of damage, as new targets for ICP0-mediated degradation. PMID: 20075863
Ubiquitin ligase does not protect cells from Nutlin-3-mediated apoptosis, indicating that RNF168 does not regulate 53BP1 protein. PMID: 20080757
Data show that the ATM signalling mediator proteins MDC1, RNF8, RNF168 and 53BP1 are also required for heterochromatic DSB repair. PMID: 20081839
RNF168 defines a new pathway involving sequential ubiquitylations on damaged chromosomes and uncovers a functional cooperation between E3 ligases in genome maintenance. PMID: 19203579
RNF168 is a ubiquitin ligase that functions as chromatin modifier, through histone ubiquitination; upon DNA lesions, RNF168 is recruited to DNA damage response foci where it contributes to increase the amount of ubiquitinated proteins. PMID: 19500350

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Involvement in disease

Riddle syndrome (RIDDLES)

Subcellular Location

Nucleus.

Protein Families

RNF168 family

Database Links

HGNC: 26661

OMIM: 611943

KEGG: hsa:165918

STRING: 9606.ENSP00000320898

UniGene: Hs.250648

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Code	CSB-BP814236HU
MSDS	MSDS
Size	$528
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Human E3 ubiquitin-protein ligase RNF168 (RNF168)

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