FADD antibody - C-terminal region (ARP30294_P050)
- Known as:
- FADD (anti-) - C-terminal region (ARP30294_P050)
- Catalog number:
- arp30294_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- FADD antibody - C-terminal region (ARP30294_P050)
Related genes to: FADD antibody - C-terminal region (ARP30294_P050)
- Gene:
- FADD NIH gene
- Name:
- Fas associated via death domain
- Previous symbol:
- -
- Synonyms:
- MORT1, GIG3
- Chromosome:
- 11q13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-07
- Date modifiied:
- 2019-04-23
Related products to: FADD antibody - C-terminal region (ARP30294_P050)
Related articles to: FADD antibody - C-terminal region (ARP30294_P050)
- H5N6 highly pathogenic avian influenza virus (HPAIV) poses a serious threat to both poultry and public health due to its ability to cross species barriers. Although interferon-stimulated genes (ISGs) are key components of the host's antiviral defense, a systematic identification and functional characterization of duck ISGs has not yet been conducted. In this study, we identified 815 potential duck ISGs induced by type II interferon (IFN-γ) in duck embryo fibroblasts (DEFs). The majority of these type II ISGs were enriched in immune-related pathways, including "cytokine-cytokine receptor interaction" and "influenza A". Functional validation using siRNA-mediated knockdown demonstrated that six ISGs, including duIFI35, promote H5N6 AIV replication when silenced. Through TUNEL assay, flow cytometry, and apoptotic pathway analysis, Our analysis revealed that H5N6 AIV infection markedly upregulates apoptotic genes such as Fas, FADD, caspase-8, BAK, cytochrome c, APAF1, caspase-9, and caspase-3 (P < 0.05), thereby promoting apoptosis in DEFs. In investigating the antiviral mechanism of duIFI35, it was found that overexpression of duIFI35 further enhanced H5N6-induced apoptosis, as evidenced by increased transcription of these apoptotic genes, whereas duIFI35 knockdown had the opposite effect. Importantly, the antiviral effect of duIFI35 was significantly diminished upon treatment with the caspase inhibitor Z-VAD-FMK (20 μM) (P < 0.05), indicating that its antiviral activity is mediated through apoptosis induction. Collectively, this study provides the first systematic identification of type II ISGs in ducks and reveals duIFI35-mediated apoptosis as a critical antiviral mechanism, offering foundational insights into ISG-driven innate immunity against AIV in waterfowl. - Source: PubMed
Publication date: 2026/04/16
Zhang TaoYang NaMa LuluXu FengxiangLin XiaobingHuang JiangwuGao FeiLiao MingFeng MinDai Manman - CD95/Fas belongs to the tumor necrosis factor (TNF) receptor superfamily and plays a pivotal role in immune homeostasis. Its ligand, CD95L (FasL or CD178) belongs to the TNF superfamily. CD95 contains three cysteine-rich domains (CRDs) in its extracellular (EC) region numbered 1-3 from the N-terminal region to the plasma membrane. While CRD2 and CRD3 interact with CD95L, CRD1 has been designed the pre-ligand assembly domain (PLAD) since it promotes the receptor self-aggregation in a ligand-independent manner. Upon CD95L binding, CD95 recruits Fas-associated death domain (FADD) at the level of the CD95 death domain (DD). FADD in turn aggregates caspase-8 to form the "death-inducing signalling complex" (DISC). Herein, we describe a method, called protein-fragment complementation assay (PCA) to identify PPIs and use it to validate interaction of CD95 with itself and with FADD. PCA is performed with the reporter enzyme Renilla reniformis luciferase (Rluc). RLuc has been divided in two inactive fragments, fused to different proteins of interest (POIs). If the two POIs interact, they can bring closer the two unfolded RLuc fragments fostering their folding and the quantification of luciferase activity. - Source: PubMed
Publication date: 2026/02/06
Msalbi DhouhaLebrault EdenLegembre Patrick - Receptor-interacting protein kinase 3 (RIPK3) has emerged as a central player in necroptosis and apoptosis activation in specific scenarios, concurrently modulating inflammatory responses. Here, we reveal that direct activation of RIPK3 concomitantly triggers mixed lineage kinase domain-like (MLKL) phosphorylation, caspase activation, and gasdermin cleavage within individual cells, inducing PANoptotic cell death. This process is orchestrated by the formation of RIPK3-MLKL-RIPK1-FADD-Caspase-8 complexes on progressively polymerized RIPK3 homo-aggregates, achieved through sequential recruitment dictated by the differential affinities of MLKL and Receptor-interacting protein kinase 1 (RIPK1) for distinct oligomeric states of RIPK3. In this process, MLKL- and GSDMD-mediated membrane rupture is respectively inhibited by Caspase-3-dependent cleavage of RIPK3 and GSDMD cleavage, while the pro-necrotic kinase activity of RIPK3 impedes RIPK1 recruitment and attenuates caspase activation. Cross-regulation between pathways results in unique cellular morphology, altered damage-associated molecular patterns (DAMPs) release profiles and distinct chemokine secretion paradigms that differ fundamentally from classical necroptosis, apoptosis and pyroptosis. This work highlights a common mechanism unveiling RIPK3 as a multimolecular platform to modulate and integrate different programmed cell death (PCD) pathways, thus providing a framework for targeting inflammatory cell death in disease. - Source: PubMed
Publication date: 2026/04/04
Yang YuWang YueWang YangWu ErpengChen HaoSun LimingZhang ChiCao ShuhuiLi JingwenQiang HuipingZhang LinchengLou YuqingQiao RongZhou ShenaoZhou YanZhong RunboZhong Hua - STING is an evolutionarily conserved key regulator of innate immunity. In the model organism Drosophila melanogaster, STING activates the NF-κB-like transcription factor Relish, initially characterized for its role in the antibacterial IMD pathway. The versatile FADD/Caspase-8 axis is widely used in various immune signaling pathways throughout the animal kingdom, including the IMD pathway. Here, we show that it functions downstream of STING in Drosophila to mediate Relish activation by the Caspase-8 homolog DREDD. We present a detailed structural model illustrating how the adapter protein FADD interacts with two separate STING dimers in the activated oligomerized form of STING, thus providing a molecular explanation for the activation-dependent recruitment of FADD. We further show that FADD interacts with IMD in a structurally distinct but functionally related manner, highlighting how the STING and IMD pathways differentially utilize the adapter protein FADD. Our results illustrate how an ancestral module is incorporated into different innate immune pathways, providing insights into the evolution of host-pathogen interactions. - Source: PubMed
Publication date: 2026/03/28
Winther Kasper GrønbjergSchneider JulietteHaas GabrielleChristensen Anna HvarregaardGoyal ShreyaLuo WeishengWei ZimingLiu JiyongKjøge KatarzynaEnghild Jan JMeignin CarineSilverman NealCai HuaImler Jean-LucHartmann Rune - - Source: PubMed
Balachandran SiddharthThomas EmmanuelBarber Glen N