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SRP3036

Sigma-Aldrich

Fas Ligand human

recombinant, expressed in CHO cells, ≥95% (SDS-PAGE), ≥95% (HPLC), suitable for cell culture

Synonym(s):

APTL, Apo I Ligand, CD95L, TNFSF6, soluble Fas Ligand (sFasL)

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in CHO cells

Assay

≥95% (HPLC)
≥95% (SDS-PAGE)

form

lyophilized

potency

≤10.0 ng/mL

mol wt

17.9 kDa

packaging

pkg of 10 μg

technique(s)

cell culture | mammalian: suitable

impurities

<0.1 EU/μg endotoxin, tested

color

white to off-white

suitability

suitable for molecular biology

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... FASLG(356)

General description

Fas Ligand (FasL) is a member of the TNF (tumor necrosis factor) superfamily that is expressed on the cell surface of activated T cells. It can be present as soluble form in the circulation or membrane bound form in cells. Recombinant human soluble Fas Ligand is a 17.9kDa protein comprising the TNF homologous region of FasL and contains an 8 residue N-terminal His-Tag. Both human and murine sFasL are fully active on human and murine cells.

Application

Fas ligand human has been used to induce apoptosis in T-cell lymphoma-derived HuT78 cells and jurkat cells.

Biochem/physiol Actions

Binding of Fas Ligand (FasL) to Fas receptor triggers apoptosis in Fas-bearing cells. FasL has the ability to kill T cells and activated B cells which leads to down-regulation of the immune response. The mechanism of Fas induced apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD (Fas-Associated protein with death domain) followed by processing of the pro-enzyme to active forms. These active caspases then cleave various cellular substrates leading to the eventual cell death. FasL is also involved in AGE (advanced glycation end-product)-mediated apoptosis in human retinal ARPE-19 cells, suggesting its role in diabetic retinopathy. Changes in the activity of FasL suppresses normal apoptosis, leading to abnormal survival and growth of tumor cells. Mutations in the FasL gene causes autoimmune lymphoproliferative syndrome.

Sequence

HHHHHHHHPS PPPEKKELRK VAHLTGKSNS RSMPLEWEDT YGIVLLSGVK YKKGGLVINE TGLYFVYSKV YFRGQSCNNL PLSHKVYMRN SKYPQDLVMM EGKMMSYCTT GQMWARSSYL GAVFNLTSAD HLYVNVSELS LVNFEESQTF FGLYKL

Physical form

Lyophilized with no additives.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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The molecular architecture of the TNF superfamily.
Bodmer JL, et al.
Trends in Biochemical Sciences, 27, 19-26 (2002)
Fas ligand mediates activation-induced cell death in human T lymphocytes.
Alderson MR, et al.
The Journal of Experimental Medicine, 71-77 (1995)
The metalloproteinase matrilysin proteolytically generates active soluble Fas ligand and potentiates epithelial cell apoptosis.
Powell WC, et al.
Current Biology, 9, 1441-1447 (1999)
Enhanced expression of Fas and FasL modulates apoptosis in the lungs of severe P. falciparum malaria patients with pulmonary edema.
Punsawad C, et al.
International Journal of Clinical and Experimental Pathology, 8, 10002-10013 (2015)
Karthik M Kodigepalli et al.
Cell cycle (Georgetown, Tex.), 16(2), 179-188 (2016-12-09)
Sterile α motif and HD domain-containing protein 1 (SAMHD1) is a mammalian dNTP hydrolase (dNTPase) that regulates intracellular dNTP balance. We have previously reported that SAMHD1 mRNA and protein levels are significantly downregulated in CD4

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