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Recombinant human Fas / CD95 Protein, Fc Tag, 100µg  

Recombinant human Fas / CD95 Protein, Fc Tag, 100µg

Recombinant Human Fas / CD95 Protein, Gln26-Asn173, produced in human 293 cells (HEK293), Fc tag

Recombinant Human Protein, FAS, ALPS1A, APO1, APT1, CD95, FAS1, FASTM, TNFRSF-6, FasR

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312,00 €

The Fas also known as FAS receptor (FasR), apoptosis antigen 1 (APO-1 or APT), cluster of differentiation 95 (CD95) or tumor necrosis factor receptor superfamily member 6 (TNFRSF6). is a death receptor on the surface of cells that leads to programmed cell death (apoptosis). It is one of two apoptosis pathways, the other being the mitochondrial pathway.[1] FasR is located on chromosome 10 in humans and 19 in mice. Similar sequences related by evolution (orthologs) are found in most mammals. Fas forms the death-inducing signaling complex (DISC) upon ligand binding. Membrane-anchored Fas ligand trimer on the surface of an adjacent cell causes trimerization of Fas receptor. This event is also mimicked by binding of an agonistic Fas antibody, though some evidence suggests that the apoptotic signal induced by the antibody is unreliable in the study of Fas signaling. To this end, several clever ways of trimerizing the antibody for in vitro research have been employed.Upon ensuing death domain (DD) aggregation, the receptor complex is internalized via the cellular endosomal machinery. This allows the adaptor molecule FADD to bind the death domain of Fas through its own death domain.[2] Recently, Fas has also been shown to promote tumor growth, since during tumor progression, it is frequently downregulated or cells are rendered apoptosis resistant. Cancer cells in general, regardless of their Fas apoptosis sensitivity, depend on constitutive activity of Fas. This is stimulated by cancer-produced Fas ligand for optimal growth.[3]

Recombinant Human Fas /CD95 Protein, With C-Fc Tag (rhFas-Fc) Gln26-Asn173 (Accession # AAH12479.1) was produced in human 293 cells (HEK293).

Molecular Characterization
rhFas-Fc, fused with Fc fragment of human IgG1 at the C-terminus and has a calculated MW of 42.8 kDa expressed. The predicted N-terminus is Gln 26. Protein migrates as 45-55 kDa in reduced SDS-PAGE resulting from glycosylation.

Less than 1.0 EU per μg of the rhFas-Fc by the LAL method.

>95% as determined by SDS-PAGE.

Lyophilized from 0.22 μm filtered solution in 50 mM tris, 100 mM glycine, pH7.0. Normally Mannitol or Trehalose are added as protectants before lyophilization.

See Certificate of Analysis for details of reconstitution instruction and specific concentration.

Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4C-8C); After reconstitution under sterile conditions for 1 month (4C-8C) or 3 months (-20C to -70C). 

Immobilized Human Fas Ligand, His Tag (Cat. No. FAL-H5241) at 5μg/mL (100 μL/well) can bind Human Fas, Fc Tag (Cat. No. FAS-H5252) with a linear range of 1.56-12.5 ng/mL (QC tested).


(1) Wajant H, 2002, Science 296 (5573): 1635–6.
(2) Huang B, et al., 1996, Nature 384 (6610): 638–41.
(3) Chen L, et al., 2010, Nature 465 (7297): 492–6.