Recombinant Human E3 ubiquitin-protein ligase RNF4(RNF4)

Code CSB-YP019889HU
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Source Yeast
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Code CSB-EP019889HU
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Source E.coli
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Code CSB-EP019889HU-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-BP019889HU
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Source Baculovirus
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Code CSB-MP019889HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names RNF4
Uniprot No. P78317
Alternative Names E3 ubiquitin ligase RNF4; E3 ubiquitin protein ligase RNF4; Protein SNURF; RES4 26; RING finger protein 4; Rnf4; RNF4_HUMAN; SLX5; Small nuclear ring finger protein; SNURF
Species Homo sapiens (Human)
Expression Region 1-190
Target Protein Sequence MSTRKRRGGA INSRQAQKRT REATSTPEIS LEAEPIELVE TAGDEIVDLT CESLEPVVVD LTHNDSVVIV DERRRPRRNA RRLPQDHADS CVVSSDDEEL SRDRDVYVTT HTPRNARDEG ATGLRPSGTV SCPICMDGYS EIVQNGRLIV STECGHVFCS QCLRDSLKNA NTCPTCRKKI NHKRYHPIYI
Protein Length Full length protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
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
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
Protein FAQs
Storage Condition Store at -20°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.

Target Data

Function E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation.
Gene References into Functions
  1. Study provides an insight into the role of the RNF4 to balance the role of SUMO signaling by directly targeting Ubc9 and SUMO E3 ligases. PMID: 29180619
  2. High RNF4 expression is associated with adenovirus infections. PMID: 29695423
  3. Respiratory syncytial virus induces NRF2 degradation through a PML-RNF4 pathway. PMID: 29107745
  4. Thus, although Rnf4 and Ube2w functionally interact in vitro, these genetic experiments indicate that in response to DNA damage Ube2w and Rnf4 function in distinct pathways. PMID: 27185577
  5. The E3 ligase RNF4 is required to ubiquitinate FXR in response to SUMOylation. PMID: 28201649
  6. RNF4-dependent ubiquitylation translates transient phosphorylation signal(s) into long-term protein stabilization, resulting in enhanced oncoprotein activation PMID: 27653698
  7. These findings indicate that SUMOylation of NDRG2 is necessary for its tumor suppressor function in lung adenocarcinoma and that RNF4 increases the efficiency of this process. PMID: 27072586
  8. post-translational modification of Nkx3.2 employing HDAC9-PIASy-RNF4 axis plays a crucial role in controlling chondrocyte viability and hypertrophic maturation during skeletal development in vertebrates. PMID: 27312341
  9. These findings illustrate a novel strategy for viral interference with the SUMO pathway, and identify the EBV miR-BHRF1-1 and the cellular RNF4 as regulators of the productive virus cycle. PMID: 28414785
  10. These results point to an important role of the affinity between RNF4 and its cognate RAD6B or UBCH5B in governing the multiplicity of substrate ubiquitination. PMID: 27678051
  11. the opposing activities of RNF4 and ataxin-3 consolidate robust MDC1-dependent signaling and repair ofDNA double-strand break. PMID: 28275011
  12. Combined effect of dynamic recruitment of RNF4 to KAP1 regulates the relative occupancy of 53BP1 and BRCA1 at double-strand break sites to direct DNA repair in a cell cycle-dependent manner. PMID: 26766492
  13. c-Myc is targeted to the proteasome for degradation in a SUMOylation-dependent manner, regulated by PIAS1, SENP7 and RNF4 PMID: 25895136
  14. Data show that RNF4 is a SUMO-targeted ubiquitin ligase that targets TRF2 for ubiquitination. PMID: 26450775
  15. novel insight into cross-talk between ubiquitin and SUMO and uncover USP11 and RNF4 as a balanced SUMO-targeted ubiquitin ligase/protease pair with a role in the DDR. PMID: 25969536
  16. RNF4 negatively regulates NF-kappaB signaling by down-regulating TAB2 PMID: 26299341
  17. RNF4 enhances Ube2E1 self-ubiquitination. PMID: 25960396
  18. NMR spectroscopy and biochemical characterization reveal how RNF4 manipulates the conformation of the SUMO chain, thereby facilitating optimal delivery of the distal SUMO domain for ubiquitin transfer. PMID: 24969970
  19. RecQ-like helicase BLM subcellular localization is regulated by SUMO-targeted ubiquitin ligase RNF4 in response to DNA damage, presumably to prevent illegitimate recombination events. PMID: 25588990
  20. Cells lacking RNF4 exhibited interstrand cross-linker hypersensitivity. The gene encoding RNF4 was epistatic with the other genes encoding members of the FA/BRCA pathway. PMID: 25751062
  21. RNF4 mediates ubiquitination and turnover of MeCP2 and thus derepresses transcription from DNA methylation. PMID: 25355316
  22. the ARM dynamically regulates the SIM-dependent recruitment of targets to RNF4, which could be critical to dynamically fine-tune the abundance of Ser(P)-824-SUMO-KAP1 and, potentially, other SUMOylated proteins during DNA damage response. PMID: 24907272
  23. SUMO chain-induced dimerization activates RNF4. PMID: 24656128
  24. The sequence and spacing of the SIMs (SUMO-interaction motifs) in RNF4 regulate the avidity-driven recognition of substrate proteins carrying SUMO chains of variable length. PMID: 24151981
  25. RNF4 is a SUMO-targeted ubiquitin E3 ligase of Rta. PMID: 23504328
  26. connect ubiquitin- and SUMO-dependent DSB recognition, revealing that RNF4-synthesized hybrid SUMO-ubiquitin chains are recognized by RAP80 to promote BRCA1 recruitment and DNA repair. PMID: 23211528
  27. SUMO interacting motif is dispensable for PML SUMOylation and interaction with RNF4 but is required for efficient PML ubiquitination, recruitment of proteasome components within NBs and proteasome-dependent degradation of PML in response to AsO PMID: 23028697
  28. RNF4 operates as a DSB response factor at the crossroads between the SUMO and ubiquitin systems. PMID: 22661229
  29. RNF4 is a novel DNA damage-responsive protein that plays a role in homologous recombination and integrates SUMO modification and ubiquitin signaling in the cellular response to genotoxic stress. PMID: 22661230
  30. RNF4 regulates the localization and function of the HTLV-1 oncoprotein Tax. PMID: 22106342
  31. Mechanistic studies show that RNF4 interacts with and requires the base excision repair enzymes TDG and APE1 for active demethylation. PMID: 20696907
  32. RNF4 is a negative regulator of TRPS1 activity PMID: 12885770
  33. Data show that the RING-domain-containing ubiquitin E3 ligase, RNF4 (also known as SNURF), targets poly-SUMO-modified proteins for degradation mediated by ubiquitin. PMID: 18408734
  34. sumoylation- and Sumo binding domain-dependent PML oligomerization within nuclear bodies is sufficient for RNF4-mediated PML degradation PMID: 19380586
  35. The different subtypes of malignant ovarian germ cell tumours all express ERalpha, ERbeta, and SNURF. PMID: 19524139
  36. Functional analysis of the rat homolog PMID: 12351196
  37. Functional analysis of the mouse homolog PMID: 12874792

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Subcellular Location Cytoplasm, Nucleus, Nucleus, PML body, Nucleus, nucleoplasm
Tissue Specificity Widely expressed at low levels in many tissues; highly expressed in testis.
Database Links

HGNC: 10067

OMIM: 602850

KEGG: hsa:6047

STRING: 9606.ENSP00000315212

UniGene: Hs.66394

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