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.
Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización
About This Item
Productos recomendados
recombinant
expressed in HEK 293 cells
Quality Level
assay
≥95% (SDS-PAGE)
form
lyophilized
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
avoid repeated freeze/thaw cycles
shipped in
wet ice
storage temp.
−20°C
General description
Recombinant, 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.
Recombinant, 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.
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.
Biochem/physiol Actions
≥1 ng/ml kills Fas-sensitive cells
Warning
Toxicity: Standard Handling (A)
Physical form
Lyophilized from PBS.
Reconstitution
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Reconstitute 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.
Other Notes
Ashkenazi, A., and Dixit, V.M. 1998. Science281, 1305.
Nagata, S., 1997 Cell88, 355.
Hahne, M., et al. 1996. Science274, 1363.
Bellgrau, D., et al. 1995. Nature377, 630.
Lowin, B., et al. 1994. Nature370, 650.
Russell, J.H., et al. 1993. Proc. Natl. Acad. Sci. USA90, 4409.
Nagata, S., 1997 Cell88, 355.
Hahne, M., et al. 1996. Science274, 1363.
Bellgrau, D., et al. 1995. Nature377, 630.
Lowin, B., et al. 1994. Nature370, 650.
Russell, J.H., et al. 1993. Proc. Natl. Acad. Sci. USA90, 4409.
Glycosylation 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.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
¿Ya tiene este producto?
Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.
Póngase en contacto con el Servicio técnico