Merck
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PF092

Sigma-Aldrich

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.

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

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This Item
05-20105-33814-551-M
recombinant

expressed in HEK 293 cells

recombinant

-

recombinant

-

recombinant

expressed in baculovirus infected Sf21 cells

form

lyophilized

form

-

form

-

form

-

manufacturer/tradename

Calbiochem®

manufacturer/tradename

Upstate®

manufacturer/tradename

Upstate®

manufacturer/tradename

Upstate®

storage condition

OK to freeze

storage condition

-

storage condition

-

storage condition

-

shipped in

wet ice

shipped in

dry ice

shipped in

dry ice

shipped in

-

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.

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.
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 Sigma-Aldrich Co. LLC

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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