Analytical Data
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Gene name
DEDD
- Application
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Alternative Names
DEDD；DEDPRO1；DEFT;Death effector domain-containing Protein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
MGSSHHHHHH SSGLVPRGSH MAGLKRRASQ VWPEEHGEQE HGLYSLHRMF DIVGTHLTHR DVRVLSFLFV DVIDDHERGL IRNGRDFLLA LERQGRCDES NFRQVLQLLR IITRHDLLPY VTLKRRRAVC PDLVDKYLEE TSIRYVTPRA LSDPEPRPPQ PSKTVPPHYP VVCCPTSGPQ MCSKRPARGR ATLGSQRKRR KSVTPDPKEK QTCDIRLRVR AEYCQHETAL QGNVFSNKQD PLERQFERFN QANTILKSRD LGSIICDIKF SELTYLDAFW RDYINGSLLE ALKGVFITDS LKQAVGHEAI KLLVNVDEED YELGRQKLLR NLMLQALP
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Molecular Weight
39 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
DEDD (Death Effector Domain-Containing) proteins are a distinct class of proteins that play crucial roles in the regulation of apoptosis and various cellular processes. The DEDD family is characterized by the presence of a death effector domain that facilitates their interaction with other proteins involved in cell death pathways. Research into DEDD proteins has gained momentum due to their implications in various diseases, including cancer and neurodegenerative disorders. These proteins can modulate apoptotic signals, influencing cell survival and death, making them potential targets for therapeutic intervention. Understanding the structural and functional characteristics of DEDD proteins is essential for elucidating their roles in cellular mechanisms. Recent advancements in molecular biology techniques have enhanced our ability to study these proteins, fostering interest in their potential as biomarkers for disease and as targets for drug development. As such, ongoing research aims to unravel the intricate networks in which DEDD proteins operate, offering insights into their contributions to health and disease, and paving the way for innovative treatments.
