Analytical Data
-
Gene name
DEFB128
- Application
-
Alternative Names
Beta-defensin 28 Defensin, beta 128
-
Species
Human
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q7Z7B8
-
Expression Region
19-93aa
-
Molecular Weight
16.0 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
Defensin Beta 128 (DEFB128) is a member of the beta defensin family, known for its role in the innate immune response. These small cationic peptides are primarily expressed in various epithelial tissues, including the skin, respiratory tract, and reproductive organs, where they function as antimicrobial agents against a broad spectrum of pathogens, including bacteria, viruses, and fungi. The interest in DEFB128 has surged due to its potential therapeutic applications, particularly in combating antibiotic-resistant infections and as a candidate for enhancing wound healing. Research has indicated that DEFB128 not only exhibits direct antimicrobial properties but also modulates inflammation and promotes the recruitment of immune cells to sites of infection. Furthermore, genetic variations in the DEFB128 gene have been associated with susceptibility to certain diseases, underlining its significance in human health. Recent advances in recombinant protein technology have enabled the production of DEFB128 in sufficient quantities for detailed study, facilitating investigations into its structure-function relationships and mechanisms of action. The exploration of DEFB128 as a therapeutic agent continues to be a promising area of research, with implications for developing new strategies to enhance innate immunity and address the growing challenge of infectious diseases. Overall, the multifaceted roles of DEFB128 in immune defense mechanisms and its potential for clinical application make it a compelling subject for ongoing scientific inquiry.











