Analytical Data
-
Gene name
Fas Ligand
- Application
-
Alternative Names
CD178; CD95L; CD95-L; FASLG; FASLG; APT1LG1; APT1-LG1; TNFSF6; Fas Antigen Ligand; TNF Superfamily Member 6; Tumor Necrosis Factor(ligand)Superfamily,Member 6
-
Species
Mouse
-
Source
HEK293
-
Tag
N-His
-
Purity
Greater than 95% as determined by reducing SDS-PAGE.
-
Uniprot
Q544E9
-
Expression Region
Pro132~Leu279
-
Molecular Weight
30kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Related Products
Protein Description
Fas ligand (FasL) is a critical member of the tumor necrosis factor (TNF) superfamily, primarily involved in the regulation of apoptosis, immune responses, and inflammation. This type II transmembrane protein binds to its receptor, Fas (CD95), triggering a signaling cascade that leads to programmed cell death in target cells. Dysregulation of the Fas/FasL pathway has been implicated in various pathological conditions, including autoimmune diseases, cancer, and viral infections. Given its pivotal role in modulating immune responses, recombinant FasL proteins have garnered significant interest in therapeutic research. Researchers are exploring engineered forms of FasL to understand its molecular mechanisms, enhance its apoptotic abilities, and evaluate its potential as a therapeutic agent in cancer immunotherapy or as a tool in the study of immune system dynamics. The development of recombinant FasL not only aids in elucidating the underlying biology of apoptosis but also opens avenues for innovative treatments that leverage apoptosis as a means to target malignant cells or modulate immune responses in various diseases.
