Recombinant Human E3 ubiquitin-protein ligase UBR5 (UBR5), partial

Code CSB-YP025520HU
MSDS
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Source Yeast
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Code CSB-EP025520HU
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Source E.coli
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Code CSB-EP025520HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP025520HU
MSDS
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Source Baculovirus
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Code CSB-MP025520HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
4432411E13Rik; AW549941; C77315; D030042K14; DD5; E3 identified by differential display; E3 ubiquitin protein ligase, HECT domain containing, 1; E3 ubiquitin-protein ligase; E3 ubiquitin-protein ligase UBR5; EDD 1; EDD; EDD1; FLJ11310; HECT domain-containing 1; hHYD; HYD; Hyperplastic discs protein homolog; Hyperplastic discs, Drosophila, homolog of; KIAA0896; MGC57263; mKIAA0896; Progestin induced protein; Progestin-induced protein; Rat100; Ubiquitin protein ligase; Ubiquitin protein ligase E3 component n recognin 5; UBR5; UBR5_HUMAN
Species
Homo sapiens (Human)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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 before Lyophilization
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
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.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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 Q&A
Q:

Is this protein expressed in mammalian cells? It requires post-translation modification to be activated.

A:
Thanks for your inquiry.
Yes. This protein is expressed in mammalian cells, and we usually use the HEK293. The expressed protein is with post-translation modification. It's much closer to the natural protein.

