Analytical Data
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Gene name
Fas/CD95
- Application
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Alternative Names
Fas cell surface death receptor
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Species
Cynomolgus
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Source
HEK293
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Tag
C-hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
F6V1W6
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Expression Region
M1-N173
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Protein Length
Partial
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Molecular Weight
47-57 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
Fas/CD95, a member of the tumor necrosis factor (TNF) receptor superfamily, plays a critical role in regulating apoptosis, immune response, and cellular homeostasis. The Fas receptor is primarily expressed on the surface of various immune cells and is known to mediate programmed cell death upon binding to its ligand, Fas ligand (FasL). Dysregulation of the Fas/FasL pathway has been implicated in a variety of pathological conditions, including autoimmune diseases, cancer, and viral infections. In particular, tumors may exploit this pathway to evade immune detection by expressing FasL, leading to the apoptosis of effector T cells. Consequently, understanding the structural and functional aspects of Fas/CD95 and its interactions can provide insight into its role in these diseases. Research involving recombinant Fas/CD95 proteins has been pivotal in elucidating the mechanistic pathways underlying its signaling. For instance, studies have investigated the receptor's engagement with its ligand and the subsequent activation of apoptotic cascades, as well as the potential for therapeutic interventions that can modulate this pathway. Investigating the recombinant forms of Fas/CD95 not only broadens our comprehension of its biological functions but also holds potential for developing novel strategies to manipulate apoptotic signaling in various clinical settings. Therefore, the study of Fas/CD95 recombinant proteins is of significant importance in the field of immunology and cancer research, as it opens avenues for the development of targeted therapies that can enhance the immune response against tumors while restoring the balance of apoptosis in autoimmune disorders.
