Analytical Data
-
Gene name
DEFb2
- Application
-
Alternative Names
DEFb2;DEFB102;DEFB2;DEFB4;Defensin beta 4A
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O15263
-
Expression Region
24-64aa
-
AA Sequence
GIGDPVTCLK SGAICHPVFC PRRYKQIGTC GLPGTKCCKK P
-
Molecular Weight
4.3 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
DEFb2 is a member of the β-defensin family, which plays a crucial role in the innate immune response of various species, including humans. These small cationic peptides are primarily produced by epithelial cells and possess antimicrobial properties, making them vital for the first line of defense against pathogens. Recent studies have indicated that DEFb2 exhibits not only direct antimicrobial activity but also immunomodulatory effects, influencing the activity of immune cells and participating in wound healing processes. Research on DEFb2 has gained attention due to its potential therapeutic applications, especially in the context of antibiotic resistance and chronic inflammatory diseases. The ability to generate recombinant DEFb2 protein allows for in-depth studies of its functional mechanisms and paves the way for the development of novel antimicrobial agents or immune modulators. Investigating the structural attributes and biological activities of DEFb2 is essential for understanding its role in immunity and for harnessing its potential in clinical settings.