Target Background

Function
E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Involved in maturation and/or transcriptional regulation of mRNA by activating CDK9 by polyubiquitination. May play a role in control of cell cycle progression. May have tumor suppressor function. Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response. Plays an essential role in extraembryonic development. Ubiquitinates acetylated PCK1. Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes.
Gene References into Functions
  1. UBR5 is a modulator of super-vigilant proteostasis of induced pluripotent stem cells from Huntington's disease patients PMID: 30038412
  2. UBR5 was highly expressed in colon cancer not only at mRNA level but also at protein level; UBR5 promoted the growth of colon cancer cells, and inhibited apoptosis. PMID: 29441938
  3. BMI1 and UBR5 repress the polymerase II (Pol II)-mediated transcription at damaged sites PMID: 27647897
  4. Results found that EDD was consistent with GOLPH3 expression and also promoted the EMT process and activated Wnt/beta-catenin signaling in epithelial ovarian cancer. PMID: 28332316
  5. UBR5 directly binds to the tumor suppressor esophageal cancer-related gene 4, increasing its ubiquitination to reducing the protein stability of ECRG4 to promote colorectal cancer progression. PMID: 28856538
  6. Wnt-dependent inactivation of the Groucho/TLE co-repressor by the HECT E3 ubiquitin ligase Hyd/UBR5 is a key prerequisite that enables Armadillo/beta-catenin to activate transcription. PMID: 28689657
  7. UBR5 downregulates proapoptotic MOAP-1 and suggest that UBR5 can confer cisplatin resistance in ovarian cancer. PMID: 27721409
  8. Data suggest that UBR5 down-regulates levels of TRAF3, a key component of Toll-like receptor signaling, via the miRNA pathway; p90RSK is an upstream regulator of UBR5; p90RSK phosphorylates UBR5 as required for translational repression of TRAF3 mRNA. (UBR5 = ubiquitin protein ligase E3 component n-recognin 5 protein; TRAF3 = TNF receptor-associated factor 3; p90RSK = 90 kDa ribosomal protein S6 kinase) PMID: 28559278
  9. Data show that ubiquitin protein ligase E3 component n-recognin 5 protein (UBR5) bound the tumor suppressor gastrokine 1 (GKN1) and increased its ubiquitination to reduce the protein stability of GKN1. PMID: 27590582
  10. Findings unveil UBR5 as a novel and critical regulator of tumor growth, metastasis, and immune response in triple negative breast cancer. PMID: 28330927
  11. Study highlights many functional biological role of UBR5 especially in cancer where it seems to be a key regulator of cell signaling. [review] PMID: 26464214
  12. Human herpesvirus-6 U14 induces cell cycle arrest in G2/M phase by associating with a cellular protein, EDD. PMID: 26340541
  13. Elevated metaphase RanGTP levels use Ubr5 to couple overall chromosome congression to SAC silencing. PMID: 26438829
  14. results confirm the role of the MLLE domain of UBR5 in substrate recruitment and suggest a potential role in regulating UBR5 ligase activity. PMID: 26224628
  15. these observations highlight the potential role of EDD in regulating mitotic progression and the cellular response to perturbed mitosis. PMID: 25833949
  16. Utilizing a high throughput RNAi screening approach author identified UBR5, a protein commonly amplified in breast cancer, as a novel regulator of ERalpha protein levels and transcriptional activity. PMID: 24441042
  17. the alpha4 N-terminus binding to endogenous PP2Ac and PABP, and the C-terminus to EDD, is reported. PMID: 24145130
  18. These results identify EDD as a dual regulator of cell survival and cisplatin resistance and suggest that EDD is a therapeutic target for ovarian cancer. PMID: 24379240
  19. UBR5 knockdown results in accumulation of cellular pregnane X receptor and an increase in its activity. PMID: 24438055
  20. As a molecular adaptor, Vpr enhanced the interaction between TERT and the VPRBP substrate receptor of the DYRK2-associated EDD-DDB1-VPRBP E3 ligase complex, resulting in increased ubiquitination of TERT. PMID: 23612978
  21. The recurrence and clustering of deleterious mutations implicate UBR5 mutations as a critical pathogenic event in a subgroup of mantle cell lymphoma. PMID: 23407552
  22. Data indicate that Dyrk2 phosphorylates TERT protein, which is then associated with the EDD-DDB1-VprBP E3 ligase complex for subsequent ubiquitin-mediated TERT protein degradation. PMID: 23362280
  23. Ubiquitination assays showed that the C-lobe of UBR5 is able to form a thioester-linked E3-ubiquitin complex, although it does not physically interact with UBCH4 in NMR experiments PMID: 23027739
  24. Study shows that TRIP12 and UBR5, two HECT domain ubiquitin E3 ligases, control accumulation of RNF168, a rate-limiting component of a pathway that ubiquitylates histones after DNA breakage. PMID: 22884692
  25. Increased p53 levels upon EDD depletion cause a G(1) arrest, as co-depletion of EDD and p53 completely rescues this effect on cell cycle progression. PMID: 22374670
  26. EDD1 suppresses death-receptor expression, and its expression is elevated in breast, pancreas, and lung cancer cell lines resistant to death receptor-mediated apoptosis. PMID: 21949371
  27. through binding to p53, EDD actively inhibits p53 phosphorylation by ATM and plays a role in ensuring smooth G(1)/S progression. PMID: 21383020
  28. EDD ubiquitinates beta-catenin through Lys29- or Lys11-linked ubiquitin chains, leading to enhanced stability of beta-catenin. PMID: 21118991
  29. The authors show that human EDD can interact independently with both human papillomavirus type 18 E6 and human E6AP. PMID: 21228227
  30. identify UBR5 as a novel E3 ligase that regulates transcription and define an additional function of TFIIS in the regulation of CDK9. PMID: 21127351
  31. study confirmed the presence of UBR5 mutation in exon 45 in high microsatellite instability cacarcinomas; could not identify exon 42 mutations in colorectal cancers and exon 51 mutations in breast cancers PMID: 20025491
  32. ubiquitin-protein ligase EDD interacts with importin alpha 5 through consensus basic nuclear localization signals and is localized in cell nuclei. EDD also binds progesterone receptor (PR) and potentiates progestin-mediated gene transactivation. PMID: 12011095
  33. EDD is a novel mediator in DNA damage signal transduction via CHK2 and emphasize the potential importance of EDD in cancer. PMID: 17074762
  34. EDD plays the role in the maintenance of genomic stability, emphasising the potential importance of dysregulated EDD expression and/or function in the evolution of cancer. PMID: 18073532
  35. These results identify EDD as a new independent prognostic marker for outcome in serous ovarian cancer PMID: 18349819

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Subcellular Location
Nucleus.
Tissue Specificity
Widely expressed. Most abundant in testis and expressed at high levels in brain, pituitary and kidney.
Database Links

HGNC: 16806

OMIM: 608413

KEGG: hsa:51366

STRING: 9606.ENSP00000429084

UniGene: Hs.492445

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