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PF033 Fas Ligand, Human, Recombinant

Fas Ligand, Human, Recombinant, consists of amino acids 103-281 fused at the N-terminus to a tag-linker peptide. Binds to human, rat, and mouse Fas.

Fas Ligand, Human, Recombinant MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: CD95L, CD178

PF033
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Overview

Replacement Information

Products

Catalogue NumberPackaging Qty/Pack
PF033-10UG Plastic ampoule 10 μg
Description
OverviewRecombinant, human, Fas ligand consisting of amino acids 103-281 fused at the N-terminus to a tag-linker peptide. Binds to human, rat, and mouse Fas. The recombinant human soluble Fas ligand recognizes the Fas receptor in human, rat and mouse. Extracellular domain of human FasL, 103 - 281 fused at the N-terminus to a tag linker peptide.
Catalogue NumberPF033
Brand Family Calbiochem®
SynonymsCD95L, CD178
References
ReferencesNoguchi, K. et al. 1996. Oncogene 13, 39.
Golstein, P. et al. 1995. Cell 81, 185.
Katsikis, P. et al. 1995. J. Exp. Med. 181, 2029.
Nagata, S. et al. 1995. Science 267, 1449.
Thompson, C., 1995. Science 267, 1456.
Watanabe-Fukunaga, R. et al. 1992. Nature 356, 314.
Product Information
ActivityED50:50 ng/ml (A20 cells)
FormLyophilized
FormulationLyophilized from PBS.
PreservativeNone
Quality LevelMQ100
Applications
Application CommentsThe soluble Fas ligand kills APO-1/Fas-sensitive cells at a concentration of >50 ng/ml. For example, cell death results when 5 x 105 murine A20 B lymphoma cells are incubated with 50-500 ng/ml of the recombinant human soluble APO1/FasL (aa 103-281) for 16 h at 37°C.
Biological Information
Purity≥95% by SDS-PAGE
Species Reactivity
  • Human
  • Mouse
  • Rat
Concentration Label Please refer to vial label for lot-specific concentration
Physicochemical Information
ContaminantsEndotoxin: <0.1 EU/µg purified protein
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Dry Ice Only
Toxicity Standard Handling
Storage -20°C
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalogue Number GTIN
PF033-10UG 04055977207989

Documentation

Fas Ligand, Human, Recombinant SDS

Title

Safety Data Sheet (SDS) 

Fas Ligand, Human, Recombinant Certificates of Analysis

TitleLot Number
PF033

References

Reference overview
Noguchi, K. et al. 1996. Oncogene 13, 39.
Golstein, P. et al. 1995. Cell 81, 185.
Katsikis, P. et al. 1995. J. Exp. Med. 181, 2029.
Nagata, S. et al. 1995. Science 267, 1449.
Thompson, C., 1995. Science 267, 1456.
Watanabe-Fukunaga, R. et al. 1992. Nature 356, 314.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision16-September-2008 RFH
SynonymsCD95L, CD178
DescriptionRecombinant, human, Fas ligand consisting of amino acids 103-281 fused at the N-terminus to a tag-linker peptide. Binds to human, mouse, and rat Fas. The recombinant protein is produced in HEK293 cells. Useful for cytotoxicity assays.

Fas/APO1/CD95 (37-42 kDa), a member of the Tumor Necrosis Factor/Nerve Growth Factor (TNF/NGF) receptor family, is an apoptosis-signaling surface receptor known to trigger apoptotic cell death. Homology exists between the Fas and TNF receptors including a region called the "death domain" which is required to propagate the apoptotic signal. The signal activates a family of cysteine proteases, or caspases, which systematically lead to cell destruction. Genetic defects in the Fas system have been shown to lead to autoimmune disorders while increased activity or deregulation contributes to the pathology of diseases such as AIDS.
BackgroundFas/APO1/CD95 (36 kDa), a member of the Tumor Necrosis Factor/Nerve Growth Factor (TNF/NGF) receptor family, is an apoptosis-signaling surface receptor known to trigger apoptotic cell death. Homology exists between the Fas and TNF receptors including a region called the "death domain" which is required to propagate the apoptotic signal. The signal activates a family of cysteine proteases, or caspases, which systematically lead to cell destruction. Genetic defects in the Fas system have been shown to lead to autoimmune disorders while increased activity or deregulation contributes to the pathology of diseases such as AIDS.
Specieshuman, mouse, rat
FormLyophilized
FormulationLyophilized from PBS.
Concentration Label Please refer to vial label for lot-specific concentration
Recommended reaction conditionsSoluble Fas ligand kills APO-1/Fas-sensitive cells at a concentration of >50 ng/ml. For example, cell death results when 5 x 105 murine A20 B lymphoma cells are incubated with 50-500 ng/ml recombinant human soluble APO1/FasL for 16 h at 37°C.
Purity≥95% by SDS-PAGE
ContaminantsEndotoxin: <0.1 EU/µg purified protein
ActivityED50:50 ng/ml (A20 cells)
SolubilityReconstitute in 50 μl H₂O to yield a final stock concentration of 100 µg/ml. Further dilute in culture medium containing 5% FCS immediately prior to use.
PreservativeNone
CommentsThe soluble Fas ligand kills APO-1/Fas-sensitive cells at a concentration of >50 ng/ml. For example, cell death results when 5 x 105 murine A20 B lymphoma cells are incubated with 50-500 ng/ml of the recombinant human soluble APO1/FasL (aa 103-281) for 16 h at 37°C.
Storage -20°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Toxicity Standard Handling
ReferencesNoguchi, K. et al. 1996. Oncogene 13, 39.
Golstein, P. et al. 1995. Cell 81, 185.
Katsikis, P. et al. 1995. J. Exp. Med. 181, 2029.
Nagata, S. et al. 1995. Science 267, 1449.
Thompson, C., 1995. Science 267, 1456.
Watanabe-Fukunaga, R. et al. 1992. Nature 356, 314.