Recombinant Human FAS-associated death domain protein(FADD)

Code CSB-YP623788HU
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Source Yeast
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Code CSB-EP623788HU
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Source E.coli
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Code CSB-EP623788HU-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-BP623788HU
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Source Baculovirus
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Code CSB-MP623788HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names FADD
Uniprot No. Q13158
Alternative Names FADD; FADD protein; FADD_HUMAN; Fas (TNFRSF6) associated via death domain; Fas associated via death domain; Fas associating death domain containing protein; Fas associating protein; Fas associating protein with death domain; Fas TNFRSF6 associated via death domain; FAS-associated death domain protein; FAS-associating death domain-containing protein; GIG 3; GIG3; Growth inhibiting gene 3 protein; Growth-inhibiting gene 3 protein; H sapiens mRNA for mediator of receptor induced toxicity; Mediator of receptor induced toxicity; MGC8528; MORT 1; MORT1; Protein FADD
Species Homo sapiens (Human)
Expression Region 1-208
Target Protein Sequence MDPFLVLLHS VSSSLSSSEL TELKFLCLGR VGKRKLERVQ SGLDLFSMLL EQNDLEPGHT ELLRELLASL RRHDLLRRVD DFEAGAAAGA APGEEDLCAA FNVICDNVGK DWRRLARQLK VSDTKIDSIE DRYPRNLTER VRESLRIWKN TEKENATVAH LVGALRSCQM NLVADLVQEV QQARDLQNRS GAMSPMSWNS DASTSEAS
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.

