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PF092 Fas Ligand Plus, Human, Recombinant

Fas Ligand Plus, Human, Recombinant, consists of amino acids 103-281 fused to a 26-amino acid linker and FLAG®-tag at the N-terminus and expressed in HEK293 cells.

Fas Ligand Plus, Human, Recombinant : FDS (Fiches de données de sécurité), certificats d’analyse (CoA) et de qualité (CoQ), dossiers, brochures et autres documents disponibles.
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PF092
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Prix & Disponibilité

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PF092-5UG
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      Description
      OverviewRecombinant, human Fas ligand (amino acids 103-281) fused to a 26-amino acid linker and FLAG®-tag at the N-terminus and expressed in HEK293 cells. Does not require enhancer for activity. Suitable for cytotoxicity assays. M.W. 32,000 - 35,000.
      Catalogue NumberPF092
      Brand Family Calbiochem®
      References
      ReferencesAshkenazi, A., and Dixit, V.M. 1998. Science 281, 1305.
      Nagata, S., 1997 Cell 88, 355.
      Hahne, M., et al. 1996. Science 274, 1363.
      Bellgrau, D., et al. 1995. Nature 377, 630.
      Lowin, B., et al. 1994. Nature 370, 650.
      Russell, J.H., et al. 1993. Proc. Natl. Acad. Sci. USA 90, 4409.
      Product Information
      FormLyophilized
      FormulationLyophilized from PBS.
      Quality LevelMQ100
      Applications
      Application CommentsGlycosylation of recombinant human sFasL is similar or identical to natural human FasL. The molecular weight is ~32 kDa (nonglycosylated) and ~35 kDa (glycosylated) by SDS-PAGE under reducing conditions. The recombinant protein is produced in HEK293 cells. It does not require enhancer for activity.
      Biological Information
      Biological activity≥1 ng/ml kills Fas-sensitive cells
      Purity≥95% by SDS-PAGE
      Physicochemical Information
      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
      Avoid freeze/thaw Avoid freeze/thaw
      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
      Référence GTIN
      PF092-5UG 04055977207491

      Documentation

      Fas Ligand Plus, Human, Recombinant FDS

      Titre

      Fiche de données de sécurité des matériaux (FDS) 

      Fas Ligand Plus, Human, Recombinant Certificats d'analyse

      TitreNuméro de lot
      PF092

      Références bibliographiques

      Aperçu de la référence bibliographique
      Ashkenazi, A., and Dixit, V.M. 1998. Science 281, 1305.
      Nagata, S., 1997 Cell 88, 355.
      Hahne, M., et al. 1996. Science 274, 1363.
      Bellgrau, D., et al. 1995. Nature 377, 630.
      Lowin, B., et al. 1994. Nature 370, 650.
      Russell, J.H., et al. 1993. Proc. Natl. Acad. Sci. USA 90, 4409.

      Brochure

      Titre
      Caspases and other Apoptosis Related Tools Brochure
      Fiche technique

      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.

      Revision03-July-2008 JSW
      DescriptionRecombinant, human Fas ligand (amino acids 103-281) fused to a 26-amino acid linker and FLAG®-tag at the N-terminus and expressed in HEK293 cells. Glycosylation of recombinant human sFasL is similar or identical to natural human FasL. The molecular weight is ~32 kDa (nonglycosylated) and ~37-42 kDa (glycosylated) by SDS-PAGE under reducing conditions. The recombinant protein is produced in HEK293 cells. It does not require enhancer for activity. Useful for cytotoxicity assays.

      Fas Ligand (FasL/APO-1L/CD95L) is a ~37-42 kDa type II transmembrane protein belonging to the TNF family. Interaction between FasL and Fas induces apoptosis of Fas-sensitive cells. FasL is implicated in CTL-mediated-killing, activation-induced cell death, creation of immune-privileged sites and tissue homeostasis. The extracellular domain of human FasL can be cleaved off by a metalloprotease, generating soluble FasL (sFasL). Circulating sFasL can be detected in serum of patients with melanoma and certain types of lymphoma.
      BackgroundFas Ligand (FasL/APO-1L/CD95L) is a ~40 kDa type II transmembrane protein belonging to the TNF family. Interaction between FasL and Fas induces apoptosis of Fas-sensitive cells. FasL is implicated in CTL-mediated-killing, activation-induced cell death, creation of immune-privileged sites and tissue homeostasis. The extracellular domain of human FasL can be cleaved off by a metalloprotease, generating soluble FasL (sFasL). Circulating sFasL can be detected in serum of patients with melanoma and certain types of lymphoma.
      FormLyophilized
      FormulationLyophilized from PBS.
      Purity≥95% by SDS-PAGE
      Biological activity≥1 ng/ml kills Fas-sensitive cells
      SolubilityReconstitute in 50 µl PBS to yield a final stock concentration of 100 µg/ml. Further dilute in culture medium with 5% FCS immediately prior to use.
      CommentsGlycosylation of recombinant human sFasL is similar or identical to natural human FasL. The molecular weight is ~32 kDa (nonglycosylated) and ~35 kDa (glycosylated) by SDS-PAGE under reducing conditions. The recombinant protein is produced in HEK293 cells. It does not require enhancer for activity.
      Storage Avoid freeze/thaw
      -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
      ReferencesAshkenazi, A., and Dixit, V.M. 1998. Science 281, 1305.
      Nagata, S., 1997 Cell 88, 355.
      Hahne, M., et al. 1996. Science 274, 1363.
      Bellgrau, D., et al. 1995. Nature 377, 630.
      Lowin, B., et al. 1994. Nature 370, 650.
      Russell, J.H., et al. 1993. Proc. Natl. Acad. Sci. USA 90, 4409.