Recombinant Human E3 Ubiquitin-Protein Ligase Rad18 (RAD18) Protein (His-SUMO)

Name: Recombinant Human E3 Ubiquitin-Protein Ligase Rad18 (RAD18) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09907P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human E3 Ubiquitin-Protein Ligase Rad18 (RAD18) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9NS91
Target Symbol	RAD18
Synonyms	2810024C04Rik; DNA repair protein rad18; E3 ubiquitin-protein ligase RAD18; EC 6.3.2.-; hHR 18; hHR18; hRAD 18; hRAD18; MGC156682; Postreplication repair E3 ubiquitin-protein ligase RAD18; Postreplication repair protein hRAD18p; Postreplication repair protein RAD18; RAD 18; RAD18; RAD18 homolog (S. cerevisiae); RAD18 homolog; RAD18 S. cerevisiae homolog; RAD18 S. cerevisiae homolog of; RAD18 transcript variant; RAD18_HUMAN; Rad18sc; Radiation sensitivity protein 18; RING finger protein 73; RNF 73; RNF73; Structural maintenance of chromosomes protein 6; YCR066W; YCR66W
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MDSLAESRWPPGLAVMKTIDDLLRCGICFEYFNIAMIIPQCSHNYCSLCIRKFLSYKTQCPTCCVTVTEPDLKNNRILDELVKSLNFARNHLLQFALESPAKSPASSSSKNLAVKVYTPVASRQSLKQGSRLMDNFLIREMSGSTSELLIKENKSKFSPQKEASPAAKTKETRSVEEIAPDPSEAKRPEPPSTSTLKQVTKVDCPVCGVNIPESHINKHLDSCLSREEKKESLRSSVHKRKPLPKTVYNLLSDRDLKKKLKEHGLSIQGNKQQLIKRHQEFVHMYNAQCDALHPKSAAEIVREIENIEKTRMRLEASKLNESVMVFTKDQTEKEIDEIHSKYRKKHKSEFQLLVDQARKGYKKIAGMSQKTVTITKEDESTEKLSSVCMGQEDNMTSVTNHFSQSKLDSPEELEPDREEDSSSCIDIQEVLSSSESDSCNSSSSDIIRDLLEEEEAWEASHKNDLQDTEISPRQNRRTRAAESAEIEPRNKRNRN
Expression Range	1-495aa
Protein Length	Full Length
Mol. Weight	72.2kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity.
Subcellular Location	Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Families	RAD18 family
Database References	HGNC: 18278 OMIM: 605256 KEGG: hsa:56852 STRING: 9606.ENSP00000264926 UniGene: PMID: 29306013 Rad18, independently of its ubiquitin ligase activity, promotes DNA polymerase eta SUMOylation by facilitating its interaction with its SUMO ligase PIAS1 and is required for DNA polymerase eta function at difficult to replicate loci. PMID: 27811911 MAGE-A4 depletion from MAGE-A4-expressing cancer cells destabilizes RAD18. PMID: 27377895 Data suggest that, as part of DNA repair in nucleus of embryonic stem cells, IGF1R interacts with and phosphorylates PCNA at tyrosine residues 60, 133, and 250; this is followed by mono- and polyubiquitination of PCNA by RAD18 and SHPRH. (IGF1R = insulin-like growth factor 1 receptor; PCNA = proliferating cell nuclear antigen; RAD18 = E3 ubiquitin-protein ligase RAD18; SHPRH = E3 ubiquitin-protein ligase SHPRH) PMID: 28924044 Ubiquitin ligases RNF168, RNF169, and RAD18 specifically bind histone H2A Lys13/15-ubiquitylated nucleosomes. 53BP1 chromatin recruitment may be activated by RNF168 and blocked by RNF169 and RAD18. PMID: 28506460 WRNIP1 connects PCNA monoubiquitination with ATMIN/ATM to activate ATM signalling in response to replication stress and contribute to the maintenance of genomic stability. PMID: 26549024 RAD18 polymorphisms are correlated with the side effects of platinum-chemotherapy in Chinese patients with advanced NSCLC. PMID: 27665847 REV1 can promote PCNA monoubiquitylation after UV radiation through interacting with ubiquitylated RAD18. PMID: 26795561 USP7-mediated de-ubiquitylation protects Rad18 from proteasomal degradation and is necessary for the integrity of the specialized translesion synthesis pathway PMID: 25961918 RAD18 can function as a mediator for DNA damage response signals to activate the G2/M checkpoint in order to maintain genome integrity and cell survival after IR exposure. PMID: 25675240 Significantly restored tolerance of RAD18-/- and RNF8-/- cells to camptothecin and olaparib without affecting Rad51 focus formation. PMID: 25417706 these results suggest that miR-145 can act as an RAD18 inhibitor and contribute as an important factor in reversing drug resistance after chemotherapy. PMID: 25913620 We obtained a molecular envelope for Rad18 UBZ-ELRM:linear Ub2 polyubiquitin chains by small-angle X-ray scattering and derived a structural model for the complex. PMID: 25756347 Rad18 protein ubiquitin-binding zinc fingers domain has alpha-helix and strand beta1 conformation. PMID: 25162118 Monoubiquitination has a role in controlling Rad18 function. PMID: 25023518 The Rad6/18 ubiquitin complex interacts with the Epstein-Barr virus deubiquitinating enzyme, BPLF1, and contributes to virus infectivity. PMID: 24672041 HHR6 and hRad18 can monoubiquitinate FANCD2 at lysine 561 in vitro. This