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Target Background

Function
(From Uniprot)
Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling.
Gene References into Functions
  1. Overexpression of FADD and Caspase-8 suppresses proliferation whilst promoting the apoptosis of human GBM cells. PMID: 28618251
  2. FADD expression and its phosphorylation can be reliable biomarkers with prognostic value for T-cell lymphoblastic lymphoma stratification. PMID: 27556297
  3. FADD interference down-regulated Rheb expression and repressed mTORC1 activity in breast cancer cell lines. The autophagy was induced by FADD deficiency in MCF7 or MDA-231 cells but rescued by recovering Rheb expression. PMID: 27013580
  4. The present data suggests FADD as a putative biomarker for pathological processes associated with the course of clinical dementia. PMID: 28320441
  5. at normal levels of expression during bacterial infection, NleB1/NleB(CR) antagonizes death receptor-induced apoptosis of infected cells by modifying FADD in an irreversible manner. PMID: 28860194
  6. Using the tDED filament structure as a template, structural analyses reveal the interaction surfaces between FADD and caspase-8 and the distinct mechanisms of regulation by cFLIP and MC159 through comingling and capping, respectively. PMID: 27746017
  7. In myelodysplastic syndrome, FADD expression is regulated by SPAG6 which influences its interaction with TRAIL death receptors. PMID: 28393201
  8. High levels of FADD and caspase-8, but not caspase-3, were associated with increased incidence of coronary events in subjects from the general population. PMID: 28302628
  9. Both Fas associated via death domain gene copy number amplification and high protein expression were significantly associated with lymph node metastasis and had the shortest disease-free survival and overall survival. PMID: 27764170
  10. autoinflammation-associated H443P nlrc4 mutant is altered in interaction with SUG1 and ubiquitinated proteins, triggering constitutive caspase-8-mediated cell death dependent on FADD but independent of Ser(533) phosphorylation. PMID: 27974463
  11. this study shows that C5a signaling induces apoptosis in brain vascular endothelial cells in experimental lupus through activation of FADD PMID: 27213693
  12. Authors identify non-canonical nuclear factor-kappaB (NF-kappaB) signaling up regulated and it was directly linked with the tumor necrosis with MT2A and pFADD genes. pFADD with MT2A can inhibit the apoptosis and promote proliferation, of colorectal cancer cells. PMID: 28061540
  13. knockdown of cFLIPL and induced expression of FADD rapidly accumulate intracellular ROS accompanied by JNK1 activation to substantiate apoptosis. PMID: 27619661
  14. Data indicate that FADD mediated apoptotic cell death was directed by ubiquitination of cFLIPL and inhibition of NF-kappaB activation. PMID: 26972597
  15. Structural analysis for the roles of DR5 death domain mutations on oligomerization of DR5 death domain-FADD complex in the death-inducing signaling complex formation has been presented. PMID: 26995783
  16. A20 targets caspase-8 and FADD to protect HTLV-I-infected cells. PMID: 26437781
  17. TCGA analysis showed that ANO1 and FADD, located at 11q13, were co-expressed at transcript level and significantly associated with overall and disease-free survival PMID: 26808319
  18. Data (including data obtained in transgenic mice) suggest FADD is key in genesis of neural tube defects in pups of diabetic mice; unfolded protein response/endoplasmic reticulum stress was prevented by over-expression of human dominant negative FADD. PMID: 26419589
  19. multifaceted kinase, CK2, phosphorylates FADD and is involved in its sub-cellular localization. PMID: 26253696
  20. The gene expression analysis showed statistically significant difference between cases and healthy controls for both FADD (p<0.02) and FAS (p<0.007) genes PMID: 25129245
  21. Observed upregulation of cortical p-194 FADD and p-FADD/FADD ratio (higher pro-survival index) in major depression; could play a major role to counteract the known activation of the intrinsic (mitochondrial) apoptotic pathway in the brain PMID: 25075716
  22. FADD death effector domain and c-FLIP death effector domain structures, the binding activity of FADD DED to the c-FLIP death effector domains, and the protein-protein interactions involving the regulation of both apoptosis and necrosis. PMID: 24355299
  23. The genotype of the promoter SNP (rs10898853) of FADD was found to be significantly associated with papillary thyroid cancer in a South Korean case control study. PMID: 24434721
  24. These results indicate that FADD, as a host pro-apoptotic protein, plays important roles in regulating HIV-1 replication and production in several ways, and apoptotic pathway inhibition is able to decrease HIV-1 replication and production PMID: 24752353
  25. depletion of alphaNAC in multiple types of cancer cells induce typical apoptotic cell death. This anti-apoptotic function is mediated by the FADD/c-Jun N-terminal kinase pathway. PMID: 24901053
  26. high expression of FADD may be an independent biomarker for poor prognosis in nasopharyngeal carcinoma. PMID: 25305096
  27. Combined FADD, TMEM16A, and PPFIA1 gene expressions are associated with invasive ductal carcinoma of the breast. PMID: 24886289
  28. FADD elevation in leukocytes might be interpreted as the molecular equivalent of an elevated general inflammatory activity in relapsing remitting multiple sclerosis PMID: 24603611
  29. Antagonizing miR-128a expression sensitized Jurkat/R cells to the Fas-mediated apoptosis through derepression of FADD expression. PMID: 24316133
  30. association between FADD protein expression in advanced-stage head and neck squamous cell carcinoma and clinicopathological features and outcome PMID: 23763459
  31. Data show that calmodulin (CaM) binds to the death domain of Fas (FasDD) with an apparent dissociation constant (Kd) of ~2 muM and 2:1 CaM:FasDD stoichiometry. PMID: 23760276
  32. data show that Pin1 prevents Fas-mediated apoptosis in activated eosinophils via interactions with phospho-FADD PMID: 23606538
  33. Kashin-Beck disease patients have significant increased FADD expression in the middle layer but decreased FLIP expression in the upper layer of the cartilage. PMID: 22126763
  34. Ubiquitination and degradation of the FADD adaptor protein regulate death receptor-mediated apoptosis and necroptosis. PMID: 22864571
  35. The FADD gene amplification was not useful for the predictive marker of cancerization but is possibly related to the malignancy of oral squamous cell carcinoma. PMID: 22838074
  36. This review discusses the possible link that could exist between the adenosine-dependent regulation of FADD in the inflammatory context of rheumatoid arthritis. PMID: 22253026
  37. FADD cleavage by NK cell granzyme M enhances its self-association to facilitate procaspase-8 recruitment for auto-processing leading to caspase cascade. PMID: 21979465
  38. formation of hydrogen-bonded secondary structure in the C-terminal domain of the Fas-associated death domain PMID: 22130896
  39. DJ-1 protects against TRAIL-induced apoptosis through the regulation of death-inducing signaling complex (DISC) formation. PMID: 21785459
  40. Polo-like kinase 1 (Plk1) failed to phosphorylate the Aur-A-unphosphorylatable FADD substitution mutant S203A. PMID: 21978935
  41. an essential role of calmodulin in mediating Fas-induced FADD-independent activation of Src-ERK signaling pathways, which promote survival signaling in pancreatic cancer cells. PMID: 21613217
  42. FADD: an endogenous inhibitor of RIP3-driven regulated necrosis PMID: 21894190
  43. Our results suggest that deregulated miR-155 promotes Fas-mediated apoptosis in human intervertebral disc degeneration by targeting FADD and caspase-3 PMID: 21706480
  44. These data provide evidence that serine 194 phosphorylated Fas-associated death domain protein is involved in the proliferation of normal and neoplastic B cells and has features of a novel proliferation marker. PMID: 21315423
  45. FADD and TRIM21 together negatively regulate the late IFN-alpha pathway in response to viral infection. PMID: 21183682
  46. our data demonstrate that in response to taxol, Plk1 endows death-promoting and tumor-suppressor functions to its substrate, FADD PMID: 20890306
  47. Results suggest that the CD95-DD+CT:FADD-DD complex formed in solution is dissociated at the lower pH. PMID: 20947025
  48. findings show that the Fas-FADD death domain (DD) complex forms an asymmetric oligomeric structure composed of 5-7 Fas DD and 5 FADD DD, whose interfaces harbor associated autoimmune lymphoproliferative syndrome mutations PMID: 20935634
  49. FADD is essential at early stages of hematopoiesis; its deletion with the Mx1-cre transgene in bone marrow cells leads to impairment of peripheral lymphoid, myeloid, and erythroid cell lineages. PMID: 21115735
  50. describe here a complex clinical disorder, its genetic basis, and some of the key mechanisms underlying its pathogenesis. Our findings highlight the key role of FADD in Fas-dependent and Fas-independent signaling pathways in humans PMID: 21109225

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Involvement in disease Infections, recurrent, associated with encephalopathy, hepatic dysfunction and cardiovascular malformations (IEHDCM)
Tissue Specificity Expressed in a wide variety of tissues, except for peripheral blood mononuclear leukocytes.
Database Links

HGNC: 3573

OMIM: 602457

KEGG: hsa:8772

STRING: 9606.ENSP00000301838

UniGene: Hs.86131

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