FAS Protein (AA 26-173) (Fc Tag)
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- Target See all FAS Proteins
- FAS (TNF Receptor Superfamily, Member 6 (FAS))
- Protein Type
- Recombinant
- Biological Activity
- Active
- Protein Characteristics
- AA 26-173
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Origin
- Human
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Source
- HEK-293 Cells
- Purification tag / Conjugate
- This FAS protein is labelled with Fc Tag.
- Sequence
- AA 26-173
- Characteristics
- This protein carries a human IgG1 Fc tag at the C-terminus. The protein has a calculated MW of 42.8 kDa. The protein migrates as 45-55 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
- Purity
- >95 % as determined by SDS-PAGE.
- Sterility
- 0.22 μm filtered
- Endotoxin Level
- Less than 1.0 EU per μg by the LAL method.
- Top Product
- Discover our top product FAS Protein
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- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Buffer
- 50 mM Tris, 100 mM Glycine, pH 7.5
- Handling Advice
- Please avoid repeated freeze-thaw cycles.
- Storage
- -20 °C
- Storage Comment
- No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C-8 °C), After reconstitution under sterile conditions for 1 month (4 °C-8 °C) or 3 months (-20 °C to -70 °C).
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- Target
- FAS (TNF Receptor Superfamily, Member 6 (FAS))
- Alternative Name
- Fas (FAS Products)
- Synonyms
- ALPS1A Protein, APO-1 Protein, APT1 Protein, CD95 Protein, FAS1 Protein, FASTM Protein, TNFRSF6 Protein, AI196731 Protein, APO1 Protein, TNFR6 Protein, Tnfrsf6 Protein, lpr Protein, Fas cell surface death receptor Protein, Fas (TNF receptor superfamily member 6) Protein, FAS Protein, Fas Protein, fas Protein
- 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.
- Molecular Weight
- 42.8 kDa
- Pathways
- p53 Signaling, Apoptosis, Production of Molecular Mediator of Immune Response, Positive Regulation of Endopeptidase Activity
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