Analytical Data
-
Gene name
TRADD
- Application
-
Alternative Names
TNFRSF1A-associated via death domain
-
Species
Human
-
Source
E. coli
-
Tag
N- GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q15628
-
Expression Region
1-312aa
-
Molecular Weight
61.2 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
TRADD (TNF Receptor-Associated Death Domain Protein) is a critical adaptor protein involved in the signaling pathways initiated by tumor necrosis factor (TNF) receptors, playing a pivotal role in apoptosis and inflammatory responses. The study of TRADD and its recombinant protein forms has gained significant attention due to its implications in various diseases, including cancer and autoimmune disorders. TRADD acts as a bridge between activated receptors and downstream signaling cascades, facilitating the recruitment of other proteins such as RIPK1 and FADD, which are essential for the transduction of apoptotic signals. Research into TRADD’s structure, function, and interactions has revealed its potential as a therapeutic target, as dysregulation of TRADD-mediated signaling can lead to pathological outcomes. Recombinant TRADD proteins have been developed to study its specific functions, binding affinities, and to explore its role in cellular models. These studies also aim to uncover the mechanisms that regulate TRADD’s activity, which could be pivotal in designing drugs that modulate TRADD functions to treat diseases where TNF signaling is disrupted. Through various biochemical and molecular biology techniques, researchers are elucidating the complex interactions TRADD has with other proteins, providing insights into how these pathways can be manipulated for therapeutic benefits. The ongoing exploration of TRADD and its recombinant forms is not only enhancing our understanding of apoptosis and inflammation but also paving the way for novel therapeutic strategies in the management of diseases characterized by TNF receptor signaling dysregulation.
