Recombinant Human FADD Protein

Name: Recombinant Human FADD Protein
Brand: Beta LifeScience
SKU: BL-1339SG
Availability: InStock

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

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Product Overview

Tag	His
Host Species	Human
Accession	NM_003824
Synonym	GIG3, MORT1, MGC8528
Background	FADD or Fas-Associated protein with Death Domain is an adaptor molecule that mediates death signaling by the Fas-receptor, tumor necrosis factor receptor and TRAIL-receptor. FADD binds to these receptors via the C-terminus Death Domain which then unmasks the N-terminal effector domain of FADD thereby allowing it to recruit caspase-8 and activate the cysteine protease cascade leading to apoptosis (1). Cells lacking FADD are defective in intracellular double-stranded RNA (dsRNA)-activated gene expression, including production of type I (alpha/beta) interferons and are thus very susceptible to viral infection (2).
Description	Recombinant full-length human FADD was produced in E. coli system, fused with a His tag at N-terminus.
Source	E.coli
AA Sequence	Full Length
Molecular Weight	~27 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human FADD Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function

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.

Database References

HGNC: 3573

OMIM: 602457

KEGG: hsa:8772

STRING: 9606.ENSP00000301838

UniGene: PMID: 28618251

FADD expression and its phosphorylation can be reliable biomarkers with prognostic value for T-cell lymphoblastic lymphoma stratification. PMID: 27556297

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

The present data suggests FADD as a putative biomarker for pathological processes associated with the course of clinical dementia. PMID: 28320441

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

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

In myelodysplastic syndrome, FADD expression is regulated by SPAG6 which influences its interaction with TRAIL death receptors. PMID: 28393201

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

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

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

this study shows that C5a signaling induces apoptosis in brain vascular endothelial cells in experimental lupus through activation of FADD PMID: 27213693

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

knockdown of cFLIPL and induced expression of FADD rapidly accumulate intracellular ROS accompanied by JNK1 activation to substantiate apoptosis. PMID: 27619661

Data indicate that FADD mediated apoptotic cell death was directed by ubiquitination of cFLIPL and inhibition of NF-kappaB activation. PMID: 26972597

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

A20 targets caspase-8 and FADD to protect HTLV-I-infected cells. PMID: 26437781

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

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

multifaceted kinase, CK2, phosphorylates FADD and is involved in its sub-cellular localization. PMID: 26253696

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

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

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

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

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

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

high expression of FADD may be an independent biomarker for poor prognosis in nasopharyngeal carcinoma. PMID: 25305096

Combined FADD, TMEM16A, and PPFIA1 gene expressions are associated with invasive ductal carcinoma of the breast. PMID: 24886289

FADD elevation in leukocytes might be interpreted as the molecular equivalent of an elevated general inflammatory activity in relapsing remitting multiple sclerosis PMID: 24603611

Antagonizing miR-128a expression sensitized Jurkat/R cells to the Fas-mediated apoptosis through derepression of FADD expression. PMID: 24316133

association between FADD protein expression in advanced-stage head and neck squamous cell carcinoma and clinicopathological features and outcome PMID: 23763459

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

data show that Pin1 prevents Fas-mediated apoptosis in activated eosinophils via interactions with phospho-FADD PMID: 23606538

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

Ubiquitination and degradation of the FADD adaptor protein regulate death receptor-mediated apoptosis and necroptosis. PMID: 22864571

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

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

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

formation of hydrogen-bonded secondary structure in the C-terminal domain of the Fas-associated death domain PMID: 22130896

DJ-1 protects against TRAIL-induced apoptosis through the regulation of death-inducing signaling complex (DISC) formation. PMID: 21785459

Polo-like kinase 1 (Plk1) failed to phosphorylate the Aur-A-unphosphorylatable FADD substitution mutant S203A. PMID: 21978935

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

FADD: an endogenous inhibitor of RIP3-driven regulated necrosis PMID: 21894190

Our results suggest that deregulated miR-155 promotes Fas-mediated apoptosis in human intervertebral disc degeneration by targeting FADD and caspase-3 PMID: 21706480

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

FADD and TRIM21 together negatively regulate the late IFN-alpha pathway in response to viral infection. PMID: 21183682

our data demonstrate that in response to taxol, Plk1 endows death-promoting and tumor-suppressor functions to its substrate, FADD PMID: 20890306

Results suggest that the CD95-DD+CT:FADD-DD complex formed in solution is dissociated at the lower pH. PMID: 20947025

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

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

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

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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Recombinant Human FADD Protein

Recombinant Human FADD Protein

Product Overview

Target Details

FAQs