Analytical Data
-
Gene name
DEDD2
- Application
-
Alternative Names
DEDD2; FLAME3; PSEC0004DNA-binding death effector domain-containing protein 2; DED-containing protein FLAME-3; FADD-like anti-apoptotic molecule 3
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8WXF8
-
Expression Region
1-185aa
-
AA Sequence
MALSGSTPAPCWEEDECLDYYGMLSLHRMFEVVGGQLTECELELLAFLLDEAPGAAGGLARARSGLELLLELERRGQCDESNLRLLGQLLRVLARHDLLPHLARKRRRPVSPERYSYGTSSSSKRTEGSCRRRRQSSSSANSQQGSPPTKRQRRSRGRPSGGARRRRRGAPAAPQQQSEPAQTFL
-
Molecular Weight
47 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
DEFB111, a member of the human beta-defensin family, is an important antimicrobial peptide that plays a crucial role in the innate immune response. Discovered in various tissues, including the epithelial cells of the respiratory and gastrointestinal tracts, DEFB111 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. Its expression is often induced by infections and inflammation, highlighting its significance in host defense mechanisms. Research on DEFB111 has gained momentum due to its potential therapeutic applications, particularly in developing new antimicrobial agents and enhancing wound healing processes. Studies have demonstrated that DEFB111 can modulate immune responses and promote the recruitment of immune cells to sites of infection. Furthermore, understanding its structure-function relationships aids in designing synthetic analogs with improved efficacy and stability. Overall, DEFB111 represents a promising target for innovative treatments against multidrug-resistant pathogens and could pave the way for novel immunomodulatory therapies to bolster the body's natural defenses.











