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- SPECIES: Human
- SOURCE SPECIES: HEK293 cells
- RECOMBINANT PROTEIN SEQUENCE: Gln 26 - Asn 173
- FUSION TAG: C-Fc Tag
- TESTED APPLICATIONS: WB
- APPLICATION NOTE: This recombinant protein can be used for WB. For research use only.
- PREDICTED MOLECULAR WEIGHT: 42.8 kDa
- BIOLOGICAL ACTIVITY: Measured by its binding ability in a functional ELISA. Immobilized Human Fas Ligand, His Tag at 5ug/mL (100 uL/well) can bind Human Fas, Fc Tag with a linear range of 1.56-12.5 ng/mL.
Properties
- PURITY: >95% as determined by SDS-PAGE.
- PHYSICAL STATE: Lyophilized
- BUFFER: 50 mM tris, 100 mM glycine, pH7.5
- STORAGE CONDITIONS: Lyophilized Protein should be stored at -20°C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20°C or -70°C. Avoid repeated freeze-thaw cycles.
Additional Info
- NCBI OFFICIAL SYMBOL: FAS
- ADDITIONAL NAMES: FAS, ALPS1A, APO1, APT1, CD95, FAS1, FASTM, TNFRSF6, FasR
- Protein Accession Number: AAH12479.1
- NCBI GENE ID NUMBER: 355
Background
- The Fas is 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. 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. 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.
- 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.
Disclaimer
- FOR RESEARCH USE ONLY
For additional information, visit ProSci's Terms & Conditions Page. - Disclaimer: Products are intended for laboratory research purposes only and should be used by qualified personnel only. They are not intended for use in humans. ProSci is not liable for damages or injuries resulting from receipt and/or use of ProSci materials. Please refer to the Material Safety Data Sheet (MSDS) for safe storage, handling, and use procedures.
Shipping Info
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