Recombinant Human Tumor necrosis factor receptor type 1-associated DEATH domain protein (TRADD)

Code CSB-EP621879HU
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Greater than 90% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Alternative Names
9130005N23Rik; AA930854; TNFR1 associated DEATH domain protein; TNFR1-associated DEATH domain protein; TNFRSF1A associated via death domain; TNFRSF1A-associated via death domain; tradd; TRADD_HUMAN; Tumor necrosis factor receptor type 1 associated DEATH domain protein; Tumor necrosis factor receptor type 1-associated DEATH domain protein
Homo sapiens (Human)
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
Protein Length
Full Length
Tag Info
N-terminal GST-tagged
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.
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
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°C/-80°C. 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.
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.

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Target Background

Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD. Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B. The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A.
Gene References into Functions
  1. potential biological significance of TRADD mediated inflammatory response in the development of uterine leiomyoma, is reported. PMID: 28698006
  2. we found that ORF3 protein downregulates TLR3-mediated NF-kappaB signaling via TRADD and RIP1. Our findings provide a new perspective on the cellular response in HEV infection and expand our understanding of the molecular mechanisms of Hepatitis E virus (HEV) pathogenesis in innate immunity. PMID: 27270888
  3. In conclusion, for the first time, we report that TRADD, TRAF2, RIP1 and TAK1 play a role in the regulating TNF-alpha signalling in human myometrium. These findings are of significance given the central role of TNF-alpha in the processes of human labour and delivery. PMID: 28337828
  4. These data for the first time identifies miR-485-5p/TRADD axis in hydrogen sulfide protecting against TNF-alpha-induced neuronal cell apoptosis. PMID: 27562714
  5. By reducing the levels of TRADD, wild type CFTR suppresses downstream proinflammatory NFkappaB signaling. PMID: 27960153
  6. NPM-RAR binding to TRADD selectively inhibits caspase activation, while allowing activation of NFkappaB and JNK PMID: 25791120
  7. The release of extracellular vesicles was triggered by TNFA from BEAS-2b cells.TNFA-triggered extracellular vesicles contained TNFR1 and TRADD. PMID: 26475675
  8. MicroRNA-30c-2-3p negatively regulates NF-kappaB signaling and cell cycle progression through downregulation of TRADD and CCNE1 in breast cancer. PMID: 25732226
  9. domains of calmodulin mediate FADD and TRADD interaction PMID: 25643035
  10. PA induced the apoptosis of HUVECs by initiating the death pathway (TNF-R1/TRADD/caspases 8 pathway), whereas AA enhanced cell survival to protect vascular endothelial cells by activating the survival pathway (TNF-R1/RIP/NF-kappaB 50/NF-kappaB 65). PMID: 25230327
  11. Biologic assessment found that NPM-RAR expression impaired TNF-induced signaling through TRADD, blunting TNF-mediated activation of caspase-3 (CASP3) and caspase-8 (CASP8), to ultimately block apoptosis. PMID: 25033841
  12. TRADD gene expression was knocked down by an antisense oligonucleotide. PMID: 24070137
  13. structure-based mutations of TNFR-1 (P367A and P368A), TRADD (F266A), and RIP1 (M637A and R638A) disrupted formation of the death domain (DD) complex and prevented stable interactions among those DDs PMID: 24361886
  14. Data indicate that the ASK1-FoxO3a-TRADD-caspase 8 pathway is present in neural tube defects (NTDs)-affected tissues. PMID: 23982205
  15. we demonstrated that the association between DR6 and TRADD was enhanced upon DQM3 stimulation and TRADD was involved in DR6-induced signaling activation PMID: 24374337
  16. Data indicate that silencing tumor necrosis factor receptor 1 (TNFR1)-associated death domain protein (TRADD) in glioma cells results in decreased NF-kappaB activity, decreased proliferation of cells, and increased sensitivity to temozolomide. PMID: 23908590
  17. death domains in several proteins, including TRADD, FADD, RIPK1 and TNFR1, were directly inactivated by NleB, an enteropathogenic Escherichia coli (EPEC) type III secretion system effector known to inhibit host nuclear factor-kappaB (NF-kappaB) signalling PMID: 23955153
  18. rpS3 appears to be recruited to the death-inducing signaling complex (DISC) to induce apoptosis by interacting TRADD in response to extracellular stresses. PMID: 22510408
  19. NSP 5a3a induces apoptosis in Head and Neck cell line HN30 through p73-DAXX and TRAF2-TRADD. PMID: 22170762
  20. Death domain SXXE/D motifs are phosphorylated, as is required for stable TNFR1-TRADD complex formation and subsequent activation of NF-kappaB in inflamed mucosa. PMID: 21724995
  21. TRADD contains a nuclear export and import sequence that allows shuttling between the nucleus and the cytoplasm. It induces apoptosis via different mechanisms. PMID: 12045187
  22. chemotherapeutic drugs exhibited their cytotoxic effects in part by down-regulating Akt signaling following TRADD expression PMID: 12446787
  23. Diphtheria toxins induce apoptosis by activating components of the death receptor pathway in a receptor-independent manner. PMID: 12576460
  24. TRADD is involved in the p75(NTR)-mediated antiapoptotic activity of nerve growth factor in breast cancer cells PMID: 12604596
  25. TRAD binds with keratin 14 and has a role in susceptibility of keratinocytes to caspase-8-mediated apoptosis PMID: 14660619
  26. TRADD activates distinct mechanisms of apoptosis from the nucleus and the cytoplasm. PMID: 15761471
  27. TRADD employs a Pelle-like surface to interact with its binding partners, either receptor TNFR1 or adaptor FADD. PMID: 16006552
  28. PAK4 has a role in TNF-alpha induced cell survival pathyways by facilitating TRADD binding to the TNF Receptor PMID: 16227624
  29. TRADD and RIP1 compete for recruitment to the TNFR1 signaling complex and the distinct programs of cell death. PMID: 16611992
  30. These findings suggest that EMAP-II sensitises endothelial cells to apoptosis by facilitating TNF-R1 apoptotic signalling via TRADD mobilization. PMID: 17051333
  31. The expression of TRADD in peripheral blood mononuclear cells was significantly decreased in SLE patients. PMID: 17235653
  32. The structure of TRADD DD was solved by NMR. PMID: 17922260
  33. unique interaction of LMP1 with TRADD encodes the transforming phenotype of viral TRADD signaling and masks TRADD's pro-apoptotic function PMID: 18198944
  34. Mutations in the TRADD gene may contribute to the development of different hematological diseases. PMID: 18661484
  35. glomerular and tubular expression of TNF-alpha, (TNF receptor-associated death domain protein)TRADD, RIP(receptor-interacting protein) and TRAF-2 (TNF receptor-associated factor-) was significantly up-regulated in Lupus nephritis PMID: 19151112

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Subcellular Location
Nucleus. Cytoplasm. Cytoplasm, cytoskeleton.
Tissue Specificity
Found in all examined tissues.
Database Links

HGNC: 12030

OMIM: 603500

KEGG: hsa:8717

STRING: 9606.ENSP00000341268

UniGene: Hs.460996

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