Analytical Data
-
Gene name
DEFb124
- Application
-
Alternative Names
DEFb124；DEFB24；Beta-defensin 124
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8NES8
-
Expression Region
23-71aa
-
AA Sequence
EFKRCWKGQGACQTYCTRQETYMHLCPDASLCCLSYALKPPPVPKHEYE
-
Molecular Weight
7.7 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
DEFb124 is a member of the defensin family of antimicrobial peptides, which play a crucial role in the innate immune response of various organisms, including plants and animals. This particular protein is derived from the skin of amphibians and has garnered attention due to its potent antimicrobial properties against a wide spectrum of pathogens, including bacteria, fungi, and viruses. The study of DEFb124 is particularly relevant in the context of increasing antibiotic resistance, as researchers seek alternative treatments that can effectively combat resistant strains of pathogens. Recent investigations have focused on elucidating the structure-function relationship of DEFb124, enabling scientists to understand how its unique folding and charge distribution contribute to its antimicrobial efficacy. Furthermore, its potential applications in medical and agricultural fields have been explored, including the development of new antiseptics or biopesticides. The ongoing research into DEFb124 not only sheds light on the evolutionary significance of antimicrobial peptides but also paves the way for innovative solutions in the fight against infectious diseases.
