Analytical Data
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Gene name
DEDD
- Application
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Alternative Names
DEDPro1 Death effector domain-containing testicular molecule FLDED-1
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75618
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Expression Region
1-318aa
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Molecular Weight
63.8 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
The study of DEDD (Death Effector Domain-containing protein) recombinant proteins has gained significant attention in the field of molecular biology and immunology due to their critical role in apoptosis and immune response regulation. DEDD proteins are characterized by the presence of the death effector domain, which allows them to interact with various apoptotic and inflammatory signaling pathways. Research has shown that DEDD proteins are involved in the control of programmed cell death, influencing cellular responses to stress and infection. With advances in recombinant DNA technology, scientists are now able to produce DEDD proteins in vitro, enabling detailed studies of their structure, function, and interactions with other cellular components. This research has potential implications for understanding the mechanisms of diseases such as cancer, where dysregulation of apoptosis is a hallmark. Furthermore, by investigating the role of DEDD proteins in immune responses, researchers hope to identify novel therapeutic targets for autoimmune diseases and other conditions characterized by immune system dysregulation. The continued exploration of DEDD recombinant proteins not only enhances our understanding of fundamental biological processes but also paves the way for innovative treatments in the clinical setting.