activity may represent a novel stress response pathway. PMID: 24036990 Findings indicate that RAD18 may serve as a key mediator of the ionizing radiation (IR)response and may function as a potential target for circumventing IR resistance in glioblastoma multiforme (GBM). PMID: 24518219 Non-canonical CRL4A/4B(CDT2) interacts with RAD18 to modulate post replication repair and cell survival. PMID: 23555860 Rad18 plays distinct roles in protecting the genome from oxidative DNA damage in different cell cycle stages. PMID: 23295675 Rad18 is targeted to PCNA by DNA polymerase eta. PMID: 23345618 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 sites. PMID: 22742833 E2F3 controls the ubiquitination of PCNA through the transcriptional regulation of Rad18. PMID: 22391204 Ser409, located within the pol-eta binding domain of Rad18, is phosphorylated by c-jun kinase in response to dna damage, promoting the interaction between Rad18 and pol-eta. PMID: 22456510 Rad18 is involved in the regulation of melanoma cell proliferation. PMID: 22145991 The Rad6-Rad18 enzyme plays an essential role in promoting replication through DNA lesions by translesion synthesis in mammalian cells. PMID: 22547805 Hydroquinone could upregulate the expression of Rad18 in L-02 hepatic cells. PMID: 19493487 RAD18 interacts with BRCTx in a phosphorylation-dependent manner PMID: 22036607 The results demonstrate that RAD6A and RAD18 form a ternary complex, RAD6A-(RAD18)(2) and the presence of only one RAD6-binding domain in the two RAD18 subunits is sufficient for ternary complex formation and the ligase activity. PMID: 21967848 Data indicate that association of RAD18 with DSBs through ubiquitylated H2A and other ubiquitylated chromatin components allows recruitment of RAD9. PMID: 21858012 Data show that the homodimeric Rad18 RING domain can recruit two Rad6b E2 enzymes, whereas the full-length Rad18 homodimer binds only to a single Rad6b molecule. PMID: 21549715 A novel pathway of Rad18-dependent DSB repair that is dissociable from known Rad18-mediated DNA repair mechanisms based on its independence from PCNA ubiquitination and requirement for E3 ligase activity. PMID: 21478670 E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. PMID: 21422291 showed that the function of FA signaling pathway is at least partly mediated through coupling with hRad6/hRad18 signaling (HHR6 pathway) PMID: 20967207 RAD18-mediated PCNA monoubiquitination is a central hub for the mobilization of the Fanconi anemia DNA repair network pathway. PMID: 20937699 Rad18 promotes FA core complex-dependent FANCD2 ubiquitination in a manner that is secondary to PCNA mono-ubiquitination. PMID: 20675655 RAD18-dependent recruitment of SNM1A to DNA repair complexes by a ubiquitin-binding zinc finger PMID: 20385554 there is no relation between Rad18 SNP and lung cancer development. PMID: 19630985 hRad18 is a novel interacting partner of HIV-1 integrase; role for post-replication/translesion DNA repair in the retroviral integration process. PMID: 12016221 action at DNA replication forks PMID: 12856420 Together, our results suggest that MMS-induced accumulation of hRad18 protein at stalled forks involves protein phosphorylation which may be performed by S-phase checkpoint kinases. PMID: 15381075 the amount of Rad18 in the nucleus is regulated differentially by mono- and polyubiquitination PMID: 15509568 We found that the RAD18 transcript is expressed ubiquitously in various tissues and very highly in the testis in mammals. PMID: 16098139 Association of Polkappa with PCNA is regulated by Rad18-mediated PCNA ubiquitination. PMID: 16611994 Rad18 is a polypeptide associated with Poleta. The study results suggest that arrested replication forks strengthen interactions among Poleta, Rad18/Rad6 and Rev1, consistent with the requirement for effective TLS by Poleta at sites of DNA lesions. PMID: 16824193 RAD18-/- cells were defective in single-strand break repair, but functional for double-strand break repair. PMID: 17158148 Higher-eukaryotic cells separately employ PARP1 and Rad18 to suppress the toxic effects of NHEJ during the HR reaction at stalled replication forks. PMID: 17242200 WRN functions in a RAD18-dependent damage avoidance pathway. PMID: 17541157 RAD18 Arg302Gln polymorphism is associated with non-small-cell lung cancer PMID: 17624554 Single nucleotide polymorphism in the RAD18 gene is associated with colorectal cancer PMID: 17914568

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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