TNFRSF6/Fas/CD95

TNFRSF6/Fas/CD95 is a TNF receptor family death-domain receptor that triggers apoptosis and supports immune control by killing pathogen-infected cells and obsolete or potentially dangerous lymphocytes^[1]. Mechanistically, activated Fas forms the death-inducing signaling complex (DISC) with receptor-associated proteins, linking CD95 engagement to apoptotic signal initiation^[2]. DISC recruitment of FLICE/caspase-8 connects Fas physically to proapoptotic proteases and drives downstream apoptosis execution^[3]. In disease models, dominant interfering FAS mutations impair apoptosis in human autoimmune lymphoproliferative syndrome, establishing Fas as a practical target for immune-homeostasis studies^[4]. Compared with membrane-bound Fas, alternative splicing of Fas/CD95 exon 6 produces a membrane receptor that promotes apoptosis or a soluble isoform that inhibits apoptosis^[5]. Earlier work also identified three functional soluble Fas forms generated by alternative splicing, supporting isoform-specific experimental design^[6]. For applications, agonistic anti-Fas antibody models induce fulminant liver injury, providing a controlled system to study Fas-mediated apoptosis and protective interventions^[7].

References:

[1]. Strasser A, et al. The many roles of FAS receptor signaling in the immune system. Immunity. 2009 Feb 20;30(2):180-92. [Content Brief]

[2]. Kischkel FC, et al. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J. 1995 Nov 15;14(22):5579-88. [Content Brief]

[3]. Muzio M, et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex. Cell. 1996 Jun 14;85(6):817-27. [Content Brief]

[4]. Fisher GH, et al. Dominant interfering Fas gene mutations impair apoptosis in a human autoimmune lymphoproliferative syndrome. Cell. 1995 Jun 16;81(6):935-46. [Content Brief]

[5]. Tejedor JR, et al. Genome-wide identification of Fas/CD95 alternative splicing regulators reveals links with iron homeostasis. Mol Cell. 2015 Jan 8;57(1):23-38. [Content Brief]

[6]. Cascino I, et al. Three functional soluble forms of the human apoptosis-inducing Fas molecule are produced by alternative splicing. J Immunol. 1995;154(6):2706-2713.

[7]. Costelli P, et al. Mice lacking TNFalpha receptors 1 and 2 are resistant to death and fulminant liver injury induced by agonistic anti-Fas antibody. Cell Death Differ. 2003 Sep;10(9):997-1004. [Content Brief]

TNFRSF6/Fas/CD95 Inhibitors (2)

TNFRSF6/Fas/CD95 Related Products (2):

By Type:	Selective (1)

Cat. No.	Product Name	Effect	Purity

HY-108847

Etanercept	Inhibitor	99.20%
Etanercept, a dimeric fusion protein that binds TNF, acts as a TNF inhibitor. Etanercept competitively inhibits the binding of both TNF-α and TNF-β to cell surface TNF receptors, rendering TNF biologically inactive. Etanercept shows efficacy against rheumatoid arthritis, juvenile idiopathic arthritis, and plaque psoriasis.

HY-100755

KR-33493	Inhibitor	99.94%
KR-33493 is a potent inhibitor of Fas-mediated cell death (FAF1).

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