Analytical Data
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Gene name
FADD
- Application
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Alternative Names
MORT1
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Species
Human
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Source
E. coli
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Tag
His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13158
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Expression Region
M1-S208
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Protein Length
Full Length
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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
FADD (Fas-associated protein with death domain) is a critical adaptor protein involved in the extrinsic apoptosis signaling pathway, which plays a pivotal role in regulating programmed cell death. Dysregulation of FADD and its associated pathways has been implicated in various diseases, especially in cancer progression, where resistance to apoptosis contributes to tumor growth and metastasis. To better understand FADD's functions and interactions, researchers have focused on generating recombinant FADD proteins using various expression systems. This allows for the study of its structural properties, signaling mechanisms, and interactions with other proteins, such as death receptors and caspases, crucial for apoptosis. Advances in recombinant protein technology have enabled the production of FADD in adequate quantities for functional assays, structural biology studies, and potential therapeutic applications. Furthermore, investigating FADD's role in distinct cellular contexts and its post-translational modifications can provide insights into how apoptotic pathways are regulated and how they can be manipulated for therapeutic benefits in conditions like cancer. Thus, the study of recombinant FADD proteins holds significant promise for uncovering new strategies to selectively induce apoptosis in tumor cells and improve cancer treatment outcomes.
