Analytical Data
-
Gene name
FASL
- Application
-
Alternative Names
Apoptosis antigen ligand ; APTLCD95 ligand ; CD95-LFas antigen ligand ; Fas ligand ; FasL; CD178
-
Species
Human
-
Source
E. coli
-
Tag
N-6*His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P48023
-
Expression Region
Q103-L281
-
Protein Length
Extracellular Domain
-
Molecular Weight
26 kDa
-
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.
Quality inspection process
Related Products
Protein Description
FASL (Fas Ligand) is a crucial member of the tumor necrosis factor (TNF) superfamily, primarily known for its role in regulating apoptosis through its interaction with the Fas receptor (FasR). This pathway plays a significant role in various physiological processes, including immune response, tissue homeostasis, and the maintenance of cellular integrity. Dysregulation of FASL signaling has been implicated in numerous diseases, particularly in cancer, where tumor cells exploit this pathway to evade immune detection. Given its importance, researchers have focused on characterizing FASL as a recombinant protein to better understand its structure-function relationships and therapeutic potential. The production of recombinant FASL allows for detailed studies on its binding affinities, signaling mechanisms, and potential as a therapeutic agent in cancer immunotherapy. Additionally, recombinant FASL can be used to investigate its role in diseases where immune regulation is compromised, such as autoimmune disorders and graft-versus-host disease. With advancements in molecular techniques and protein engineering, the study of recombinant FASL not only enhances our understanding of apoptosis and immune regulation but also opens avenues for novel therapeutic interventions targeting FASL signaling pathways in various diseases.
