Fas/TNFRSF6/CD95 Antibody (LOB 3/17) Summary
| Immunogen |
Fusion protein comprising extracellular domain of human Fas linked to human Fc.
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| Specificity |
Recognizes the human CD95 cell surface antigen, a 40-50kD glycoprotein expressed by activated T and B cells, NK cells and thymocytes.
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| Isotype |
IgG1
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| Clonality |
Monoclonal
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| Host |
Mouse
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| Gene |
FAS
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| Purity |
Protein A purified
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Applications/Dilutions
| Dilutions |
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| Positive Control |
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Reactivity Notes
Reacts with Rhesus Monkey and Human.
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
|
| Buffer |
Tris (pH 8.) and NaCl
|
| Preservative |
0.09% Sodium Azide
|
| Concentration |
1 mg/ml
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| Purity |
Protein A purified
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Alternate Names for Fas/TNFRSF6/CD95 Antibody (LOB 3/17)
- Apo-1 antigen
- Apo-1
- apoptosis antigen 1
- Apoptosis-mediating surface antigen FAS
- APT1
- APT1FASTM
- CD95 antigen
- CD95
- CD95ALPS1A
- Fas (TNF receptor superfamily, member 6)
- Fas AMA
- Fas antigen
- Fas
- FAS1
- FASLG receptor
- TNFRSF6
- TNFRSF6member 6
- tumor necrosis factor receptor superfamily member 6
Background
CD95 is a member of the TNF-receptor superfamily. This receptor contains a death domain. It has been shown to play a central role in the physiological regulation of programmed cell death, and has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The interaction of this receptor with its ligand allows the formation of a death-inducing signaling complex that includes Fas-associated death domain protein, caspase 8, and caspase 10. The autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, and leads to apoptosis. CD95 has been also shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is found to be involved in transducing the proliferating signals in normal diploid fibroblast and T cells. At least eight alternatively spliced transcript variants encoding seven distinct isoforms have been described. The isoforms lacking the transmembrane domain may negatively regulate the apoptosis mediated by the full length isoform.
